|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
1-643 |
0e+00 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 1214.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 1 MYKLSDPFDYLNDNSYSNSNPEAFWDEVAKKNVFWEKMYDKVYSGDEIYPDWFKGGELNTCYNLLDIHIKNPAKRDQDAL 80
Cdd:PTZ00237 1 MYKLSDPFDYENDSNYANSNPESFWDEVAKKYVHWDKMYDKVYSGDEIYPDWFKGGELNTCYNVLDIHVKNPLKRDQDAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 81 IYECPYLKKTIKLTYYQLYEKVCKFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGYSVKSLIDRI 160
Cdd:PTZ00237 81 IYECPYLKKTIKLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 161 ETITPKLIITTNYGIFNDEIITFTPNLKEAIELSTFKPSNVITLFRNEVLDETKLKKVQNIPTIPNTLSWYDEIKKLKEN 240
Cdd:PTZ00237 161 ETITPKLIITTNYGILNDEIITFTPNLKEAIELSTFKPSNVITLFRNDITSESDLKKIETIPTIPNTLSWYDEIKKIKEN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 241 NQSPFYEYVPVESSHPLYILYTSGTTGNTKAVVRSNGPHMVGIKY-YTFRKESDIPQIVFSNANIGWVSFHGFFYGLLSG 319
Cdd:PTZ00237 241 NQSPFYEYVPVESSHPLYILYTSGTTGNSKAVVRSNGPHLVGLKYyWRSIIEKDIPTVVFSHSSIGWVSFHGFLYGSLSL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 320 GNTLVMYEGGIIKNEHIEDDLWIAIVKHKVTHTFPSPSVFRYLIKTDPEGTIVRSKYDLSNLKEIWCGGEVIEESIPEYI 399
Cdd:PTZ00237 321 GNTFVMFEGGIIKNKHIEDDLWNTIEKHKVTHTLTLPKTIRYLIKTDPEATIIRSKYDLSNLKEIWCGGEVIEESIPEYI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 400 EQKLKIKCLRVYGQSEIGVTSFISVHALNIPYRATGVPSIYIRPSILSEEGEVLNSNEIGLVAFKLPMPPSFAITFYKND 479
Cdd:PTZ00237 401 ENKLKIKSSRGYGQTEIGITYLYCYGHINIPYNATGVPSIFIKPSILSEDGKELNVNEIGEVAFKLPMPPSFATTFYKND 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 480 EKFKQLFTRFPGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGILSPDCRTAPIGI 559
Cdd:PTZ00237 481 EKFKQLFSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 560 LVLK---ENPSIDLNKLQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQILSNLLNDPNYQLPDDVNDSELFYK 636
Cdd:PTZ00237 561 LVLKqdqSNQSIDLNKLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQIISKFLNDSNYQLPDNVNDSEIFYK 640
|
....*..
gi 66822211 637 IKELYMK 643
Cdd:PTZ00237 641 IKELYMK 647
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
10-637 |
9.92e-170 |
|
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: 497.99 E-value: 9.92e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 10 YLNDNSYSNSNPEAFWDEVAKKnVFWEKMYDKVYSGDEI-YPDWFKGGELNTCYNLLDIHIKNPaKRDQDALIYECPYLK 88
Cdd:cd05967 1 YEEVYARSIAEPEAFWAEQARL-IDWFKPPEKILDNSNPpFTRWFVGGRLNTCYNALDRHVEAG-RGDQIALIYDSPVTG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 89 KTIKLTYYQLYEKVCKFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGYSVKSLIDRIETITPKLI 168
Cdd:cd05967 79 TERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKPKLI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 169 ITTNYGIFNDEIITFTPNLKEAIELSTFKPSNVITLFRNEVldETKLKKVQniptipNTLSWYDEIKklkennQSPFYEY 248
Cdd:cd05967 159 VTASCGIEPGKVVPYKPLLDKALELSGHKPHHVLVLNRPQV--PADLTKPG------RDLDWSELLA------KAEPVDC 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 249 VPVESSHPLYILYTSGTTGNTKAVVRSNGPHMVGIkYYTFRKESDIPQ--IVFSNANIGWVSFHGFF-YGLLSGGNTLVM 325
Cdd:cd05967 225 VPVAATDPLYILYTSGTTGKPKGVVRDNGGHAVAL-NWSMRNIYGIKPgdVWWAASDVGWVVGHSYIvYGPLLHGATTVL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 326 YEGgiiKNEHIED--DLWIAIVKHKVTHTFPSPSVFRYLIKTDPEGTIVRsKYDLSNLKEIWCGGEVIEESIPEYIEQKL 403
Cdd:cd05967 304 YEG---KPVGTPDpgAFWRVIEKYQVNALFTAPTAIRAIRKEDPDGKYIK-KYDLSSLRTLFLAGERLDPPTLEWAENTL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 404 KIKCLRVYGQSEIG---VTSFISVHALNIPYRATGVPSIYIRPSILSEEGEVLNSNEIGLVAFKLPMPPSFAITFYKNDE 480
Cdd:cd05967 380 GVPVIDHWWQTETGwpiTANPVGLEPLPIKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIKLPLPPGCLLTLWKNDE 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 481 KFKQL-FTRFPGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGILSPDCRTAPIGI 559
Cdd:cd05967 460 RFKKLyLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGL 539
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66822211 560 LVLKENPSIDLNKLQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQILSNLLNDPNYQLPDDVNDSELFYKI 637
Cdd:cd05967 540 VVLKEGVKITAEELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKIADGEDYTIPSTIEDPSVLDEI 617
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
52-613 |
1.78e-125 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 382.54 E-value: 1.78e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 52 WFKGGELNTCYNLLDIHIKnpAKRDQDALIYECPyLKKTIKLTYYQLYEKVCKFSRVLLNLNVSKNDNVLIFMANTLEPL 131
Cdd:COG0365 2 WFVGGRLNIAYNCLDRHAE--GRGDKVALIWEGE-DGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 132 IAMLSCARIGATQCTLFDGYSVKSLIDRIETITPKLIITTNYGIFNDEIITFTPNLKEAIELSTfKPSNVItlfrneVLD 211
Cdd:COG0365 79 IAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEALEELP-SLEHVI------VVG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 212 ETklkkvQNIPTIPNTLSWYDEIKklkenNQSPFYEYVPVESSHPLYILYTSGTTGNTKAVVRSNGPHMVGIkYYTFR-- 289
Cdd:COG0365 152 RT-----GADVPMEGDLDWDELLA-----AASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHA-ATTAKyv 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 290 ---KESDipqIVFSNANIGWVSFHG-FFYGLLSGGNTLVMYEGgiiKNEHIE-DDLWIAIVKHKVTHTFPSPSVFRYLIK 364
Cdd:COG0365 221 ldlKPGD---VFWCTADIGWATGHSyIVYGPLLNGATVVLYEG---RPDFPDpGRLWELIEKYGVTVFFTAPTAIRALMK 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 365 TDPEgtiVRSKYDLSNLKEIWCGGEVIEESIPEYIEQKLKIKCLRVYGQSEIGvTSFISvhalNIPYR-----ATGVPSI 439
Cdd:COG0365 295 AGDE---PLKKYDLSSLRLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTETG-GIFIS----NLPGLpvkpgSMGKPVP 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 440 YIRPSILSEEGEVLNSNEIGLVAFKLPMpPSFAITFYKNDEKFKQ-LFTRFPGYYDSGDLGYIDQRGFYTIVSRSDDQIK 518
Cdd:COG0365 367 GYDVAVVDEDGNPVPPGEEGELVIKGPW-PGMFRGYWNDPERYREtYFGRFPGWYRTGDGARRDEDGYFWILGRSDDVIN 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 519 ISCNKIQLNTIDTSILKHPSVLECCSIGILSPDCRTAPIGILVLKENPSIDlNKLQNEINNIITQDIESLAVLKKIIVIN 598
Cdd:COG0365 446 VSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPS-DELAKELQAHVREELGPYAYPREIEFVD 524
|
570
....*....|....*
gi 66822211 599 QLPKTKVGKIPRQIL 613
Cdd:COG0365 525 ELPKTRSGKIMRRLL 539
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
17-613 |
2.01e-113 |
|
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: 352.63 E-value: 2.01e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 17 SNSNPEAFWDEVAKKnVFWEKMYDKV--YSGDEIYPDWFKGGELNTCYNLLDIHIKNpaKRDQDALIYECPYLKKTIKLT 94
Cdd:cd05966 10 SIEDPEEFWGEIAKE-LDWFKPWDKVldWSKGPPFIKWFEGGKLNISYNCLDRHLKE--RGDKVAIIWEGDEPDQSRTIT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 95 YYQLYEKVCKFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGYSVKSLIDRIETITPKLIITTNYG 174
Cdd:cd05966 87 YRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRINDAQCKLVITADGG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 175 IFNDEIITFTPNLKEAIELsTFKPSNVITLFRNEvlDETKLKKVQNIptipntlsWYDEIKKlkenNQSPFYEYVPVESS 254
Cdd:cd05966 167 YRGGKVIPLKEIVDEALEK-CPSVEKVLVVKRTG--GEVPMTEGRDL--------WWHDLMA----KQSPECEPEWMDSE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 255 HPLYILYTSGTTGNTKAVVRSNGPHMVGIkYYTFR-----KESDipqIVFSNANIGWVSFHGFF-YGLLSGGNTLVMYEG 328
Cdd:cd05966 232 DPLFILYTSGSTGKPKGVVHTTGGYLLYA-ATTFKyvfdyHPDD---IYWCTADIGWITGHSYIvYGPLANGATTVMFEG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 329 giIKNEHIEDDLWIAIVKHKVTHTFPSPSVFRYLIKtdpEGTIVRSKYDLSNLKEIWCGGEVIEesiPE----YIEQKLK 404
Cdd:cd05966 308 --TPTYPDPGRYWDIVEKHKVTIFYTAPTAIRALMK---FGDEWVKKHDLSSLRVLGSVGEPIN---PEawmwYYEVIGK 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 405 IKCLRV--YGQSEIG---VTSFISVHALNiPYRATgVPSIYIRPSILSEEGEVLNSNEIGLVAFKLPMpPSFAITFYKND 479
Cdd:cd05966 380 ERCPIVdtWWQTETGgimITPLPGATPLK-PGSAT-RPFFGIEPAILDEEGNEVEGEVEGYLVIKRPW-PGMARTIYGDH 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 480 EKFKQL-FTRFPGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGIlsPDCRT--AP 556
Cdd:cd05966 457 ERYEDTyFSKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGR--PHDIKgeAI 534
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 66822211 557 IGILVLKENPSIDlNKLQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:cd05966 535 YAFVTLKDGEEPS-DELRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRIL 590
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
17-608 |
3.00e-105 |
|
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: 331.08 E-value: 3.00e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 17 SNSNPEAFWDEvAKKNVFWEKMYDKV----YSGDEIYPDWFKGGELNTCYNLLDIHIKNpaKRDQDALIYECPYLKKTIK 92
Cdd:cd17634 8 SINDPDTFWGE-AGKILDWITPYQKVkntsFAPGAPSIKWFEDATLNLAANALDRHLRE--NGDRTAIIYEGDDTSQSRT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 93 LTYYQLYEKVCKFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGYSVKSLIDRIETITPKLIITTN 172
Cdd:cd17634 85 ISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITAD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 173 YGIFNDEIITFTPNLKEAIELSTFKPSNVITLFRNEVldetklkkvqNIPTIPNTLSWYDEIKKlkenNQSPFYEYVPVE 252
Cdd:cd17634 165 GGVRAGRSVPLKKNVDDALNPNVTSVEHVIVLKRTGS----------DIDWQEGRDLWWRDLIA----KASPEHQPEAMN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 253 SSHPLYILYTSGTTGNTKAVVRSNGPHMVGIKyYTFRKESDI--PQIVFSNANIGWVSFHGFF-YGLLSGGNTLVMYEGg 329
Cdd:cd17634 231 AEDPLFILYTSGTTGKPKGVLHTTGGYLVYAA-TTMKYVFDYgpGDIYWCTADVGWVTGHSYLlYGPLACGATTLLYEG- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 330 iIKNEHIEDDLWIAIVKHKVTHTFPSPSVFRYLIKTDPEGTivrSKYDLSNLKEIWCGGEVIE-ESIPEYIEQKLKIKCL 408
Cdd:cd17634 309 -VPNWPTPARMWQVVDKHGVNILYTAPTAIRALMAAGDDAI---EGTDRSSLRILGSVGEPINpEAYEWYWKKIGKEKCP 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 409 RV--YGQSEIGvTSFISVHALNIPYRA--TGVPSIYIRPSILSEEGEVLNSNEIGLVAFKLPMPPSfAITFYKNDEKFKQ 484
Cdd:cd17634 385 VVdtWWQTETG-GFMITPLPGAIELKAgsATRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPWPGQ-TRTLFGDHERFEQ 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 485 -LFTRFPGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGILSPDCRTAPIGILVLK 563
Cdd:cd17634 463 tYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLN 542
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 66822211 564 ENpSIDLNKLQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKI 608
Cdd:cd17634 543 HG-VEPSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
16-610 |
6.25e-102 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 323.44 E-value: 6.25e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 16 YSNSNPEAFWDEVAKKnVFWEKMYDKV--YSgDEIYPDWFKGGELNTCYNLLDIHIknPAKRDQDALIYECPYLKKTIKL 93
Cdd:PRK10524 10 RSIDDPEAFWAEQARR-IDWQTPFTQVldYS-NPPFARWFVGGRTNLCHNAVDRHL--AKRPEQLALIAVSTETDEERTY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 94 TYYQLYEKVCKFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGYSVKSLIDRIETITPKLIITTNY 173
Cdd:PRK10524 86 TFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAARIDDAKPVLIVSADA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 174 GIFNDEIITFTPNLKEAIELSTFKPSNVITLFRNevLDEtklkkvqnIPTIPNTLSWYDEIKKLKENNQspfyeyVPV-- 251
Cdd:PRK10524 166 GSRGGKVVPYKPLLDEAIALAQHKPRHVLLVDRG--LAP--------MARVAGRDVDYATLRAQHLGAR------VPVew 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 252 -ESSHPLYILYTSGTTGNTKAVVRSNGPHMVGIKY---YTFRKESdiPQIVFSNANIGWVSFHGFF-YGLLSGGNTLVMY 326
Cdd:PRK10524 230 lESNEPSYILYTSGTTGKPKGVQRDTGGYAVALATsmdTIFGGKA--GETFFCASDIGWVVGHSYIvYAPLLAGMATIMY 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 327 EG-------GIiknehieddlWIAIV-KHKVTHTFPSPSVFRYLIKTDPEgtiVRSKYDLSNLKEIWCGGEVIEESIPEY 398
Cdd:PRK10524 308 EGlptrpdaGI----------WWRIVeKYKVNRMFSAPTAIRVLKKQDPA---LLRKHDLSSLRALFLAGEPLDEPTASW 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 399 IEQKLKIKCLRVYGQSEIG---VTSFISVHALNIPYRATGVPSIYIRPSILSEE-GEVLNSNEIGLVAFKLPMPPSFAIT 474
Cdd:PRK10524 375 ISEALGVPVIDNYWQTETGwpiLAIARGVEDRPTRLGSPGVPMYGYNVKLLNEVtGEPCGPNEKGVLVIEGPLPPGCMQT 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 475 FYKNDEKF-KQLFTRF-PGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGILSPDC 552
Cdd:PRK10524 455 VWGDDDRFvKTYWSLFgRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALK 534
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66822211 553 RTAPIGILVLKENPSID----LNKLQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPR 610
Cdd:PRK10524 535 GQVAVAFVVPKDSDSLAdreaRLALEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLR 596
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
17-613 |
3.34e-95 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 305.91 E-value: 3.34e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 17 SNSNPEAFWDEVAKKnVFWEKMYDKVYSGDEIYPDWFKGGELNTCYNLLDIHIKNpaKRDQDALIYECPYLKKTIKLTYY 96
Cdd:PRK00174 26 SVEDPEGFWAEQAKR-LDWFKPFDTVLDWNAPFIKWFEDGELNVSYNCLDRHLKT--RGDKVAIIWEGDDPGDSRKITYR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 97 QLYEKVCKFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGYSVKSLIDRIETITPKLIITTNYGIF 176
Cdd:PRK00174 103 ELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVVFGGFSAEALADRIIDAGAKLVITADEGVR 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 177 NDEIITFTPNLKEAIELStfkPS--NVITLFRNEvldetklkkvQNIPTIPNTLSWYDEIKKlkenNQSPFYEYVPVESS 254
Cdd:PRK00174 183 GGKPIPLKANVDEALANC---PSveKVIVVRRTG----------GDVDWVEGRDLWWHELVA----GASDECEPEPMDAE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 255 HPLYILYTSGTTGNTKAVVRSNGPHMVGIkYYTFR-----KESDipqIVFSNANIGWVSFHGFF-YGLLSGGNTLVMYEG 328
Cdd:PRK00174 246 DPLFILYTSGSTGKPKGVLHTTGGYLVYA-AMTMKyvfdyKDGD---VYWCTADVGWVTGHSYIvYGPLANGATTLMFEG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 329 giIKNEHIEDDLWIAIVKHKVTHTFPSPSVFRYLIKtdpEGTIVRSKYDLSNLKEIWCGGEVIEesiPE----YIEQKLK 404
Cdd:PRK00174 322 --VPNYPDPGRFWEVIDKHKVTIFYTAPTAIRALMK---EGDEHPKKYDLSSLRLLGSVGEPIN---PEawewYYKVVGG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 405 IKCLRV--YGQSEIG---VTSFISVHALNiPYRATgVPSIYIRPSILSEEGEVLNSNEIGLVAFKLPMpPSFAITFYKND 479
Cdd:PRK00174 394 ERCPIVdtWWQTETGgimITPLPGATPLK-PGSAT-RPLPGIQPAVVDEEGNPLEGGEGGNLVIKDPW-PGMMRTIYGDH 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 480 EKFKQ-LFTRFPGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGIlsPDCRT--AP 556
Cdd:PRK00174 471 ERFVKtYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGR--PDDIKgqGI 548
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 66822211 557 IGILVLK--ENPSIDLNKlqnEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:PRK00174 549 YAFVTLKggEEPSDELRK---ELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRIL 604
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
255-608 |
5.52e-77 |
|
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: 248.74 E-value: 5.52e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 255 HPLYILYTSGTTGNTKAVVRSNGPHMVGIKYYTFRKESDIPQIVFSNANIGWVSFHGFFYGLLSGGNTLVMYEGGIIkne 334
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDP--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 335 hieDDLWIAIVKHKVTHTFPSPSVFRYLIKTDPegtivRSKYDLSNLKEIWCGGEVIEESIPEYIEQKLKIKCLRVYGQS 414
Cdd:cd04433 78 ---EAALELIEREKVTILLGVPTLLARLLKAPE-----SAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 415 EIG-VTSFISVHALNIPYRATGVPSIYIRPSILSEEGEVLNSNEIGLVAFKLPMPPSFaitfYKNDEKFKQLFTRfPGYY 493
Cdd:cd04433 150 ETGgTVATGPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKG----YWNNPEATAAVDE-DGWY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 494 DSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGILSPDCRTAPIGILVLKENPSIDLnkl 573
Cdd:cd04433 225 RTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDA--- 301
|
330 340 350
....*....|....*....|....*....|....*
gi 66822211 574 qNEINNIITQDIESLAVLKKIIVINQLPKTKVGKI 608
Cdd:cd04433 302 -EELRAHVRERLAPYKVPRRVVFVDALPRTASGKI 335
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
9-613 |
7.49e-64 |
|
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: 221.98 E-value: 7.49e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 9 DYLNDNSYSNSNPEAFWDEVAKKNVF-WEKMYDKV--YSGDEIYPDWFKGGELNTCYNLLDIHIKNpaKRDQDALIYECP 85
Cdd:cd05968 8 DLEAFLERSAEDNAWFWGEFVKDVGIeWYEPPYQTldLSGGKPWAAWFVGGRMNIVEQLLDKWLAD--TRTRPALRWEGE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 86 ylKKTIK-LTYYQLYEKVCKFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGYSVKSLIDRIETIT 164
Cdd:cd05968 86 --DGTSRtLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 165 PKLIITTNYGIFNDEIITFTPNLKEAIElSTFKPSNVItlfrneVLDETKLkkvqNIPTIPNTLSWYDEIKKlkennqSP 244
Cdd:cd05968 164 AKALITADGFTRRGREVNLKEEADKACA-QCPTVEKVV------VVRHLGN----DFTPAKGRDLSYDEEKE------TA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 245 FYEYVPVESSHPLYILYTSGTTGNTKAVVRSngpHM-VGIK-----YYTFR-KESDIpqiVFSNANIGWVSFHGFFYGLL 317
Cdd:cd05968 227 GDGAERTESEDPLMIIYTSGTTGKPKGTVHV---HAgFPLKaaqdmYFQFDlKPGDL---LTWFTDLGWMMGPWLIFGGL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 318 SGGNTLVMYEGgiIKNEHIEDDLWIAIVKHKVTHTFPSPSVFRYLIktdPEGTIVRSKYDLSNLKEIWCGGEVIE-ESIP 396
Cdd:cd05968 301 ILGATMVLYDG--APDHPKADRLWRMVEDHEITHLGLSPTLIRALK---PRGDAPVNAHDLSSLRVLGSTGEPWNpEPWN 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 397 EYIEQKLKIKC--LRVYGQSEIGVTSFISVHALNIPYRATGVPSIYIRPSILSEEGEVLnSNEIGLVAFKLPMPpSFAIT 474
Cdd:cd05968 376 WLFETVGKGRNpiINYSGGTEISGGILGNVLIKPIKPSSFNGPVPGMKADVLDESGKPA-RPEVGELVLLAPWP-GMTRG 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 475 FYKNDEKF-KQLFTRFPGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGILSPDCR 553
Cdd:cd05968 454 FWRDEDRYlETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKG 533
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 554 TAPIGILVLKENPSiDLNKLQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:cd05968 534 EAIVCFVVLKPGVT-PTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVI 592
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
4-613 |
2.47e-62 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 219.00 E-value: 2.47e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 4 LSDPFDYLNDNSYSNSNPEAFWDEVAKKnVFWEKMY--DKVYSGD------EIYPDWFKGGELNTCYNLLDIHIKNpAKR 75
Cdd:PLN02654 26 VSSPQQYMEMYKRSVDDPAGFWSDIASQ-FYWKQKWegDEVCSENldvrkgPISIEWFKGGKTNICYNCLDRNVEA-GNG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 76 DQDALIYECPYLKKTIKLTYYQLYEKVCKFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGYSVKS 155
Cdd:PLN02654 104 DKIAIYWEGNEPGFDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAES 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 156 LIDRIETITPKLIITTNYGIFNDEIItftpNLKEAIELStfkpsnvitlfrnevLDETKLK--KVQNIPTIPNTLSWYDE 233
Cdd:PLN02654 184 LAQRIVDCKPKVVITCNAVKRGPKTI----NLKDIVDAA---------------LDESAKNgvSVGICLTYENQLAMKRE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 234 IKKLKENNQSPFYEYVP----------VESSHPLYILYTSGTTGNTKAVVRSNGPHMV----GIKYYTFRKESDipqIVF 299
Cdd:PLN02654 245 DTKWQEGRDVWWQDVVPnyptkcevewVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVytatTFKYAFDYKPTD---VYW 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 300 SNANIGWVSFHGFF-YGLLSGGNTLVMYEGgiIKNEHIEDDLWIAIVKHKVTHTFPSPSVFRYLIKtdpEGTIVRSKYDL 378
Cdd:PLN02654 322 CTADCGWITGHSYVtYGPMLNGATVLVFEG--APNYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMR---DGDEYVTRHSR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 379 SNLKEIWCGGEVIEESIPEYI-----EQKLKIKclRVYGQSEIG---VTSFISVHALNiPYRATgVPSIYIRPSILSEEG 450
Cdd:PLN02654 397 KSLRVLGSVGEPINPSAWRWFfnvvgDSRCPIS--DTWWQTETGgfmITPLPGAWPQK-PGSAT-FPFFGVQPVIVDEKG 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 451 EVLNSNEIGLVAFKLPMPPSFAiTFYKNDEKFK-QLFTRFPGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTI 529
Cdd:PLN02654 473 KEIEGECSGYLCVKKSWPGAFR-TLYGDHERYEtTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEV 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 530 DTSILKHPSVLECCSIGIlspDCRTAPIGI-----LVLKENPSIDLNKlqnEINNIITQDIESLAVLKKIIVINQLPKTK 604
Cdd:PLN02654 552 ESALVSHPQCAEAAVVGI---EHEVKGQGIyafvtLVEGVPYSEELRK---SLILTVRNQIGAFAAPDKIHWAPGLPKTR 625
|
....*....
gi 66822211 605 VGKIPRQIL 613
Cdd:PLN02654 626 SGKIMRRIL 634
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
91-520 |
1.96e-58 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 202.16 E-value: 1.96e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 91 IKLTYYQLYEKVCKFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGYSVKSLIDRIETITPKLIIT 170
Cdd:pfam00501 20 RRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAKVLIT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 171 tnygifnDEIITFTPNLKEAIELstFKPSNVITLFRNEVLDEtklkkvqniptipntlswyDEIKKLKENNQSPFYEYVP 250
Cdd:pfam00501 100 -------DDALKLEELLEALGKL--EVVKLVLVLDRDPVLKE-------------------EPLPEEAKPADVPPPPPPP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 251 VESSHPLYILYTSGTTGNTKAVVRSngpH------MVGIKYYTFRKESDIPQIVFSN-ANIGWV-SFHGFFYGLLSGGNT 322
Cdd:pfam00501 152 PDPDDLAYIIYTSGTTGKPKGVMLT---HrnlvanVLSIKRVRPRGFGLGPDDRVLStLPLFHDfGLSLGLLGPLLAGAT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 323 LVMYEGGiikNEHIEDDLWIAIVKHKVTHTFPSPSVFRYLIKTDPEgtivrSKYDLSNLKEIWCGGEVIEESIPEYIEQK 402
Cdd:pfam00501 229 VVLPPGF---PALDPAALLELIERYKVTVLYGVPTLLNMLLEAGAP-----KRALLSSLRLVLSGGAPLPPELARRFREL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 403 LKIKCLRVYGQSEigvTSFISVHALNIPYRATGVPSI-----YIRPSILSEE-GEVLNSNEIGLVAFKlpmPPSFAITFY 476
Cdd:pfam00501 301 FGGALVNGYGLTE---TTGVVTTPLPLDEDLRSLGSVgrplpGTEVKIVDDEtGEPVPPGEPGELCVR---GPGVMKGYL 374
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 66822211 477 KNDEKFKQLFTRfPGYYDSGDLGYIDQRGFYTIVSRSDDQIKIS 520
Cdd:pfam00501 375 NDPELTAEAFDE-DGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
93-613 |
6.94e-54 |
|
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: 190.79 E-value: 6.94e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 93 LTYYQLYEKVCKFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGYSVKSLIDRIETITPKLIITTn 172
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITT- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 173 ygifndeiitftPNLKEAIELSTfkpsnvitlfrnevldetklkkvqniptipntlswydeikklkennqspfyeyvpve 252
Cdd:cd05969 80 ------------EELYERTDPED--------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 253 sshPLYILYTSGTTGNTKAVVRSngpHMVGIKYY-TFRKESDI-PQIVF-SNANIGWVSfhGFFYGLLS---GGNTLVMY 326
Cdd:cd05969 91 ---PTLLHYTSGTTGTPKGVLHV---HDAMIFYYfTGKYVLDLhPDDIYwCTADPGWVT--GTVYGIWApwlNGVTNVVY 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 327 EGgiikneHIEDDLWIAIVK-HKVTHTFPSPSVFRYLIKtdpEGTIVRSKYDLSNLKEIWCGGEVIEESIPEYIEQKLKI 405
Cdd:cd05969 163 EG------RFDAESWYGIIErVKVTVWYTAPTAIRMLMK---EGDELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGV 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 406 KCLRVYGQSEIGVTSFISVHALNIPYRATGVPSIYIRPSILSEEGEVLNSNEIGLVAFKlPMPPSFAITFYKNDEKFKQL 485
Cdd:cd05969 234 PIHDTWWQTETGSIMIANYPCMPIKPGSMGKPLPGVKAAVVDENGNELPPGTKGILALK-PGWPSMFRGIWNDEERYKNS 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 486 FTRfpGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGILSPDCRTAPIGILVLKEN 565
Cdd:cd05969 313 FID--GWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEG 390
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 66822211 566 --PSidlNKLQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:cd05969 391 fePS---DELKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVL 437
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
76-613 |
4.72e-50 |
|
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: 180.39 E-value: 4.72e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 76 DQDALIYEcpylkkTIKLTYYQLYEKVCKFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGYSVKS 155
Cdd:COG0318 14 DRPALVFG------GRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 156 LIDRIETITPKLIITtnygifndeiitftpnlkeaielstfkpsnvitlfrnevldetklkkvqniptipntlswydeik 235
Cdd:COG0318 88 LAYILEDSGARALVT----------------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 236 klkennqspfyeyvpvesshpLYILYTSGTTGNTKAVVRSNG----PHMVGIKYYTFRKESdipqiVFsnanIGWVS-FH 310
Cdd:COG0318 103 ---------------------ALILYTSGTTGRPKGVMLTHRnllaNAAAIAAALGLTPGD-----VV----LVALPlFH 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 311 GF------FYGLLSGGnTLVMYEggiikNEHIEdDLWIAIVKHKVTHTFPSPSVFRYLIKTDPegtivRSKYDLSNLKEI 384
Cdd:COG0318 153 VFgltvglLAPLLAGA-TLVLLP-----RFDPE-RVLELIERERVTVLFGVPTMLARLLRHPE-----FARYDLSSLRLV 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 385 WCGGEVIEESIPEYIEQKLKIKCLRVYGQSEIGVTSFISVHALNIPYRAT-GVPSIYIRPSILSEEGEVLNSNEIGLVAF 463
Cdd:COG0318 221 VSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPEDPGERRPGSvGRPLPGVEVRIVDEDGRELPPGEVGEIVV 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 464 KlpmPPSFAITFYKNDEKFKQLFTrfPGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECC 543
Cdd:COG0318 301 R---GPNVMKGYWNDPEATAEAFR--DGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAA 375
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 544 SIGILSPDCRTAPIGILVLKENPSIDLNKLQNEINNIITqdieSLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:COG0318 376 VVGVPDEKWGERVVAFVVLRPGAELDAEELRAFLRERLA----RYKVPRRVEFVDELPRTASGKIDRRAL 441
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
93-613 |
1.59e-44 |
|
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: 164.43 E-value: 1.59e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 93 LTYYQLYEKVCKFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGYSVKSLIDRIETITPKLIITtn 172
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 173 ygifndeiitftpnlkeaielstfkpsnvitlfrnevldetklkkvqniptipntlswydeikklkennqspfyeyvpvE 252
Cdd:cd05972 79 -------------------------------------------------------------------------------D 79
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 253 SSHPLYILYTSGTTGNTKAVVRSNG---PHMVGIKYYTFRKESDIpqiVFSNANIGWVSFHGF-FYGLLSGGNTLVMYEG 328
Cdd:cd05972 80 AEDPALIYFTSGTTGLPKGVLHTHSyplGHIPTAAYWLGLRPDDI---HWNIADPGWAKGAWSsFFGPWLLGATVFVYEG 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 329 GIIKNEHIEDDLwiaiVKHKVTHTFPSPSVFRYLIKTDPEGtivrskYDLSNLKEIWCGGEVIEESIPEYIEQKLKIKCL 408
Cdd:cd05972 157 PRFDAERILELL----ERYGVTSFCGPPTAYRMLIKQDLSS------YKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIR 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 409 RVYGQSEIGVTsFISVHALNIPYRATGVPSIYIRPSILSEEGEVLNSNEIGLVAFKLPmPPSFAITFYKNDEKFKQLFTR 488
Cdd:cd05972 227 DGYGQTETGLT-VGNFPDMPVKPGSMGRPTPGYDVAIIDDDGRELPPGEEGDIAIKLP-PPGLFLGYVGDPEKTEASIRG 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 489 fpGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGilSPD-CRTAPIGILVLKENPS 567
Cdd:cd05972 305 --DYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVG--SPDpVRGEVVKAFVVLTSGY 380
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 66822211 568 IDLNKLQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:cd05972 381 EPSEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVEL 426
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
16-608 |
1.87e-44 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 168.22 E-value: 1.87e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 16 YSNSNPEAFWDEVAK-KNVFWEKMYDKVYSGDEIYPD--WFKGGELNTCYNLLdihikNPAKRDQDALIYEcpYLKKTI- 91
Cdd:cd05943 25 WSVDDPGAFWAAVWDfSGVRGSKPYDVVVVSGRIMPGarWFPGARLNYAENLL-----RHADADDPAAIYA--AEDGERt 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 92 KLTYYQLYEKVCKFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGYSVKSLIDRIETITPKLIITT 171
Cdd:cd05943 98 EVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPGVLDRFGQIEPKVLFAV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 172 NYGIFND----------EIITFTPNLKEAIelstfkpsnvitlfrneVLDETKLKKVQNIPTIPNTLSWYDEIkkLKENN 241
Cdd:cd05943 178 DAYTYNGkrhdvrekvaELVKGLPSLLAVV-----------------VVPYTVAAGQPDLSKIAKALTLEDFL--ATGAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 242 QSPFYEYVPVesSHPLYILYTSGTTGNTKAVVRSNG----PHMvgikyytfrKE----SDIP--QIVFSNANIGWVSFHG 311
Cdd:cd05943 239 GELEFEPLPF--DHPLYILYSSGTTGLPKCIVHGAGgtllQHL---------KEhilhCDLRpgDRLFYYTTCGWMMWNW 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 312 FFYGLLSGGnTLVMYEGG-IIKNEHIeddLWIAIVKHKVTHTFPSPSVFRYLIKTdpeGTIVRSKYDLSNLKEIWCGGEV 390
Cdd:cd05943 308 LVSGLAVGA-TIVLYDGSpFYPDTNA---LWDLADEEGITVFGTSAKYLDALEKA---GLKPAETHDLSSLRTILSTGSP 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 391 IEESIPEYIEQKLKikcLRVYGQSEIGVTSFISVHALnipyratGVPSIYIRPS------------ILSEEGEVLnSNEI 458
Cdd:cd05943 381 LKPESFDYVYDHIK---PDVLLASISGGTDIISCFVG-------GNPLLPVYRGeiqcrglgmaveAFDEEGKPV-WGEK 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 459 G-LVAFKlPMpPSFAITFYkNDE---KFKQ-LFTRFPGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSI 533
Cdd:cd05943 450 GeLVCTK-PF-PSMPVGFW-NDPdgsRYRAaYFAKYPGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVV 526
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66822211 534 LKHPSVLECCSIGILSPDCRTAPIGILVLKENPSIDlNKLQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKI 608
Cdd:cd05943 527 EKIPEVEDSLVVGQEWKDGDERVILFVKLREGVELD-DELRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKK 600
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
39-613 |
3.55e-43 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 163.53 E-value: 3.55e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 39 YDKVYSG---DEI--YPDWFKGGELNTCYNLLDIHIKNPaKRDQDALIYECPYLKKTIklTYYQLYEKVCKFSRVLLNLN 113
Cdd:PRK04319 18 YEETYATfswEEVekEFSWLETGKVNIAYEAIDRHADGG-RKDKVALRYLDASRKEKY--TYKELKELSNKFANVLKELG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 114 VSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGYSVKSLIDRIETITPKLIITTNygifndeiitftpnlkeaiel 193
Cdd:PRK04319 95 VEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTP--------------------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 194 stfkpsnviTLFRNEVLDET-KLKKV----QNIPTIPNTLSWYDEIkklkeNNQSPFYEYVPVESSHPLYILYTSGTTGN 268
Cdd:PRK04319 154 ---------ALLERKPADDLpSLKHVllvgEDVEEGPGTLDFNALM-----EQASDEFDIEWTDREDGAILHYTSGSTGK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 269 TKAVVRSNGP---HMVGIKYYTFRKESDIpqiVFSNANIGWVSfhGFFYGL---LSGGNTLVMYEGgiiknEHIEDDLWI 342
Cdd:PRK04319 220 PKGVLHVHNAmlqHYQTGKYVLDLHEDDV---YWCTADPGWVT--GTSYGIfapWLNGATNVIDGG-----RFSPERWYR 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 343 AIVKHKVTHTFPSPSVFRYLIKTDPEgtiVRSKYDLSNLKEIWCGGEVIEesiPEYIEQKLKIKCLRV---YGQSEIGVT 419
Cdd:PRK04319 290 ILEDYKVTVWYTAPTAIRMLMGAGDD---LVKKYDLSSLRHILSVGEPLN---PEVVRWGMKVFGLPIhdnWWMTETGGI 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 420 SFISVHALNIPYRATGVPSIYIRPSILSEEGEVLNSNEIGLVAFKLPMPPSFAiTFYKNDEKFKQLFtrFPGYYDSGDLG 499
Cdd:PRK04319 364 MIANYPAMDIKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAIKKGWPSMMR-GIWNNPEKYESYF--AGDWYVSGDSA 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 500 YIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGIlsPDCRTAPI--GILVLKEN--PSidlNKLQN 575
Cdd:PRK04319 441 YMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGK--PDPVRGEIikAFVALRPGyePS---EELKE 515
|
570 580 590
....*....|....*....|....*....|....*...
gi 66822211 576 EINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:PRK04319 516 EIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVL 553
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
92-608 |
1.34e-41 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 157.76 E-value: 1.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 92 KLTYYQLYEKVCKFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGYSVKSLIDRIETITPKLIITT 171
Cdd:cd05911 10 ELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 172 NYGIfndeiitftPNLKEAIELSTFKPsNVITLfrnevldETKLKKVQNIPTIpntLSWYDEIKKlkennqsPFYEYVPV 251
Cdd:cd05911 90 PDGL---------EKVKEAAKELGPKD-KIIVL-------DDKPDGVLSIEDL---LSPTLGEED-------EDLPPPLK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 252 ES-SHPLYILYTSGTTGNTKAVVRSngpHMVGI----KYYTFRKESDIPQIVFsnanIGWVSFH---GFFYGLLS---GG 320
Cdd:cd05911 143 DGkDDTAAILYSSGTTGLPKGVCLS---HRNLIanlsQVQTFLYGNDGSNDVI----LGFLPLYhiyGLFTTLASllnGA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 321 NTLVMYEGgiiknehiEDDLWIAIV-KHKVTHTFPSPSVFRYLIKtDPEgtivRSKYDLSNLKEIWCGGEVIEESIPEYI 399
Cdd:cd05911 216 TVIIMPKF--------DSELFLDLIeKYKITFLYLVPPIAAALAK-SPL----LDKYDLSSLRVILSGGAPLSKELQELL 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 400 EQKLKIKCLRV-YGQSEIGVTSFISVHALNIPyRATG--VPSIYIRpsILSEEG-EVLNSNEIGLVAFKLP--MPPsfai 473
Cdd:cd05911 283 AKRFPNATIKQgYGMTETGGILTVNPDGDDKP-GSVGrlLPNVEAK--IVDDDGkDSLGPNEPGEICVRGPqvMKG---- 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 474 tFYKNDEKFKQLFTRfPGYYDSGDLGYIDQRGFYTIVSRSDDQIKisCNKIQL--NTIDTSILKHPSVLECCSIGILSPD 551
Cdd:cd05911 356 -YYNNPEATKETFDE-DGWLHTGDIGYFDEDGYLYIVDRKKELIK--YKGFQVapAELEAVLLEHPGVADAAVIGIPDEV 431
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66822211 552 CRTAPIGILVLKENPSIDLNKLQNEINniitqdiESLAVLKK----IIVINQLPKTKVGKI 608
Cdd:cd05911 432 SGELPRAYVVRKPGEKLTEKEVKDYVA-------KKVASYKQlrggVVFVDEIPKSASGKI 485
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
92-613 |
8.96e-36 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 141.48 E-value: 8.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 92 KLTYYQLYEKVCKFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGAtqctlfdgysvkslidrietitpkLIITT 171
Cdd:PRK06187 31 RTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGA------------------------VLHPI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 172 NYGIFNDEIiTFTPNLKEAielstfkpsnVITLFRNEVLDETKlkkvQNIPTIPNTLSWY-----DEIKKLKEN------ 240
Cdd:PRK06187 87 NIRLKPEEI-AYILNDAED----------RVVLVDSEFVPLLA----AILPQLPTVRTVIvegdgPAAPLAPEVgeyeel 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 241 --NQSPFYEYVPVESSHPLYILYTSGTTGNTKAVvrsngphmvgikYYTFRkesdipQIV----FSNANIGWVS------ 308
Cdd:PRK06187 152 laAASDTFDFPDIDENDAAAMLYTSGTTGHPKGV------------VLSHR------NLFlhslAVCAWLKLSRddvylv 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 309 ----FH----GFFY-GLLSGGNtlvmyegGIIKNEHIEDDLWIAIVKHKVTHTFPSPSVFRYLIKtDPEgtivRSKYDLS 379
Cdd:PRK06187 214 ivpmFHvhawGLPYlALMAGAK-------QVIPRRFDPENLLDLIETERVTFFFAVPTIWQMLLK-APR----AYFVDFS 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 380 NLKEIWCGGEVIEESIPEYIEQKLKIKCLRVYGQSE---IGVTSFISVHALN-IPYR-ATG--VPSIYIRpsILSEEGEV 452
Cdd:PRK06187 282 SLRLVIYGGAALPPALLREFKEKFGIDLVQGYGMTEtspVVSVLPPEDQLPGqWTKRrSAGrpLPGVEAR--IVDDDGDE 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 453 L--NSNEIGLVAFKlpmPPSFAITFYKNDEKFKQLFTrfPGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTID 530
Cdd:PRK06187 360 LppDGGEVGEIIVR---GPWLMQGYWNRPEATAETID--GGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELE 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 531 TSILKHPSVLECCSIGIlsPDCRT--APIGILVLKENPSIDlnklQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKI 608
Cdd:PRK06187 435 DALYGHPAVAEVAVIGV--PDEKWgeRPVAVVVLKPGATLD----AKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKI 508
|
....*
gi 66822211 609 PRQIL 613
Cdd:PRK06187 509 LKRVL 513
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
59-610 |
9.83e-35 |
|
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: 138.78 E-value: 9.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 59 NTCYNLLDIHIKNpaKRDQDALIYeCPYLKKTIKLTYYQLYEKVCKFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCA 138
Cdd:cd05970 17 NFAYDVVDAMAKE--YPDKLALVW-CDDAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 139 RIGATQCTLFDGYSVKSLIDRIETITPKLIITTNYGIFNDEIitftpnlKEAIELSTfkpsnvitlfrnevldeTKLKKV 218
Cdd:cd05970 94 KLGAIAIPATHQLTAKDIVYRIESADIKMIVAIAEDNIPEEI-------EKAAPECP-----------------SKPKLV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 219 QNIPTIPNtlSWYDEIKKLKenNQSPFYEYVPVESSH----PLYILYTSGTTGNTKAVVRSNG-P--HMVGIKYYTFRKE 291
Cdd:cd05970 150 WVGDPVPE--GWIDFRKLIK--NASPDFERPTANSYPcgedILLVYFSSGTTGMPKMVEHDFTyPlgHIVTAKYWQNVRE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 292 SDIPQIVfsnANIGWV-SFHGFFYGLLSGGNTLVMYEGGIIKNEHIEDdlwiAIVKHKVTHTFPSPSVFRYLIKTDpegt 370
Cdd:cd05970 226 GGLHLTV---ADTGWGkAVWGKIYGQWIAGAAVFVYDYDKFDPKALLE----KLSKYGVTTFCAPPTIYRFLIRED---- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 371 ivRSKYDLSNLKEIWCGGEVIEESIPEYIEQKLKIKCLRVYGQSEIGVTsFISVHALNIPYRATGVPSIYIRPSILSEEG 450
Cdd:cd05970 295 --LSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETTLT-IATFPWMEPKPGSMGKPAPGYEIDLIDREG 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 451 EVLNSNEIGLVAFKLP--MPPSFAITFYKNDEKFKQLFtrFPGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNT 528
Cdd:cd05970 372 RSCEAGEEGEIVIRTSkgKPVGLFGGYYKDAEKTAEVW--HDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFE 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 529 IDTSILKHPSVLECCSIGIlsPDcrtaPIGILVLKenPSIDLNK-------LQNEINNIITQDIESLAVLKKIIVINQLP 601
Cdd:cd05970 450 VESALIQHPAVLECAVTGV--PD----PIRGQVVK--ATIVLAKgyepseeLKKELQDHVKKVTAPYKYPRIVEFVDELP 521
|
....*....
gi 66822211 602 KTKVGKIPR 610
Cdd:cd05970 522 KTISGKIRR 530
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
252-613 |
7.18e-33 |
|
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: 131.79 E-value: 7.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 252 ESSHPLYILYTSGTTGNTKAVVRSN----GpHMVGIKYY--TFRKESDIpqiVFSNANIGWVSfhGFFYGLLSG---GNT 322
Cdd:cd05971 86 GSDDPALIIYTSGTTGPPKGALHAHrvllG-HLPGVQFPfnLFPRDGDL---YWTPADWAWIG--GLLDVLLPSlyfGVP 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 323 LVMYeggiiKNEHIEDDLWIAIVK-HKVTHTFPSPSVFRyLIKTDPEGtivRSKYDLsNLKEIWCGGEVIEESIPEYIEQ 401
Cdd:cd05971 160 VLAH-----RMTKFDPKAALDLMSrYGVTTAFLPPTALK-MMRQQGEQ---LKHAQV-KLRAIATGGESLGEELLGWARE 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 402 KLKIKCLRVYGQSEigvTSFISVHALNI-PYR--ATGVPSIYIRPSILSEEGEVLNSNEIGLVAFKLPMPPSFaITFYKN 478
Cdd:cd05971 230 QFGVEVNEFYGQTE---CNLVIGNCSALfPIKpgSMGKPIPGHRVAIVDDNGTPLPPGEVGEIAVELPDPVAF-LGYWNN 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 479 DEKFKQLFTRfpGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGIlsPDcrtaPIG 558
Cdd:cd05971 306 PSATEKKMAG--DWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGI--PD----PIR 377
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 559 ILVLKE----NPSI-DLNKLQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:cd05971 378 GEIVKAfvvlNPGEtPSDALAREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRREL 437
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
91-613 |
2.42e-30 |
|
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: 125.72 E-value: 2.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 91 IKLTYYQLYEKVCKFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGYSVKSLIDRIETITPKLIIT 170
Cdd:cd17642 43 VNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFC 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 171 TNYGIfnDEIITFtpnlkeaielstfkpsnvitlfrnevldETKLKKVQNIPTIPNT--LSWYDEIKKLKENNQSP---F 245
Cdd:cd17642 123 SKKGL--QKVLNV----------------------------QKKLKIIKTIIILDSKedYKGYQCLYTFITQNLPPgfnE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 246 YEYVPVESSHP---LYILYTSGTTGNTKAVVRsngPHM-VGIKYYTFRKESDIPQIVFSNANIGWVSF-HGF----FYGL 316
Cdd:cd17642 173 YDFKPPSFDRDeqvALIMNSSGSTGLPKGVQL---THKnIVARFSHARDPIFGNQIIPDTAILTVIPFhHGFgmftTLGY 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 317 LSGGNTLVMYEggiikneHIEDDLWI-AIVKHKVTHTFPSPSVFRYLIKTdpegTIVrSKYDLSNLKEIWCGGEVIEESI 395
Cdd:cd17642 250 LICGFRVVLMY-------KFEEELFLrSLQDYKVQSALLVPTLFAFFAKS----TLV-DKYDLSNLHEIASGGAPLSKEV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 396 PEYIEQKLKIKCLRV-YGQSEIGVTSFISVHALNIPyRATG--VPSIYIRpSILSEEGEVLNSNEIGLVAFKLPMppsfA 472
Cdd:cd17642 318 GEAVAKRFKLPGIRQgYGLTETTSAILITPEGDDKP-GAVGkvVPFFYAK-VVDLDTGKTLGPNERGELCVKGPM----I 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 473 ITFYKNDEKFKQLFTRFPGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGILSPDC 552
Cdd:cd17642 392 MKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDA 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66822211 553 RTAPIGILVLKENPSIDlnklQNEINNIITQDIESLAVLK-KIIVINQLPKTKVGKIPRQIL 613
Cdd:cd17642 472 GELPAAVVVLEAGKTMT----EKEVMDYVASQVSTAKRLRgGVKFVDEVPKGLTGKIDRRKI 529
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
16-608 |
4.64e-28 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 119.51 E-value: 4.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 16 YSNSNPEAFWDEVakknvfWE------KMYDKVYSGDEIYPD--WFKGGELNTCYNLLDIHiknpaKRDQDALIYECPyL 87
Cdd:PRK03584 42 WSVEDLEAFWQSV------WDffgvigSTPYTVVLAGRRMPGarWFPGARLNYAENLLRHR-----RDDRPAIIFRGE-D 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 88 KKTIKLTYYQLYEKVCKFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGAT-QCTLFDgYSVKSLIDRIETITPK 166
Cdd:PRK03584 110 GPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIwSSCSPD-FGVQGVLDRFGQIEPK 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 167 LIITTN-YGiFNDEIITFTPNLKEAIE-LSTFKPSNVITlfrnevldetKLKKVQNIPTIPNTLSWYDeikkLKENNQSP 244
Cdd:PRK03584 189 VLIAVDgYR-YGGKAFDRRAKVAELRAaLPSLEHVVVVP----------YLGPAAAAAALPGALLWED----FLAPAEAA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 245 FYEYVPVESSHPLYILYTSGTTGNTKAVVRSNG----PHMvgikyytfrKE----SDI-PQ-IVFSNANIGW------VS 308
Cdd:PRK03584 254 ELEFEPVPFDHPLWILYSSGTTGLPKCIVHGHGgillEHL---------KElglhCDLgPGdRFFWYTTCGWmmwnwlVS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 309 fhgffyGLLSGGnTLVMYEGGIIKNEHieDDLWIAIVKHKVTHTFPSPSVFRYLIKtdpEGTIVRSKYDLSNLKEIWCGG 388
Cdd:PRK03584 325 ------GLLVGA-TLVLYDGSPFYPDP--NVLWDLAAEEGVTVFGTSAKYLDACEK---AGLVPGETHDLSALRTIGSTG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 389 EVIEESIPEYIEQKLK--IKCLRVYGQSEIgVTSFI------SVHALNIPYRATGVpsiyiRPSILSEEGEVLnSNEIG- 459
Cdd:PRK03584 393 SPLPPEGFDWVYEHVKadVWLASISGGTDI-CSCFVggnpllPVYRGEIQCRGLGM-----AVEAWDEDGRPV-VGEVGe 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 460 LVAFKlPMpPSFAITFYkNDEKFKQL----FTRFPGYYDSGDLGYIDQRGFYTIVSRSDDQI-----KISCNKI--QLNT 528
Cdd:PRK03584 466 LVCTK-PF-PSMPLGFW-NDPDGSRYrdayFDTFPGVWRHGDWIEITEHGGVVIYGRSDATLnrggvRIGTAEIyrQVEA 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 529 IdtsilkhPSVLECCSIGILSPDcrtapiG----IL--VLKENPSIDlNKLQNEINNIITQDIESLAVLKKIIVINQLPK 602
Cdd:PRK03584 543 L-------PEVLDSLVIGQEWPD------GdvrmPLfvVLAEGVTLD-DALRARIRTTIRTNLSPRHVPDKIIAVPDIPR 608
|
....*.
gi 66822211 603 TKVGKI 608
Cdd:PRK03584 609 TLSGKK 614
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
93-610 |
2.02e-27 |
|
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: 115.40 E-value: 2.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 93 LTYYQLYEKVCKFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLfdgysvkslidrietitpkliittN 172
Cdd:cd17631 21 LTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPL------------------------N 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 173 YGIFNDEIitftpnlkeaielstfkpSNVITLFRNEVLdetklkkvqniptipntlswYDEikklkennqspfyeyvpve 252
Cdd:cd17631 77 FRLTPPEV------------------AYILADSGAKVL--------------------FDD------------------- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 253 sshPLYILYTSGTTGNTKAVVRSNGphMVGIKYYTfrkesdipQIVFSNANIGWVSFHGF--FYGLLSGGNTL-VMYEGG 329
Cdd:cd17631 100 ---LALLMYTSGTTGRPKGAMLTHR--NLLWNAVN--------ALAALDLGPDDVLLVVAplFHIGGLGVFTLpTLLRGG 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 330 --IIKNEHIEDDLWIAIVKHKVTHTFPSPSVFrYLIKTDPEgtivRSKYDLSNLKEIWCGGE-VIEESIPEYIEQKLKIk 406
Cdd:cd17631 167 tvVILRKFDPETVLDLIERHRVTSFFLVPTMI-QALLQHPR----FATTDLSSLRAVIYGGApMPERLLRALQARGVKF- 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 407 cLRVYGQSEI--GVTSFISVHALNIPyRATGVPSIYIRPSILSEEGEVLNSNEIGLVAFKLP--MPpsfaiTFYKNDEKF 482
Cdd:cd17631 241 -VQGYGMTETspGVTFLSPEDHRRKL-GSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPhvMA-----GYWNRPEAT 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 483 KQLFtrFPGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGIlsPDCR--TAPIGIL 560
Cdd:cd17631 314 AAAF--RDGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGV--PDEKwgEAVVAVV 389
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 66822211 561 VLKENPSIDLNKLqneinniITQDIESLA---VLKKIIVINQLPKTKVGKIPR 610
Cdd:cd17631 390 VPRPGAELDEDEL-------IAHCRERLArykIPKSVEFVDALPRNATGKILK 435
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
92-613 |
4.74e-27 |
|
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: 114.97 E-value: 4.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 92 KLTYYQLYEKVCKFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATqctlfdgysvkslidrietitpklIITT 171
Cdd:cd05936 24 KLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAV------------------------VVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 172 NygifndeiITFTPNLKEAIelstFKPSNVITLFRNEVLdETKLKKvqniptipntlswydeikklkennQSPFYEYVPV 251
Cdd:cd05936 80 N--------PLYTPRELEHI----LNDSGAKALIVAVSF-TDLLAA------------------------GAPLGERVAL 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 252 ESSHPLYILYTSGTTGNTKAVVRSNGPhmvgikyytfrkesdipqiVFSNAN--IGWVS---------------FHGF-- 312
Cdd:cd05936 123 TPEDVAVLQYTSGTTGVPKGAMLTHRN-------------------LVANALqiKAWLEdllegddvvlaalplFHVFgl 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 313 ----FYGLLSGGnTLVMYEGGIIKN--EHIEddlwiaivKHKVTHtFPS-PSVFRYLIKTdPEgtivRSKYDLSNLKEIW 385
Cdd:cd05936 184 tvalLLPLALGA-TIVLIPRFRPIGvlKEIR--------KHRVTI-FPGvPTMYIALLNA-PE----FKKRDFSSLRLCI 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 386 CGGEVIEESIPEYIEQKLKIKCLRVYGQSEigvTS-FISVHALNIPYRA----TGVPSIYIRpsILSEEGEVLNSNEIGL 460
Cdd:cd05936 249 SGGAPLPVEVAERFEELTGVPIVEGYGLTE---TSpVVAVNPLDGPRKPgsigIPLPGTEVK--IVDDDGEELPPGEVGE 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 461 VAFKLP--MPpsfaiTFYKNDEKFKQLFTRfpGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPS 538
Cdd:cd05936 324 LWVRGPqvMK-----GYWNRPEETAEAFVD--GWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPA 396
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66822211 539 VLECCSIGILSPDCRTAPIGILVLKENPSIDLNKlqneinnIITQDIESLA---VLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:cd05936 397 VAEAAVVGVPDPYSGEAVKAFVVLKEGASLTEEE-------IIAFCREQLAgykVPRQVEFRDELPKSAVGKILRREL 467
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
94-608 |
1.62e-26 |
|
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: 113.88 E-value: 1.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 94 TYYQLYEKVCKFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATqctlfdgysvkslidrIETITPKL-----I 168
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAV----------------LHTINPRLfpeqiA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 169 ITTNYGifNDEIITFTPNLKEAIE--LSTFKP-SNVITLFRNEVLDEtklkkvqniPTIPNTLSWYDEIkklkeNNQSPF 245
Cdd:cd12119 91 YIINHA--EDRVVFVDRDFLPLLEaiAPRLPTvEHVVVMTDDAAMPE---------PAGVGVLAYEELL-----AAESPE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 246 YEYVPVESSHPLYILYTSGTTGNTKAVV---RSNGPHMVGIKYYTFR--KESDI--PQIVFSNANiGW-VSFHGFFYG-- 315
Cdd:cd12119 155 YDWPDFDENTAAAICYTSGTTGNPKGVVyshRSLVLHAMAALLTDGLglSESDVvlPVVPMFHVN-AWgLPYAAAMVGak 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 316 -LLSG----GNTLVMyeggIIKNEhieddlwiaivkhKVTHTFPSPSVFRYLIKTdPEGTivrsKYDLSNLKEIWCGGEV 390
Cdd:cd12119 234 lVLPGpyldPASLAE----LIERE-------------GVTFAAGVPTVWQGLLDH-LEAN----GRDLSSLRRVVIGGSA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 391 IEESIPEYIEQKLkIKCLRVYGQSE---IGVTSFISVHALNIP------YRA-TGVPSIYIRPSILSEEGEVL--NSNEI 458
Cdd:cd12119 292 VPRSLIEAFEERG-VRVIHAWGMTEtspLGTVARPPSEHSNLSedeqlaLRAkQGRPVPGVELRIVDDDGRELpwDGKAV 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 459 G-LVAfklpMPPSFAITFYKNDEKfKQLFTRfPGYYDSGDLGYIDQRGFYTIVSRSDDQIK-----IScnKIQLNTIdts 532
Cdd:cd12119 371 GeLQV----RGPWVTKSYYKNDEE-SEALTE-DGWLRTGDVATIDEDGYLTITDRSKDVIKsggewIS--SVELENA--- 439
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66822211 533 ILKHPSVLECCSIGILSPDCRTAPIGILVLKENPSIDlnklQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKI 608
Cdd:cd12119 440 IMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVT----AEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKI 511
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
93-615 |
5.13e-26 |
|
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: 111.46 E-value: 5.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 93 LTYYQLYEKVCKFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGYSVKSLIDRIETITPKLIITtn 172
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 173 ygifndeiitftpnlkeaielstfkpsnvitlfrnevlDETKLKKVqniptipntlswydeikklkennqspfyeyvpve 252
Cdd:cd05973 79 --------------------------------------DAANRHKL---------------------------------- 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 253 SSHPLYILYTSGTTGNTKAVvrsngPH----MVGIKYYtFRKESDI-PQIVFSN-ANIGWVsfHGFFY---GLLSGGNTL 323
Cdd:cd05973 87 DSDPFVMMFTSGTTGLPKGV-----PVplraLAAFGAY-LRDAVDLrPEDSFWNaADPGWA--YGLYYaitGPLALGHPT 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 324 VMYEGGIIKnehieDDLWIAIVKHKVTHTFPSPSVFRYLIkTDPEGTIVRSKydlSNLKEIWCGGEVIEESIPEYIEQKL 403
Cdd:cd05973 159 ILLEGGFSV-----ESTWRVIERLGVTNLAGSPTAYRLLM-AAGAEVPARPK---GRLRRVSSAGEPLTPEVIRWFDAAL 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 404 KIKCLRVYGQSEIGVTsFISVHALNIPYRA--TGVPSIYIRPSILSEEGEVLNSNEIGLVAFKLPMPPSFAITFYKNDEk 481
Cdd:cd05973 230 GVPIHDHYGQTELGMV-LANHHALEHPVHAgsAGRAMPGWRVAVLDDDGDELGPGEPGRLAIDIANSPLMWFRGYQLPD- 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 482 fkqlfTRFP--GYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGILSPDcRTAPI-G 558
Cdd:cd05973 308 -----TPAIdgGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPE-RTEVVkA 381
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 66822211 559 ILVLKEN--PSIDLNKlqnEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQILSN 615
Cdd:cd05973 382 FVVLRGGheGTPALAD---ELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
258-610 |
9.88e-26 |
|
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: 110.63 E-value: 9.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 258 YILYTSGTTGNTKAVVRSNGphmvgiKYYTFR----------KESDIpqiVFSNANI--GWVSFHGFFYGLLSGGNTLVM 325
Cdd:cd05919 95 YLLYSSGTTGPPKGVMHAHR------DPLLFAdamarealglTPGDR---VFSSAKMffGYGLGNSLWFPLAVGASAVLN 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 326 YEggiiknEHIEDDLWIAIVKHKVTHTFPSPSVFRYLIktdPEGTIvrSKYDLSNLKEIWCGGEVIEESIPEYIEQKLKI 405
Cdd:cd05919 166 PG------WPTAERVLATLARFRPTVLYGVPTFYANLL---DSCAG--SPDALRSLRLCVSAGEALPRGLGERWMEHFGG 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 406 KCLRVYGQSEIGVTsFISVHALNIPYRATG--VPSIYIRpsILSEEGEVLNSNEIGLVAFKLPmppSFAITFYKNDEKFK 483
Cdd:cd05919 235 PILDGIGATEVGHI-FLSNRPGAWRLGSTGrpVPGYEIR--LVDEEGHTIPPGEEGDLLVRGP---SAAVGYWNNPEKSR 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 484 QLFTRfpGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGILSPDCRTAPIGILVLK 563
Cdd:cd05919 309 ATFNG--GWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLK 386
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 66822211 564 eNPSIDLNKLQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPR 610
Cdd:cd05919 387 -SPAAPQESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQR 432
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
62-613 |
3.60e-25 |
|
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: 109.77 E-value: 3.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 62 YNLLDIHIKNPAKR--DQDALIYecpylkKTIKLTYYQLYEKVCKFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCAR 139
Cdd:cd05959 3 YNAATLVDLNLNEGrgDKTAFID------DAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 140 IGA------TQCT-------LFDGYSvkslidRIETITPKliittnygifndeiitFTPNLKEAIELStfkpsnvitlfr 206
Cdd:cd05959 77 AGIvpvpvnTLLTpddyayyLEDSRA------RVVVVSGE----------------LAPVLAAALTKS------------ 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 207 nEVLDETkLKKVQNIPTIPNTLSWYDEIKKLkennqSPFYEYVPVESSHPLYILYTSGTTGNTKAVVrsngpHMVGIKYY 286
Cdd:cd05959 123 -EHTLVV-LIVSGGAGPEAGALLLAELVAAE-----AEQLKPAATHADDPAFWLYSSGSTGRPKGVV-----HLHADIYW 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 287 TFR---------KESDIpqiVFSNANIgwvsfhgFF-YGLlsgGNTLV--MYEGG--IIKNEHIEDDLWIA-IVKHKVTH 351
Cdd:cd05959 191 TAElyarnvlgiREDDV---CFSAAKL-------FFaYGL---GNSLTfpLSVGAttVLMPERPTPAAVFKrIRRYRPTV 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 352 TFPSPSVFRYLIKTDpegtiVRSKYDLSNLKEIWCGGEVIEESIPEYIEQKLKIKCLRVYGQSEIGVTsFISVHALNIPY 431
Cdd:cd05959 258 FFGVPTLYAAMLAAP-----NLPSRDLSSLRLCVSAGEALPAEVGERWKARFGLDILDGIGSTEMLHI-FLSNRPGRVRY 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 432 RATGVPSIYIRPSILSEEGEVLNSNEIGLVAFKlpmPPSFAITFYKNDEKFKQLFTrfPGYYDSGDLGYIDQRGFYTIVS 511
Cdd:cd05959 332 GTTGKPVPGYEVELRDEDGGDVADGEPGELYVR---GPSSATMYWNNRDKTRDTFQ--GEWTRTGDKYVRDDDGFYTYAG 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 512 RSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGILSPDCRTAPIGILVLKENpSIDLNKLQNEINNIITQDIESLAVL 591
Cdd:cd05959 407 RADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPG-YEDSEALEEELKEFVKDRLAPYKYP 485
|
570 580
....*....|....*....|..
gi 66822211 592 KKIIVINQLPKTKVGKIPRQIL 613
Cdd:cd05959 486 RWIVFVDELPKTATGKIQRFKL 507
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
255-610 |
2.56e-24 |
|
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: 104.02 E-value: 2.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 255 HPLYILYTSGTTGNTKAVVRSNGPHMVgikyyTFRKESDIPQIvfSNANI----GWVSFHGFFYGLLSggntlVMYEGG- 329
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIE-----SFVCNEDLFNI--SGEDAilapGPLSHSLFLYGAIS-----ALYLGGt 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 330 -IIKNEHIEDDLWIAIVKHKVTHTFPSPSVFRYLIKTD-PEGTIvrskydlsnlKEIWCGGEVIEESIPEYIEQKL-KIK 406
Cdd:cd17633 69 fIGQRKFNPKSWIRKINQYNATVIYLVPTMLQALARTLePESKI----------KSIFSSGQKLFESTKKKLKNIFpKAN 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 407 CLRVYGQSEigvTSFISVHALN--IPYRATGVPSIYIRPSILSEEGevlnsNEIGLVAFKLPMPPSFAIT--FYKNDekf 482
Cdd:cd17633 139 LIEFYGTSE---LSFITYNFNQesRPPNSVGRPFPNVEIEIRNADG-----GEIGKIFVKSEMVFSGYVRggFSNPD--- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 483 kqlftrfpGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGIlsPDCRTAPIGILVL 562
Cdd:cd17633 208 --------GWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGI--PDARFGEIAVALY 277
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 66822211 563 KENPSIDLNKLQNEINNIITQDIEslavlKKIIVINQLPKTKVGKIPR 610
Cdd:cd17633 278 SGDKLTYKQLKRFLKQKLSRYEIP-----KKIIFVDSLPYTSSGKIAR 320
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
76-610 |
2.72e-24 |
|
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: 106.07 E-value: 2.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 76 DQDALIYEcpylkkTIKLTYYQLYEKVCKFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATqCTLFDgysVKS 155
Cdd:cd05930 2 DAVAVVDG------DQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAA-YVPLD---PSY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 156 LIDRIETI----TPKLIITtnygifndeiitftpnlkeaielstfkpsnvitlfrnevldetklkkvqniptipntlswy 231
Cdd:cd05930 72 PAERLAYIledsGAKLVLT------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 232 deikklkennqspfyeyvpvESSHPLYILYTSGTTGNTKAVVrsnGPHMvGIKYYTFRKESDIP----QIVFSNANIGW- 306
Cdd:cd05930 91 --------------------DPDDLAYVIYTSGSTGKPKGVM---VEHR-GLVNLLLWMQEAYPltpgDRVLQFTSFSFd 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 307 VSFHGFFYGLLSGGnTLVmyeggIIKNEHIED--DLWIAIVKHKVTHTFPSPSVFRYLIKTDPEGtivrskyDLSNLKEI 384
Cdd:cd05930 147 VSVWEIFGALLAGA-TLV-----VLPEEVRKDpeALADLLAEEGITVLHLTPSLLRLLLQELELA-------ALPSLRLV 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 385 WCGGEVIEESIPEYIEQKLKIKCLR-VYGQSE--IGVTSFiSVHALNIPYRAT--GVP----SIYI-----RPSILSEEG 450
Cdd:cd05930 214 LVGGEALPPDLVRRWRELLPGARLVnLYGPTEatVDATYY-RVPPDDEEDGRVpiGRPipntRVYVldenlRPVPPGVPG 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 451 EVLnsneIGlvafklpmPPSFAITFYKNDEKFKQLFTRFPG-----YYDSGDLGYIDQRGfyTIV--SRSDDQIKISCNK 523
Cdd:cd05930 293 ELY----IG--------GAGLARGYLNRPELTAERFVPNPFgpgerMYRTGDLVRWLPDG--NLEflGRIDDQVKIRGYR 358
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 524 IQLNTIDTSILKHPSVLECCSIGILSPDCRTAPIGILVLKENPSIDLNKLQNEINniitqdiESL---AVLKKIIVINQL 600
Cdd:cd05930 359 IELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDEEELRAHLA-------ERLpdyMVPSAFVVLDAL 431
|
570
....*....|
gi 66822211 601 PKTKVGKIPR 610
Cdd:cd05930 432 PLTPNGKVDR 441
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
93-619 |
2.56e-23 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 103.79 E-value: 2.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 93 LTYYQLYEKVCKFSRVLLN-LNVSKNDNVLIFMANTLEPLIAMLSCARIGATqctlfdgysvkslidrietITPkliitt 171
Cdd:PRK06839 28 MTYKQLHEYVSKVAAYLIYeLNVKKGERIAILSQNSLEYIVLLFAIAKVECI-------------------AVP------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 172 nygiFNdeiITFTPNlkeaiELS-TFKPSNVITL-----FRNEVLDETKLKKVQniPTIpntlswydEIKKLKENNQSPF 245
Cdd:PRK06839 83 ----LN---IRLTEN-----ELIfQLKDSGTTVLfvektFQNMALSMQKVSYVQ--RVI--------SITSLKEIEDRKI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 246 YEYVPVESSHPLYILYTSGTTGNTKAVVRS------NGPHMVGIKYYTFRKESDIPQIVFSNANIGWVSFHGFFYGllsg 319
Cdd:PRK06839 141 DNFVEKNESASFIICYTSGTTGKPKGAVLTqenmfwNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAFPTLFAG---- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 320 gntlvmyeGGIIKNEHIEDDLWIAIV-KHKVTHTFPSPSVFRYLIKtdpegTIVRSKYDLSNLKEIWCGGE-VIEESIPE 397
Cdd:PRK06839 217 --------GVIIVPRKFEPTKALSMIeKHKVTVVMGVPTIHQALIN-----CSKFETTNLQSVRWFYNGGApCPEELMRE 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 398 YIEQKLKIKclRVYGQSEIGVTSF-ISVHALNIPYRATGVPSIYIRPSILSEEGEVLNSNEIGLVAFKLPMppsfAITFY 476
Cdd:PRK06839 284 FIDRGFLFG--QGFGMTETSPTVFmLSEEDARRKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPN----VMKEY 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 477 KNDEKFKQLFTRfPGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGILSPDCRTAP 556
Cdd:PRK06839 358 WNRPDATEETIQ-DGWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIP 436
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66822211 557 IGILVLKENPSIdlnkLQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQILSNLLND 619
Cdd:PRK06839 437 IAFIVKKSSSVL----IEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQLKS 495
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
243-615 |
1.57e-22 |
|
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: 101.77 E-value: 1.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 243 SPFYEYVPVESSHPLYILYTSGTTGNTKAVVRSNGPHMVGIK----YYTFRKESDIpqiVFSNANIGWV--SFHGFFYGL 316
Cdd:cd05928 163 STEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKvngrYWLDLTASDI---MWNTSDTGWIksAWSSLFEPW 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 317 LSGGNTLV----MYEGGIIKNehieddlwiAIVKHKVTHTFPSPSVFRYLIKTDpegtivRSKYDLSNLKEIWCGGEVIE 392
Cdd:cd05928 240 IQGACVFVhhlpRFDPLVILK---------TLSSYPITTFCGAPTVYRMLVQQD------LSSYKFPSLQHCVTGGEPLN 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 393 ESIPEYIEQKLKIKCLRVYGQSEIGVTSFISvHALNIPYRATGVPSIYIRPSILSEEGEVLNSNEIGLVAFKL-PMPPSF 471
Cdd:cd05928 305 PEVLEKWKAQTGLDIYEGYGQTETGLICANF-KGMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRVkPIRPFG 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 472 AITFYKnDEKFKQLFTRFPGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGilSPD 551
Cdd:cd05928 384 LFSGYV-DNPEKTAATIRGDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVS--SPD 460
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66822211 552 crtaPIGILVLKE----NP---SIDLNKLQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQILSN 615
Cdd:cd05928 461 ----PIRGEVVKAfvvlAPqflSHDPEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRD 527
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
93-613 |
2.58e-22 |
|
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: 100.25 E-value: 2.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 93 LTYYQLYEKVCKFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATqctlfdgysvkslidrietitpkliittn 172
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAV----------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 173 ygifndeIITFTPNLKEAiELSTF-KPSNVITLFRNEVLDETKLkkvqniptipntlswydeikklkennqspfyeyvpv 251
Cdd:cd05935 53 -------VVPINPMLKER-ELEYIlNDSGAKVAVVGSELDDLAL------------------------------------ 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 252 esshplyILYTSGTTGNTKAVVRSNG---PHMVGIKYYTFRKESDIpqIVFSNANIGWVSFHGFFYGLLSGGNTLVMYeg 328
Cdd:cd05935 89 -------IPYTSGTTGLPKGCMHTHFsaaANALQSAVWTGLTPSDV--ILACLPLFHVTGFVGSLNTAVYVGGTYVLM-- 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 329 GIIKNEHIEDdlwiAIVKHKVTHTFPSPSVFRYLIKTdPEgtivRSKYDLSNLKEIWCGGEVIEESIPEYIEQKLKIKCL 408
Cdd:cd05935 158 ARWDRETALE----LIEKYKVTFWTNIPTMLVDLLAT-PE----FKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFV 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 409 RVYGQSEIgvtsfISVHALNIPYR----ATGVPSIYIRPSILS-EEGEVLNSNEIGLVAFKlpmPPSFAITFYKNDEKFK 483
Cdd:cd05935 229 EGYGLTET-----MSQTHTNPPLRpklqCLGIP*FGVDARVIDiETGRELPPNEVGEIVVR---GPQIFKGYWNRPEETE 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 484 QLFTRFPG--YYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGIlsPDCRTA--PIGI 559
Cdd:cd05935 301 ESFIEIKGrrFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISV--PDERVGeeVKAF 378
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 66822211 560 LVLKenPSIDLNKLQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:cd05935 379 IVLR--PEYRGKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
91-608 |
2.71e-22 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 100.48 E-value: 2.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 91 IKLTYYQLYEKVCKFSRVLLNLNVSkNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGYSVKSLIDRIETITPKLIIT 170
Cdd:cd05909 6 TSLTYRKLLTGAIALARKLAKMTKE-GENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 171 TnygifndeiitftpnlKEAIELSTFKPSNVITLFrnevldetklKKVQNIPTIPNTLSWYDEIKKLKENNQSPFYEY-- 248
Cdd:cd05909 85 S----------------KQFIEKLKLHHLFDVEYD----------ARIVYLEDLRAKISKADKCKAFLAGKFPPKWLLri 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 249 ---VPVESSHPLYILYTSGTTGNTKAVVRSNGPHMVGIkYYTFRKESDIPQIVFSNAnigWVSFHGF------FYGLLSG 319
Cdd:cd05909 139 fgvAPVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANV-EQITAIFDPNPEDVVFGA---LPFFHSFgltgclWLPLLSG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 320 GNtLVMY----EGGIIKNehieddlwiAIVKHKVTHTFPSPSVFRYLIKTdpegtivRSKYDLSNLKEIWCGGEVIEESI 395
Cdd:cd05909 215 IK-VVFHpnplDYKKIPE---------LIYDKKATILLGTPTFLRGYARA-------AHPEDFSSLRLVVAGAEKLKDTL 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 396 PEYIEQKLKIKCLRVYGQSEigVTSFISVHALNIPYRATGV----PSIYIRpsILSEEG-EVLNSNEIGLVAFKlpmPPS 470
Cdd:cd05909 278 RQEFQEKFGIRILEGYGTTE--CSPVISVNTPQSPNKEGTVgrplPGMEVK--IVSVEThEEVPIGEGGLLLVR---GPN 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 471 FAITFYKNDEKFKQLFTRfpGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKH-PSVLECCSIGIls 549
Cdd:cd05909 351 VMLGYLNEPELTSFAFGD--GWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSV-- 426
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 66822211 550 PDCRTAPIGILVLKEnPSIDLNKLQNEINNIitqDIESLAVLKKIIVINQLPKTKVGKI 608
Cdd:cd05909 427 PDGRKGEKIVLLTTT-TDTDPSSLNDILKNA---GISNLAKPSYIHQVEEIPLLGTGKP 481
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
90-615 |
1.74e-21 |
|
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: 98.15 E-value: 1.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 90 TIKLTYYQLYEKVCKFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGYSVKSLIDRIETITPKLII 169
Cdd:cd05926 12 TPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 170 TTNYGifndeiitFTPNLKEAIELstfkpsnVITLFRNEVLDETKLKKVQNiPTIPNTLSWYDEIKKLKennqspfyeyv 249
Cdd:cd05926 92 TPKGE--------LGPASRAASKL-------GLAILELALDVGVLIRAPSA-ESLSNLLADKKNAKSEG----------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 250 PVESSHPLYILYTSGTTGNTKAVVRSNGPHMVGIKYY--TFR-KESDIPQIVFSNANIgwvsfHGFFYGLLSggnTLvmY 326
Cdd:cd05926 145 VPLPDDLALILHTSGTTGRPKGVPLTHRNLAASATNItnTYKlTPDDRTLVVMPLFHV-----HGLVASLLS---TL--A 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 327 EGG--IIKNEHIEDDLWIAIVKHKVTHTFPSPSVFRYLIKT-DPEGTIVRSKydlsnLKEIWCGGEVIEESIPEYIEQKL 403
Cdd:cd05926 215 AGGsvVLPPRFSASTFWPDVRDYNATWYTAVPTIHQILLNRpEPNPESPPPK-----LRFIRSCSASLPPAVLEALEATF 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 404 KIKCLRVYGQSEigVTSFISVHALNIPYRATG-VPsiyiRPS-----ILSEEGEVLNSNEIGLVAFKLPmppsfAITF-Y 476
Cdd:cd05926 290 GAPVLEAYGMTE--AAHQMTSNPLPPGPRKPGsVG----KPVgvevrILDEDGEILPPGVVGEICLRGP-----NVTRgY 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 477 KNDEKF-KQLFTRFpGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGIlsPDCR-- 553
Cdd:cd05926 359 LNNPEAnAEAAFKD-GWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGV--PDEKyg 435
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66822211 554 ---TAPIgilVLKENPSIDlnklQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQILSN 615
Cdd:cd05926 436 eevAAAV---VLREGASVT----EEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
249-610 |
1.23e-19 |
|
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: 92.12 E-value: 1.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 249 VPVESSHPLYILYTSGTTGNTKAVVRSNGPHMVG----IKYYTFRKESDIPQIVfsnanigwvSFHgFFYGL------LS 318
Cdd:cd05922 112 HEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANarsiAEYLGITADDRALTVL---------PLS-YDYGLsvlnthLL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 319 GGNTLVMYEGGIIknehiEDDLWIAIVKHKVTHTFPSPSVFRYL--IKTDPEGtivrskydLSNLKEIW-CGGEVIEESI 395
Cdd:cd05922 182 RGATLVLTNDGVL-----DDAFWEDLREHGATGLAGVPSTYAMLtrLGFDPAK--------LPSLRYLTqAGGRLPQETI 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 396 PEYIEQKLKIKCLRVYGQSE-IGVTSFISVHALNIPYRATGVPSIYIRPSILSEEGEVLNSNEIGLVAFKLPmppsFAIT 474
Cdd:cd05922 249 ARLRELLPGAQVYVMYGQTEaTRRMTYLPPERILEKPGSIGLAIPGGEFEILDDDGTPTPPGEPGEIVHRGP----NVMK 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 475 FYKNDEKFKQLFTRFPGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGIlsPDCRT 554
Cdd:cd05922 325 GYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGL--PDPLG 402
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 66822211 555 APIGILVLKEnPSIDLnklqNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPR 610
Cdd:cd05922 403 EKLALFVTAP-DKIDP----KDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDY 453
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
68-608 |
2.36e-19 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 92.14 E-value: 2.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 68 HIKNPAKR--DQDALIYecpyLKKTIKLTYYQLYEKVCKFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQC 145
Cdd:PRK12583 23 AFDATVARfpDREALVV----RHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 146 TLFDGYSVKSLIDRIETITPKLII------TTNYGIFNDEIItftPNLKEAielstfkpsnvitlfRNEVLDETKLKKVQ 219
Cdd:PRK12583 99 NINPAYRASELEYALGQSGVRWVIcadafkTSDYHAMLQELL---PGLAEG---------------QPGALACERLPELR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 220 NI----PTIPNTLSWYDEIKKLKE--NNQSPFYEYVPVESSHPLYILYTSGTTGNTKAVVRS-----NGPHMVGIKYYTf 288
Cdd:PRK12583 161 GVvslaPAPPPGFLAWHELQARGEtvSREALAERQASLDRDDPINIQYTSGTTGFPKGATLShhnilNNGYFVAESLGL- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 289 rKESD---IPqivfsnanigwVSFHGFFYGLLSggNTLVMYEGG--IIKNEHIEDDLWI-AIVKHKVTHTFPSPSVFRYL 362
Cdd:PRK12583 240 -TEHDrlcVP-----------VPLYHCFGMVLA--NLGCMTVGAclVYPNEAFDPLATLqAVEEERCTALYGVPTMFIAE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 363 IkTDPEgtivRSKYDLSNLKE-IWCGGEVIEESIPEYIEQKLKIKCLRVYGQSEIGVTSFISVHALNIPYRATGVPSI-- 439
Cdd:PRK12583 306 L-DHPQ----RGNFDLSSLRTgIMAGAPCPIEVMRRVMDEMHMAEVQIAYGMTETSPVSLQTTAADDLERRVETVGRTqp 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 440 YIRPSILSEEGEVLNSNEIGLVAFKlpmPPSFAITFYKNDEKFKQLFTRfPGYYDSGDLGYIDQRGFYTIVSRSDDQIKI 519
Cdd:PRK12583 381 HLEVKVVDPDGATVPRGEIGELCTR---GYSVMKGYWNNPEATAESIDE-DGWMHTGDLATMDEQGYVRIVGRSKDMIIR 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 520 SCNKIQLNTIDTSILKHPSVLECCSIGIlsPDCRTAP--IGILVLKENPSIDLnklqNEINNIITQDIESLAVLKKIIVI 597
Cdd:PRK12583 457 GGENIYPREIEEFLFTHPAVADVQVFGV--PDEKYGEeiVAWVRLHPGHAASE----EELREFCKARIAHFKVPRYFRFV 530
|
570
....*....|.
gi 66822211 598 NQLPKTKVGKI 608
Cdd:PRK12583 531 DEFPMTVTGKV 541
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
93-613 |
7.25e-19 |
|
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: 89.99 E-value: 7.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 93 LTYYQLYEKVCKFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGYSVKSLIDRIETITPKLIITTN 172
Cdd:cd05904 33 LTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 173 ygifndeiitftpnlKEAIELSTFKPSNVitlfrneVLDETKlkkvqniptipnTLSWYdeIKKLKENNQSPFYEYVPVE 252
Cdd:cd05904 113 ---------------ELAEKLASLALPVV-------LLDSAE------------FDSLS--FSDLLFEADEAEPPVVVIK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 253 SSHPLYILYTSGTTGNTKAVVRSngpH-----MVGIkYYTFRKESDIPQIVFsnanIGWVS-FH-----GFFYGLLSGGN 321
Cdd:cd05904 157 QDDVAALLYSSGTTGRSKGVMLT---HrnliaMVAQ-FVAGEGSNSDSEDVF----LCVLPmFHiyglsSFALGLLRLGA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 322 TLV---MYEGGIIKNehieddlwiAIVKHKVTHTFPSPSVFRYLIKtDPEGtivrSKYDLSNLKEIWCGG-----EVIEE 393
Cdd:cd05904 229 TVVvmpRFDLEELLA---------AIERYKVTHLPVVPPIVLALVK-SPIV----DKYDLSSLRQIMSGAaplgkELIEA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 394 sipeyIEQKL-KIKCLRVYGQSEIG--VTSFISVHALNIPYRATG--VPSIYIRpsILS-EEGEVLNSNEIGLVAFKLP- 466
Cdd:cd05904 295 -----FRAKFpNVDLGQGYGMTESTgvVAMCFAPEKDRAKYGSVGrlVPNVEAK--IVDpETGESLPPNQTGELWIRGPs 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 467 -MppsfaiTFYKNDEKFKQLFTRFPGYYDSGDLGYIDQRGFYTIVSRSDDQIKisCNKIQ-----LNTIdtsILKHPSVL 540
Cdd:cd05904 368 iM------KGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIK--YKGFQvapaeLEAL---LLSHPEIL 436
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66822211 541 ECCSIGILSPDCRTAPIGILVLKENPSIDlnklQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:cd05904 437 DAAVIPYPDEEAGEVPMAFVVRKPGSSLT----EDEIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
242-608 |
1.12e-18 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 89.76 E-value: 1.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 242 QSPFYEYVPVESshPLYILYTSGTTGNTKAVVRSNGP--------HMVGIKYytfrkeSDIPQIVfsnANIGWVSFHG-- 311
Cdd:PRK12406 142 QQEPYDGPPVPQ--PQSMIYTSGTTGHPKGVRRAAPTpeqaaaaeQMRALIY------GLKPGIR---ALLTGPLYHSap 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 312 FFYGLLSG--GNTLVM---YEggiiknehiEDDLWIAIVKHKVTHTFPSPSVFRYLIKTDPEgtiVRSKYDLSNLKEIW- 385
Cdd:PRK12406 211 NAYGLRAGrlGGVLVLqprFD---------PEELLQLIERHRITHMHMVPTMFIRLLKLPEE---VRAKYDVSSLRHVIh 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 386 ----CGGEVIEESI----PEYIEqklkikclrVYGQSEIGVTSF-ISVHALNIPyRATGVPSIYIRPSILSEEGEVLNSN 456
Cdd:PRK12406 279 aaapCPADVKRAMIewwgPVIYE---------YYGSTESGAVTFaTSEDALSHP-GTVGKAAPGAELRFVDEDGRPLPQG 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 457 EIGLVAFKLPMPPSFaiTFYKNDEKFKQLftRFPGYYDSGDLGYIDQRGFYTIVSRSDDQIkISCN-KIQLNTIDTSILK 535
Cdd:PRK12406 349 EIGEIYSRIAGNPDF--TYHNKPEKRAEI--DRGGFITSGDVGYLDADGYLFLCDRKRDMV-ISGGvNIYPAEIEAVLHA 423
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66822211 536 HPSVLECCSIGIlsPDCRTAPIGILVLKENPSIDLnklqnEINNIITQDIESLA---VLKKIIVINQLPKTKVGKI 608
Cdd:PRK12406 424 VPGVHDCAVFGI--PDAEFGEALMAVVEPQPGATL-----DEADIRAQLKARLAgykVPKHIEIMAELPREDSGKI 492
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
93-619 |
2.65e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 88.30 E-value: 2.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 93 LTYYQLYEKVCKfSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGYSVKSLIDRIETITPKLIITTN 172
Cdd:PRK07638 27 LTYKDWFESVCK-VANWLNEKESKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNADMIVTER 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 173 YgifndeiitftpnlkeaielstfkpsnvitlFRNEVLDEtklkkvqNIPTIpntlSWyDEIKKLKENNQSpfyEYVPVE 252
Cdd:PRK07638 106 Y-------------------------------KLNDLPDE-------EGRVI----EI-DEWKRMIEKYLP---TYAPIE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 253 SSH--PLYILYTSGTTGNTKAVVRSNGP--HMVGIKYYTFRKESD----IPQIVFSNAnigwvsfhgFFYGLLSggnTLv 324
Cdd:PRK07638 140 NVQnaPFYMGFTSGSTGKPKAFLRAQQSwlHSFDCNVHDFHMKREdsvlIAGTLVHSL---------FLYGAIS---TL- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 325 mYEGGIIkneHIEDDL-------WIAIVKHKVTHTFPSPSVFRYLIKTDPEgtivrskydlSNLKEIWCGGEVIEESIPE 397
Cdd:PRK07638 207 -YVGQTV---HLMRKFipnqvldKLETENISVMYTVPTMLESLYKENRVIE----------NKMKIISSGAKWEAEAKEK 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 398 YIEQKLKIKCLRVYGQSEIGVTSFISVHALNIPYRATGVPSIYIRPSILSEEGEVLNSNEIGLVAFKLPMppSFAitFYK 477
Cdd:PRK07638 273 IKNIFPYAKLYEFYGASELSFVTALVDEESERRPNSVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQ--FFM--GYI 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 478 NDEKFKQLFTRfPGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGIlsPDCRTAPI 557
Cdd:PRK07638 349 IGGVLARELNA-DGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGV--PDSYWGEK 425
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66822211 558 GILVLKENPsidlNKLQneINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQILSNLLND 619
Cdd:PRK07638 426 PVAIIKGSA----TKQQ--LKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSWIEN 481
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
248-610 |
4.35e-18 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 87.30 E-value: 4.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 248 YVPVESSHPL-----------------------YILYTSGTTGNTKAVVRSNG------PHMVGikYYTFrkesdIPQIV 298
Cdd:cd05945 68 YVPLDASSPAerireildaakpalliadgddnaYIIFTSGSTGRPKGVQISHDnlvsftNWMLS--DFPL-----GPGDV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 299 FSN-ANIGW-VSFHGFFYGLLSGGnTLVmyeggIIKNEHIED--DLWIAIVKHKVTHTFPSPSVFRYLIKT---DPEGti 371
Cdd:cd05945 141 FLNqAPFSFdLSVMDLYPALASGA-TLV-----PVPRDATADpkQLFRFLAEHGITVWVSTPSFAAMCLLSptfTPES-- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 372 vrskydLSNLKEIWCGGEVIEESIPEYIEQKL-KIKCLRVYGQSE--IGVTSF-ISVHALNipyRATGVPSIYIRP---- 443
Cdd:cd05945 213 ------LPSLRHFLFCGEVLPHKTARALQQRFpDARIYNTYGPTEatVAVTYIeVTPEVLD---GYDRLPIGYAKPgakl 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 444 SILSEEGEVLNSNEIG--LVAfklpmPPSFAITFYKNDEKFKQLFTRFPGY--YDSGDLGYIDQRGFYTIVSRSDDQIKI 519
Cdd:cd05945 284 VILDEDGRPVPPGEKGelVIS-----GPSVSKGYLNNPEKTAAAFFPDEGQraYRTGDLVRLEADGLLFYRGRLDFQVKL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 520 SCNKIQLNTIDTSILKHPSVLECCSIGILSPDCRTAPIGILVLKENpsiDLNKLQNEINNIITQDIESLAVLKKIIVINQ 599
Cdd:cd05945 359 NGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPG---AEAGLTKAIKAELAERLPPYMIPRRFVYLDE 435
|
410
....*....|.
gi 66822211 600 LPKTKVGKIPR 610
Cdd:cd05945 436 LPLNANGKIDR 446
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
261-613 |
1.10e-17 |
|
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: 85.99 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 261 YTSGTTGNTKAVV----------RSNGPHMVGIKyytfrkESD----IPQIVFSnanigwvsfhgffYGLlsGGNTLVMY 326
Cdd:cd05958 104 FTSGTTGAPKATMhfhrdplasaDRYAVNVLRLR------EDDrfvgSPPLAFT-------------FGL--GGVLLFPF 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 327 EGG---IIKNEHIEDDLWIAIVKHKVTHTFPSPSVFRYLIKTDPEGtivrsKYDLSNLKEIWCGGEVIEESIPEYIEQKL 403
Cdd:cd05958 163 GVGasgVLLEEATPDLLLSAIARYKPTVLFTAPTAYRAMLAHPDAA-----GPDLSSLRKCVSAGEALPAALHRAWKEAT 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 404 KIKCLRVYGQSEIgVTSFISVHALNIPYRATGVPSIYIRPSILSEEGEVLNSNEIGLVAFKLPmppsfaiTFYK-NDEKF 482
Cdd:cd05958 238 GIPIIDGIGSTEM-FHIFISARPGDARPGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRGP-------TGCRyLADKR 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 483 KQLFTRfPGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGILSPDCRTAPIGILVL 562
Cdd:cd05958 310 QRTYVQ-GGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVL 388
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 66822211 563 KENPSIDlNKLQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:cd05958 389 RPGVIPG-PVLARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFAL 438
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
93-613 |
1.56e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 86.24 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 93 LTYYQLYEKVCKFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGYSVKSLIDRIETITPKLIITTN 172
Cdd:PRK06710 50 ITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 173 YGIFNDEIITFTPNLKEAI--ELSTFKP--SNVITLFRNEVLDETKLKKVQNiptipNTLSWYDEIKKLKENNQSpfyey 248
Cdd:PRK06710 130 LVFPRVTNVQSATKIEHVIvtRIADFLPfpKNLLYPFVQKKQSNLVVKVSES-----ETIHLWNSVEKEVNTGVE----- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 249 VPVESSHPLYIL-YTSGTTGNTKAVVRSN----GPHMVGIKYYTFRKESDipQIVfsnanIGWVSFHgFFYGLLSGGNTL 323
Cdd:PRK06710 200 VPCDPENDLALLqYTGGTTGFPKGVMLTHknlvSNTLMGVQWLYNCKEGE--EVV-----LGVLPFF-HVYGMTAVMNLS 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 324 VM--YEGGIIKNEHIEDdLWIAIVKHKVThTFP-SPSVFRYLIKTDpegtiVRSKYDLSNLKEIWCGGEVIEESIPEYIE 400
Cdd:PRK06710 272 IMqgYKMVLIPKFDMKM-VFEAIKKHKVT-LFPgAPTIYIALLNSP-----LLKEYDISSIRACISGSAPLPVEVQEKFE 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 401 QKLKIKCLRVYGQSEIG-VTSFISVHALNIPyRATGVPSIYIRPSILS-EEGEVLNSNEIGLVAFKlpmPPSFAITFYKN 478
Cdd:PRK06710 345 TVTGGKLVEGYGLTESSpVTHSNFLWEKRVP-GSIGVPWPDTEAMIMSlETGEALPPGEIGEIVVK---GPQIMKGYWNK 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 479 DEKFKQLFTrfPGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGILSPDCRTAPIG 558
Cdd:PRK06710 421 PEETAAVLQ--DGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKA 498
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 66822211 559 ILVLKENPSIDlnklQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:PRK06710 499 FVVLKEGTECS----EEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
316-608 |
4.42e-17 |
|
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: 83.30 E-value: 4.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 316 LLSGGNTLVMYEGGIiKNEHIEDDLWIAIVKHKVTHTFPSPSVFRYLIKTdPEGTivrskyDLSNLKEIWCGGEVIEESI 395
Cdd:cd05944 66 LASGAHVVLAGPAGY-RNPGLFDNFWKLVERYRITSLSTVPTVYAALLQV-PVNA------DISSLRFAMSGAAPLPVEL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 396 PEYIEQKLKIKCLRVYGQSEigVTSFISVHALNIPYR--ATGVPSIYIRPSILSEEGEV-----LNSNEIGLVAFKLPMp 468
Cdd:cd05944 138 RARFEDATGLPVVEGYGLTE--ATCLVAVNPPDGPKRpgSVGLRLPYARVRIKVLDGVGrllrdCAPDEVGEICVAGPG- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 469 psfAITFYKNDEKFKQLFTRfPGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGIL 548
Cdd:cd05944 215 ---VFGGYLYTEGNKNAFVA-DGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQP 290
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 549 SPDCRTAPIGILVLKENPSIDLNKLQNEINNIITqdiESLAVLKKIIVINQLPKTKVGKI 608
Cdd:cd05944 291 DAHAGELPVAYVQLKPGAVVEEEELLAWARDHVP---ERAAVPKHIEVLEELPVTAVGKV 347
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
248-613 |
5.07e-17 |
|
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: 83.88 E-value: 5.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 248 YVPVESSHPLY-------------------ILYTSGTTGNTKAVV--RSNGPHMVG--IKYYTFRKESDIPQIvfsnanI 304
Cdd:cd05941 64 AVPLNPSYPLAeleyvitdsepslvldpalILYTSGTTGRPKGVVltHANLAANVRalVDAWRWTEDDVLLHV------L 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 305 GWVSFHGFFYGL---LSGGNTLVMyeggiikneHIEDDLWI-AIVKHK--VTHTFPSPSVFRYLIKT---DPEGTIVRSK 375
Cdd:cd05941 138 PLHHVHGLVNALlcpLFAGASVEF---------LPKFDPKEvAISRLMpsITVFMGVPTIYTRLLQYyeaHFTDPQFARA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 376 YDLSNLKEIWCGGEVIEESIPEYIEQKLKIKCLRVYGQSEIGVtsfisvhALNIPY----RATGV----PSIYIRpsILS 447
Cdd:cd05941 209 AAAERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTEIGM-------ALSNPLdgerRPGTVgmplPGVQAR--IVD 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 448 EE-GEVLNSNEIGLVAFKlpmPPSFAITFYKNDEKFKQLFTRfPGYYDSGDLGYIDQRGFYTIVSR-SDDQIKISCNKIQ 525
Cdd:cd05941 280 EEtGEPLPRGEVGEIQVR---GPSVFKEYWNKPEATKEEFTD-DGWFKTGDLGVVDEDGYYWILGRsSVDIIKSGGYKVS 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 526 LNTIDTSILKHPSVLECCSIGILSPDCRTAPIGILVLKEN-PSIDLNKLQNEINniitqdiESLAVLK---KIIVINQLP 601
Cdd:cd05941 356 ALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGaAALSLEELKEWAK-------QRLAPYKrprRLILVDELP 428
|
410
....*....|..
gi 66822211 602 KTKVGKIPRQIL 613
Cdd:cd05941 429 RNAMGKVNKKEL 440
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
259-613 |
5.47e-17 |
|
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: 83.55 E-value: 5.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 259 ILYTSGTTGNTKAVVRSNGPHmvgikYYTfrkesdipqIVFSNANIG------WVS----FHgffyglLSGGNTL---VM 325
Cdd:cd05912 82 IMYTSGTTGKPKGVQQTFGNH-----WWS---------AIGSALNLGlteddnWLCalplFH------ISGLSILmrsVI 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 326 YEGGIIKNEHI-EDDLWIAIVKHKVTHTFPSPSVFRYLIKTDPEGtivrskYDlSNLKEIWCGGEVIEESIPEYIEQKlK 404
Cdd:cd05912 142 YGMTVYLVDKFdAEQVLHLINSGKVTIISVVPTMLQRLLEILGEG------YP-NNLRCILLGGGPAPKPLLEQCKEK-G 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 405 IKCLRVYGQSEigvtSFISVHALNIPYRAT-----GVPSIYIRPSILSEEGevlNSNEIGLVAFKLPMppsfaIT--FYK 477
Cdd:cd05912 214 IPVYQSYGMTE----TCSQIVTLSPEDALNkigsaGKPLFPVELKIEDDGQ---PPYEVGEILLKGPN-----VTkgYLN 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 478 NDEKFKQLFTRfpGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGILSPDCRTAPI 557
Cdd:cd05912 282 RPDATEESFEN--GWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPV 359
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 66822211 558 GILVLKENPSidlnklQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:cd05912 360 AFVVSERPIS------EEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
256-608 |
5.67e-17 |
|
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: 83.58 E-value: 5.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 256 PLYILYTSGTTGNTKAVVRSNGPHMVGIKYYTFRKESDIPQIVFSNANIGwvSFHGFFYGLlsggnTLVMYEGGIIkneh 335
Cdd:cd05903 95 VALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFLVASPMA--HQTGFVYGF-----TLPLLLGAPV---- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 336 IEDDLW-----IAIVK-HKVTHTFPSPSVFRYLIKTdPEgtivRSKYDLSNLKEIWCGGEVIEESIPEYIEQKLKIKCLR 409
Cdd:cd05903 164 VLQDIWdpdkaLALMReHGVTFMMGATPFLTDLLNA-VE----EAGEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCS 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 410 VYGQSEIG--VTSFISVHALNIpYRATGVPSIYIRPSILSEEGEVLNSNEIGLVAFKlpmPPSFAITFYKNDEKFKQLFT 487
Cdd:cd05903 239 AYGSTECPgaVTSITPAPEDRR-LYTDGRPLPGVEIKVVDDTGATLAPGVEGELLSR---GPSVFLGYLDRPDLTADAAP 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 488 RfpGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGIlsPDCRTAP--IGILVLKEN 565
Cdd:cd05903 315 E--GWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVAL--PDERLGEraCAVVVTKSG 390
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 66822211 566 PSIDLNKLQNEINNiitQDIESLAVLKKIIVINQLPKTKVGKI 608
Cdd:cd05903 391 ALLTFDELVAYLDR---QGVAKQYWPERLVHVDDLPRTPSGKV 430
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
70-608 |
5.85e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 84.21 E-value: 5.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 70 KNPAKRdqdALIYEcpylkkTIKLTYYQLYEKVCKFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGAtqctlfd 149
Cdd:PRK08316 23 RYPDKT---ALVFG------DRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGA------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 150 gysvkslidrietitpkLIITTNYGIFNDEII---------------TFTPNLKEAIELSTFKPSnVITLFRNEVLDETK 214
Cdd:PRK08316 87 -----------------VHVPVNFMLTGEELAyildhsgaraflvdpALAPTAEAALALLPVDTL-ILSLVLGGREAPGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 215 LKKVqniptipntLSWYDeikklkenNQSPFYEYVPVESSHPLYILYTSGTTGNTKAVVRSNGPHM-------VGIKYyt 287
Cdd:PRK08316 149 WLDF---------ADWAE--------AGSVAEPDVELADDDLAQILYTSGTESLPKGAMLTHRALIaeyvsciVAGDM-- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 288 frKESDIPQI---VFSNAnigwvSFHGFFYGLLSGGNTLVMYEGGIIKN--EHIEddlwiaivKHKVTHTFPSPSVFRYL 362
Cdd:PRK08316 210 --SADDIPLHalpLYHCA-----QLDVFLGPYLYVGATNVILDAPDPELilRTIE--------AERITSFFAPPTVWISL 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 363 IktdpegtivRS----KYDLSNLKEIWCG-----GEVIEEsipeyIEQKL-KIKCLRVYGQSEIGvtsfisvhalniPYr 432
Cdd:PRK08316 275 L---------RHpdfdTRDLSSLRKGYYGasimpVEVLKE-----LRERLpGLRFYNCYGQTEIA------------PL- 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 433 AT--------------GVPSIYIRPSILSEEGEVLNSNEIGLVAFKlpmPPSFAITFYKNDEKFKQLFTrfPGYYDSGDL 498
Cdd:PRK08316 328 ATvlgpeehlrrpgsaGRPVLNVETRVVDDDGNDVAPGEVGEIVHR---SPQLMLGYWDDPEKTAEAFR--GGWFHSGDL 402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 499 GYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGIlsPDCR-----TApigILVLKENPSIDLNKL 573
Cdd:PRK08316 403 GVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGL--PDPKwieavTA---VVVPKAGATVTEDEL 477
|
570 580 590
....*....|....*....|....*....|....*...
gi 66822211 574 qneinniITQDIESLA---VLKKIIVINQLPKTKVGKI 608
Cdd:PRK08316 478 -------IAHCRARLAgfkVPKRVIFVDELPRNPSGKI 508
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
253-617 |
8.91e-17 |
|
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: 83.36 E-value: 8.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 253 SSHPLYILYTSGTTGNTKAVVRSNGPHMVGIKYYT----FRKESDIPQivFSNANIGwVSFHGFFYGLLSGGnTLVmyeg 328
Cdd:cd05918 105 PSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGralgLTSESRVLQ--FASYTFD-VSILEIFTTLAAGG-CLC---- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 329 gIIKNEHIEDDLWIAIVKHKVTHTFPSPSVFRYLiktDPEgtivrskyDLSNLKEIWCGGEVIEESIpeyIEQ-KLKIKC 407
Cdd:cd05918 177 -IPSEEDRLNDLAGFINRLRVTWAFLTPSVARLL---DPE--------DVPSLRTLVLGGEALTQSD---VDTwADRVRL 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 408 LRVYGQSE--IGVTSFISV---HALNI--PYRATGV---PSIYIRPSILSEEGEVLNS---------NEIGLVAFKLPMP 468
Cdd:cd05918 242 INAYGPAEctIAATVSPVVpstDPRNIgrPLGATCWvvdPDNHDRLVPIGAVGELLIEgpilargylNDPEKTAAAFIED 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 469 PSFAITFYKNDekfkqlFTRFpgyYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGIL 548
Cdd:cd05918 322 PAWLKQEGSGR------GRRL---YRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEVV 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 549 SPDCRTAP---IGILVLKE-----NPSIDLNKLQNEINNIITQDIESLA--------VLKKIIVINQLPKTKVGKIPRQI 612
Cdd:cd05918 393 KPKDGSSSpqlVAFVVLDGsssgsGDGDSLFLEPSDEFRALVAELRSKLrqrlpsymVPSVFLPLSHLPLTASGKIDRRA 472
|
....*
gi 66822211 613 LSNLL 617
Cdd:cd05918 473 LRELA 477
|
|
| ACAS_N |
pfam16177 |
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many ... |
16-63 |
9.55e-17 |
|
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: 74.43 E-value: 9.55e-17
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 66822211 16 YSNSNPEAFWDEVAKKnVFWEKMYDKVYSGDE-IYPDWFKGGELNTCYN 63
Cdd:pfam16177 7 RSIEDPEGFWGEVAKE-LDWFKPFDKVLDGSNgPFAKWFVGGKLNVCYN 54
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
94-543 |
1.05e-16 |
|
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: 82.70 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 94 TYYQLYEKVCKFSRVLLNL-NVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGYSVksliDRIETI----TPKLI 168
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPA----ERLAFIledaGARLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 169 ITTnygifndeiitftPNLKEAIELSTFKPSNVITLFRNEVLDETKLKKVQniptipntlswydeikklkennqspfyey 248
Cdd:TIGR01733 77 LTD-------------SALASRLAGLVLPVILLDPLELAALDDAPAPPPPD----------------------------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 249 VPVESSHPLYILYTSGTTGNTKAVV---RSNGPHMVGIKYYTFRKESDipqIVFSNANIGW-VSFHGFFYGLLSGGNTLV 324
Cdd:TIGR01733 115 APSGPDDLAYVIYTSGSTGRPKGVVvthRSLVNLLAWLARRYGLDPDD---RVLQFASLSFdASVEEIFGALLAGATLVV 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 325 MYEGgiikNEHIEDDLW-IAIVKHKVTHTFPSPSVFRYLIKTDPEgtivrskyDLSNLKEIWCGGEVIE-ESIPEYIEQK 402
Cdd:TIGR01733 192 PPED----EERDDAALLaALIAEHPVTVLNLTPSLLALLAAALPP--------ALASLRLVILGGEALTpALVDRWRARG 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 403 LKIKCLRVYGQSE--IGVTSFISVHALNIPYRAT--GVP----SIYirpsILSEEGEVLNSNEIG--LVAfklpmPPSFA 472
Cdd:TIGR01733 260 PGARLINLYGPTEttVWSTATLVDPDDAPRESPVpiGRPlantRLY----VLDDDLRPVPVGVVGelYIG-----GPGVA 330
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66822211 473 ITFYKNDEKFKQLFTRFPGY-------YDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECC 543
Cdd:TIGR01733 331 RGYLNRPELTAERFVPDPFAggdgarlYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAV 408
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
92-616 |
2.24e-16 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 82.76 E-value: 2.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 92 KLTYYQLYEKVCKFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQC---TLFDGYSVKSLIDRIEtitPKLI 168
Cdd:PLN03102 39 RFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNpinTRLDATSIAAILRHAK---PKIL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 169 ittnygiFNDEiiTFTPNLKEAIELSTFKPS--NVITLFRNEVlDETKLKKVQNIPtipntlswYDEIKKLKENNQSPFY 246
Cdd:PLN03102 116 -------FVDR--SFEPLAREVLHLLSSEDSnlNLPVIFIHEI-DFPKRPSSEELD--------YECLIQRGEPTPSLVA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 247 EYVPVESSH-PLYILYTSGTTGNTKAVVRSN-GPHMVGIKYYTFRKESDIPQIVFS----NANiGWVsfhgFFYGLLSGG 320
Cdd:PLN03102 178 RMFRIQDEHdPISLNYTSGTTADPKGVVISHrGAYLSTLSAIIGWEMGTCPVYLWTlpmfHCN-GWT----FTWGTAARG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 321 NTLVMYEggiikneHIE-DDLWIAIVKHKVTHTFPSPSVFRYLIKTDpegtivrsKYDLSNLK---EIWCGGEVIEESIP 396
Cdd:PLN03102 253 GTSVCMR-------HVTaPEIYKNIEMHNVTHMCCVPTVFNILLKGN--------SLDLSPRSgpvHVLTGGSPPPAALV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 397 EYIEQkLKIKCLRVYGQSE-IGVTSFISVHAL--NIP------------YRATGVPSIYIRpSILSEEGEVLNSNEIGLV 461
Cdd:PLN03102 318 KKVQR-LGFQVMHAYGLTEaTGPVLFCEWQDEwnRLPenqqmelkarqgVSILGLADVDVK-NKETQESVPRDGKTMGEI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 462 AFKlpmPPSFAITFYKNDEKFKQLFTRfpGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLE 541
Cdd:PLN03102 396 VIK---GSSIMKGYLKNPKATSEAFKH--GWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLE 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 542 CCSIGILSPDCRTAPIGILVLK---ENPSIDLNKLQNEINNIIT---QDIESLAVLKKIIVINQLPKTKVGKIPRQILSN 615
Cdd:PLN03102 471 TAVVAMPHPTWGETPCAFVVLEkgeTTKEDRVDKLVTRERDLIEycrENLPHFMCPRKVVFLQELPKNGNGKILKPKLRD 550
|
.
gi 66822211 616 L 616
Cdd:PLN03102 551 I 551
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
250-618 |
2.29e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 82.24 E-value: 2.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 250 PVESSHPLYILYTSGTTGNTKAVVRSNGphmvgikyytfrkesdipqivfsnaNIGWVSF-HGFFYGLLSGGNTLV---- 324
Cdd:PRK06145 145 AVAPTDLVRLMYTSGTTDRPKGVMHSYG-------------------------NLHWKSIdHVIALGLTASERLLVvgpl 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 325 -------------MYEGGIIKNEHIED--DLWIAIVKHKVTHTFPSPsVFRYLIKTDPEgtivRSKYDLSNLKeiWC--G 387
Cdd:PRK06145 200 yhvgafdlpgiavLWVGGTLRIHREFDpeAVLAAIERHRLTCAWMAP-VMLSRVLTVPD----RDRFDLDSLA--WCigG 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 388 GEVIEES-IPEYIEQKLKIKCLRVYGQSE-IGVTSFISVHALNIPYRATGVPSIYIRPSILSEEGEVLNSNEIGLVAFKl 465
Cdd:PRK06145 273 GEKTPESrIRDFTRVFTRARYIDAYGLTEtCSGDTLMEAGREIEKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMR- 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 466 pmPPSFAITFYKNDEKFKQLFtrFPGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSI 545
Cdd:PRK06145 352 --GPKVTKGYWKDPEKTAEAF--YGDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVI 427
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66822211 546 GILSPDCRTAPIGILVLKENPSIDLNKLQNEINniitQDIESLAVLKKIIVINQLPKTKVGKIPRQILSNLLN 618
Cdd:PRK06145 428 GVHDDRWGERITAVVVLNPGATLTLEALDRHCR----QRLASFKVPRQLKVRDELPRNPSGKVLKRVLRDELN 496
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
317-608 |
3.21e-16 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 82.31 E-value: 3.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 317 LSGGNTLVMYEGGIIKNEHIEDDLWIAIVKHKVTHTFPSPSVFRYLIKTDPEGtivrskYDLSNLKEIWCGGEVIEESIP 396
Cdd:PRK07529 277 LARGAHVVLATPQGYRGPGVIANFWKIVERYRINFLSGVPTVYAALLQVPVDG------HDISSLRYALCGAAPLPVEVF 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 397 EYIEQKLKIKCLRVYGqseigVTSFISVHALNIPYRATGVPSIYIR-P------SILSEEGEVLNS---NEIGLVAFKLP 466
Cdd:PRK07529 351 RRFEAATGVRIVEGYG-----LTEATCVSSVNPPDGERRIGSVGLRlPyqrvrvVILDDAGRYLRDcavDEVGVLCIAGP 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 467 MppsfaiTF--YKNDEKFKQLFTrFPGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCS 544
Cdd:PRK07529 426 N------VFsgYLEAAHNKGLWL-EDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAA 498
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66822211 545 IGilSPDCRTA--PIGILVLKENPSIDLNKLQNEINNIITqdiESLAVLKKIIVINQLPKTKVGKI 608
Cdd:PRK07529 499 VG--RPDAHAGelPVAYVQLKPGASATEAELLAFARDHIA---ERAAVPKHVRILDALPKTAVGKI 559
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
254-610 |
6.90e-16 |
|
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: 79.23 E-value: 6.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 254 SHPLYILYTSGTTGNTKAVVRSNGphmvgikyyTFRKESDIPQIVFSNANIGWVSF---HGFFYGLLSGGNTLVMYEGGI 330
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANK---------TFFAVPDILQKEGLNWVVGDVTYlplPATHIGGLWWILTCLIHGGLC 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 331 I--KNEHIEDDLWIAIVKHKVTHTFPSPSVFRYLIkTDPEGTIVRSKydlsNLKEIWCGGEVIEESIPEYIEQKLKIKCL 408
Cdd:cd17635 72 VtgGENTTYKSLFKILTTNAVTTTCLVPTLLSKLV-SELKSANATVP----SLRLIGYGGSRAIAADVRFIEATGLTNTA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 409 RVYGQSEIGVTSFISVHALNIPYRATGVPSIYIRPSILSEEGEVLNSNEIGLVAFKlpmPPSFAITFYKNDEKFKQLFTR 488
Cdd:cd17635 147 QVYGLSETGTALCLPTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIK---SPANMLGYWNNPERTAEVLID 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 489 fpGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGIlsPDCRTAPIGILVLKENPSI 568
Cdd:cd17635 224 --GWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEI--SDEEFGELVGLAVVASAEL 299
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 66822211 569 DLNKLQNEINNIITQdIESLAVLKKIIVINQLPKTKVGKIPR 610
Cdd:cd17635 300 DENAIRALKHTIRRE-LEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
253-610 |
7.48e-16 |
|
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: 80.30 E-value: 7.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 253 SSHPLYILYTSGTTGNTKAVVRSNGPHMVG---IKYYTFRKESDIPQIVFSNaniGWVSfHGF--FYGLLSGGNTLVMYe 327
Cdd:cd05974 84 ADDPMLLYFTSGTTSKPKLVEHTHRSYPVGhlsTMYWIGLKPGDVHWNISSP---GWAK-HAWscFFAPWNAGATVFLF- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 328 ggiikNEHIEDD--LWIAIVKHKVTHTFPSPSVFRYLIKTDPEGTIVRskydlsnLKEIWCGGEVIEesiPEYIEQKLKI 405
Cdd:cd05974 159 -----NYARFDAkrVLAALVRYGVTTLCAPPTVWRMLIQQDLASFDVK-------LREVVGAGEPLN---PEVIEQVRRA 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 406 KCLRV---YGQSEIgvtsfiSVHALNIPYR-----ATGVPSIYIRPSILSEEGEVLNSNEIGLVAFKlpMPPSFAITFYK 477
Cdd:cd05974 224 WGLTIrdgYGQTET------TALVGNSPGQpvkagSMGRPLPGYRVALLDPDGAPATEGEVALDLGD--TRPVGLMKGYA 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 478 NDEKfKQLFTRFPGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGILSPDCRTAPI 557
Cdd:cd05974 296 GDPD-KTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPK 374
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 66822211 558 GILVLKE--NPSIDLNKlqneinNIITQDIESLAVLKKI--IVINQLPKTKVGKIPR 610
Cdd:cd05974 375 AFIVLRAgyEPSPETAL------EIFRFSRERLAPYKRIrrLEFAELPKTISGKIRR 425
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
91-613 |
2.06e-15 |
|
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: 79.09 E-value: 2.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 91 IKLTYYQLYEKVCKFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGAtqctlfdgysVKSLIDrietitPKL-II 169
Cdd:cd05923 27 LRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGA----------VPALIN------PRLkAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 170 TTNYGIFNDEIIT-FTPNLKEAIELSTFKPSNVITLfrnEVLDETKlkkvqnIPTipntlswydeikklkenNQSPFYEY 248
Cdd:cd05923 91 ELAELIERGEMTAaVIAVDAQVMDAIFQSGVRVLAL---SDLVGLG------EPE-----------------SAGPLIED 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 249 VPVESSHPLYILYTSGTTGNTKAVV---RSNGPHMVGIkyytfrkeSDIPQIVFSNAN--IGW------VSFHGFFYGLL 317
Cdd:cd05923 145 PPREPEQPAFVFYTSGTTGLPKGAVipqRAAESRVLFM--------STQAGLRHGRHNvvLGLmplyhvIGFFAVLVAAL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 318 SGGNTLVMYEggiiknehiEDDLWIA---IVKHKVTHTFPSPSVFRYLIktdpeGTIVRSKYDLSNLKEIWCGGEVIEES 394
Cdd:cd05923 217 ALDGTYVVVE---------EFDPADAlklIEQERVTSLFATPTHLDALA-----AAAEFAGLKLSSLRHVTFAGATMPDA 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 395 IPEYIEQKLKIKCLRVYGQSEIgvtsFISVHALNIPYRATGVPSIYIR---PSILSEEGEVLNSNEIGLVAFKLPMPPSF 471
Cdd:cd05923 283 VLERVNQHLPGEKVNIYGTTEA----MNSLYMRDARTGTEMRPGFFSEvriVRIGGSPDEALANGEEGELIVAAAADAAF 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 472 aiTFYKNDEKFKQLFTRFpGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGIlsPD 551
Cdd:cd05923 359 --TGYLNQPEATAKKLQD-GWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGV--AD 433
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66822211 552 CRTAPIGILVLKENPSidlNKLQNEINNI-ITQDIESLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:cd05923 434 ERWGQSVTACVVPREG---TLSADELDQFcRASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
94-627 |
3.72e-15 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 78.64 E-value: 3.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 94 TYYQLYEKVCKFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATqctlfdgysvkslidrIETITPKLIITTNY 173
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAI----------------CHTVNPRLFPEQIA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 174 GIFN---DEII----TFTPNLkEAIELSTFKPSNVITLFRNEVLDETklkkvqnipTIPNTLSWYDEIKKLKENnqspfY 246
Cdd:PRK06018 105 WIINhaeDRVVitdlTFVPIL-EKIADKLPSVERYVVLTDAAHMPQT---------TLKNAVAYEEWIAEADGD-----F 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 247 EYVPVESSHPLYILYTSGTTGNTKAVV---RSN--------GPHMVGIKyytfRKESDIPQIVFSNANiGWvsfhGFFYG 315
Cdd:PRK06018 170 AWKTFDENTAAGMCYTSGTTGDPKGVLyshRSNvlhalmanNGDALGTS----AADTMLPVVPLFHAN-SW----GIAFS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 316 LLSGGNTLVMyEGGIIKNEHIEDDLwiaiVKHKVTHTFPSPSVFRYLIKTdpegtIVRSKYDLSNLKEIWCGGEVIEESI 395
Cdd:PRK06018 241 APSMGTKLVM-PGAKLDGASVYELL----DTEKVTFTAGVPTVWLMLLQY-----MEKEGLKLPHLKMVVCGGSAMPRSM 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 396 PEYIEqKLKIKCLRVYGQSE---IGVTSFISVHALNIPYRA-------TGVPSIYIRPSILSEEGEVLNSNeiGLVAFKL 465
Cdd:PRK06018 311 IKAFE-DMGVEVRHAWGMTEmspLGTLAALKPPFSKLPGDArldvlqkQGYPPFGVEMKITDDAGKELPWD--GKTFGRL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 466 PMP-PSFAITFYKNDEKfkQLFTRfpGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCS 544
Cdd:PRK06018 388 KVRgPAVAAAYYRVDGE--ILDDD--GFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAV 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 545 IGILSPDCRTAPIGILVLKEnpsiDLNKLQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQILSNLLNDpnYQL 624
Cdd:PRK06018 464 IGVYHPKWDERPLLIVQLKP----GETATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALREQFKD--YKL 537
|
...
gi 66822211 625 PDD 627
Cdd:PRK06018 538 PTA 540
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
94-615 |
1.29e-14 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 77.10 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 94 TYYQLYEKVCKFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGYSVKSLIDRIET------ITPKL 167
Cdd:PRK06087 51 TYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKcqakmfFAPTL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 168 IITTNYGIFNDEIITFTPNLKEAIELSTFKPSNvitlfrnevldetklkkvqniptipNTLSwydeIKKLKENNQsPFYE 247
Cdd:PRK06087 131 FKQTRPVDLILPLQNQLPQLQQIVGVDKLAPAT-------------------------SSLS----LSQIIADYE-PLTT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 248 YVPVESSHPLYILYTSGTTGNTKAVVRSNGPHMVGIKYYTFRKESDIPQIVFSNANIGWVSfhGFFYGLlsggnTLVMYE 327
Cdd:PRK06087 181 AITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHAT--GFLHGV-----TAPFLI 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 328 GG-IIKNEHIEDDLWIAIV-KHKVTHTF-PSPSVFRYLiktdpeGTIVRSKYDLSNLKEIWCGGEVIEESIPEYIEQKlK 404
Cdd:PRK06087 254 GArSVLLDIFTPDACLALLeQQRCTCMLgATPFIYDLL------NLLEKQPADLSALRFFLCGGTTIPKKVARECQQR-G 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 405 IKCLRVYGQSEIGVTSFISVH---ALNIPYRATGVPSIYIRpsILSEEGEVLNSNEIGLVAFKLPMppsfaiTF--YKND 479
Cdd:PRK06087 327 IKLLSVYGSTESSPHAVVNLDdplSRFMHTDGYAAAGVEIK--VVDEARKTLPPGCEGEEASRGPN------VFmgYLDE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 480 ekfKQLFTRF---PGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGIlsPDCRTAP 556
Cdd:PRK06087 399 ---PELTARAldeEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAM--PDERLGE 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66822211 557 --IGILVLKENPSIDlnKLQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQILSN 615
Cdd:PRK06087 474 rsCAYVVLKAPHHSL--TLEEVVAFFSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
251-617 |
1.76e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 76.62 E-value: 1.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 251 VESSHPLYILYTSGTTGNTKAVVRSNGP-------HMVGIKYYTfrKESDIPQIV--FSnanigwvsfHGffygllSGGN 321
Cdd:PRK07470 160 VDHDDPCWFFFTSGTTGRPKAAVLTHGQmafvitnHLADLMPGT--TEQDASLVVapLS---------HG------AGIH 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 322 TLVMYEGG----IIKNEHIE-DDLWIAIVKHKVTHTFPSPSVFRYLIKtDPEgtivRSKYDLSNLKEiwcggeVIEESIP 396
Cdd:PRK07470 223 QLCQVARGaatvLLPSERFDpAEVWALVERHRVTNLFTVPTILKMLVE-HPA----VDRYDHSSLRY------VIYAGAP 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 397 EYIE-QKLKIKCL-----RVYGQSEigVTSFISV-----HAL----NIPYRATGVPSIYIRPSILSEEGEVLNSNEIGLV 461
Cdd:PRK07470 292 MYRAdQKRALAKLgkvlvQYFGLGE--VTGNITVlppalHDAedgpDARIGTCGFERTGMEVQIQDDEGRELPPGETGEI 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 462 AFKlpMPPSFAiTFYKNDEKFKQLFTRfpGYYDSGDLGYIDQRGFYTIVSRSDDqIKIS-CNKIQLNTIDTSILKHPSVL 540
Cdd:PRK07470 370 CVI--GPAVFA-GYYNNPEANAKAFRD--GWFRTGDLGHLDARGFLYITGRASD-MYISgGSNVYPREIEEKLLTHPAVS 443
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66822211 541 ECCSIGIlsPDCRTAPIGI--LVLKENPSIDlnklQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQILSNLL 617
Cdd:PRK07470 444 EVAVLGV--PDPVWGEVGVavCVARDGAPVD----EAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVREEL 516
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
259-617 |
2.04e-14 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 76.42 E-value: 2.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 259 ILYTSGTTGNTKAVVRSNGPHMVGIKYYTFRKESDIPQIVFSNANIGWVS-FHG-----FFYGLLSGGNTLVmyeggiIK 332
Cdd:PLN02574 203 IMYSSGTTGASKGVVLTHRNLIAMVELFVRFEASQYEYPGSDNVYLAALPmFHIyglslFVVGLLSLGSTIV------VM 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 333 NEHIEDDLWIAIVKHKVTHtFPS-PSVFRYLIK-TDPEGTIVrskydLSNLKEIWCGGE-VIEESIPEYIEQKLKIKCLR 409
Cdd:PLN02574 277 RRFDASDMVKVIDRFKVTH-FPVvPPILMALTKkAKGVCGEV-----LKSLKQVSCGAApLSGKFIQDFVQTLPHVDFIQ 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 410 VYGQSE---IGVTSFISVHALNipYRATGVPSIYIRPSILS-EEGEVLNSNEIGLVAFKLPMppsfAITFYKNDEKFKQL 485
Cdd:PLN02574 351 GYGMTEstaVGTRGFNTEKLSK--YSSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGPG----VMKGYLNNPKATQS 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 486 FTRFPGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGILSPDCRTAPIGILVLKEN 565
Cdd:PLN02574 425 TIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQG 504
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 66822211 566 PSIDlnklQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQILSNLL 617
Cdd:PLN02574 505 STLS----QEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRSL 552
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
93-613 |
2.16e-14 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 76.45 E-value: 2.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 93 LTYYQLYEKVCKFSRVLLN-LNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGYSVKSLIDR-IETITPKLIIT 170
Cdd:PRK08751 51 ITYREADQLVEQFAAYLLGeLQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQlIDSGASVLVVI 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 171 TNYGIFNDEIITFTPnLKEAI-----ELSTFKPSNVITLFRNEVldetklKKVQNIPTIPNTLSWYDEIKKLKENNQSPf 245
Cdd:PRK08751 131 DNFGTTVQQVIADTP-VKQVIttglgDMLGFPKAALVNFVVKYV------KKLVPEYRINGAIRFREALALGRKHSMPT- 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 246 yeyVPVESSHPLYILYTSGTTGNTKAVV---RSNGPHMVGIKYY--TFRKESDIPQIVFSNANIgwvsFHGFfygLLSGG 320
Cdd:PRK08751 203 ---LQIEPDDIAFLQYTGGTTGVAKGAMlthRNLVANMQQAHQWlaGTGKLEEGCEVVITALPL----YHIF---ALTAN 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 321 NTLVMYEGG---IIKNEHIEDDLWIAIVKHKVTHTFPSPSVFRYLIKTDPEGTIvrskyDLSNLKEIWCGGEVIEESIPE 397
Cdd:PRK08751 273 GLVFMKIGGcnhLISNPRDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQI-----DFSSLKMTLGGGMAVQRSVAE 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 398 YIEQKLKIKCLRVYGQSEIGVTSFISVHALNIPYRATGVPSIYIRPSILSEEGEVLNSNEIGLVAFKlpmPPSFAITFYK 477
Cdd:PRK08751 348 RWKQVTGLTLVEAYGLTETSPAACINPLTLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIK---GPQVMKGYWK 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 478 NDEKFKQLFTRfPGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGIlsPDCRTAPI 557
Cdd:PRK08751 425 RPEETAKVMDA-DGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGV--PDEKSGEI 501
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 558 -GILVLKENPSIDLNKLQNEINNIITQdieslavLKKIIVIN---QLPKTKVGKIPRQIL 613
Cdd:PRK08751 502 vKVVIVKKDPALTAEDVKAHARANLTG-------YKQPRIIEfrkELPKTNVGKILRREL 554
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
92-608 |
4.47e-14 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 75.09 E-value: 4.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 92 KLTYYQLYEKVCKFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGAtqctlfdgysvkslidrietITPKLIItt 171
Cdd:PRK13295 55 RFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGA--------------------VLNPLMP-- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 172 nygIFNDEIITFTPNLKEAielstfKPSNVITLFRN----EVLDETK--LKKVQNIPTI----PNTLSwydeiKKLKEnn 241
Cdd:PRK13295 113 ---IFRERELSFMLKHAES------KVLVVPKTFRGfdhaAMARRLRpeLPALRHVVVVggdgADSFE-----ALLIT-- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 242 qsPFYEYVP-----VESSHP-----LYILYTSGTTGNTKAVVRSNGPHMVGIKYYTFRKESDIPQIVFSNANIGwvsfH- 310
Cdd:PRK13295 177 --PAWEQEPdapaiLARLRPgpddvTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMA----Hq 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 311 -GFFYGL---LSGGNTLVMyeggiiknehieDDLW-----IAIVK-HKVTHTFPSPSVFrylikTDPEGTIVRSKYDLSN 380
Cdd:PRK13295 251 tGFMYGLmmpVMLGATAVL------------QDIWdparaAELIRtEGVTFTMASTPFL-----TDLTRAVKESGRPVSS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 381 LKEIWCGGEVIEESIPEYIEQKLKIKCLRVYGQSEIG-VTSFISVHALNIPYRATGVPSIYIRPSILSEEGEVLNSNEIG 459
Cdd:PRK13295 314 LRTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGaVTLTKLDDPDERASTTDGCPLPGVEVRVVDADGAPLPAGQIG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 460 lvAFKLPMPPSFAITFykndeKFKQLF-TRFPGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPS 538
Cdd:PRK13295 394 --RLQVRGCSNFGGYL-----KRPQLNgTDADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPA 466
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66822211 539 VLECCSIGIlsPDCRTA--PIGILVLKENPSIDLNKLQNEINniiTQDIESLAVLKKIIVINQLPKTKVGKI 608
Cdd:PRK13295 467 IAQVAIVAY--PDERLGerACAFVVPRPGQSLDFEEMVEFLK---AQKVAKQYIPERLVVRDALPRTPSGKI 533
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
92-618 |
9.43e-14 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 73.84 E-value: 9.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 92 KLTYYQLYEKVCKFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGYSVKSLIDRIETITPKLIITT 171
Cdd:PRK03640 27 KVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLITD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 172 nygifndeiitftpnlkeaielstfkpsnvitlfrnevlDETKLKKVQNIPTIpntlswYDEIKKLKENNQSPfYEYVPV 251
Cdd:PRK03640 107 ---------------------------------------DDFEAKLIPGISVK------FAELMNGPKEEAEI-QEEFDL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 252 ESShpLYILYTSGTTGNTKAVVRSNGPHmvgikYYTfrkesdipqIVFSNANIG------WVS----FHgffyglLSGGN 321
Cdd:PRK03640 141 DEV--ATIMYTSGTTGKPKGVIQTYGNH-----WWS---------AVGSALNLGlteddcWLAavpiFH------ISGLS 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 322 TL---VMYEGGIIKNEHI-EDDLWIAIVKHKVTHTFPSPSVFRYLIKTDPEGTivrskYDlSNLKEIWCGGEVIEESIPE 397
Cdd:PRK03640 199 ILmrsVIYGMRVVLVEKFdAEKINKLLQTGGVTIISVVSTMLQRLLERLGEGT-----YP-SSFRCMLLGGGPAPKPLLE 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 398 YIEQKlKIKCLRVYGQSEigvTSfISVHALNIPYRATGVPS---------IYIRpsilsEEGEVLNSNEIGLVAFKLPMp 468
Cdd:PRK03640 273 QCKEK-GIPVYQSYGMTE---TA-SQIVTLSPEDALTKLGSagkplfpceLKIE-----KDGVVVPPFEEGEIVVKGPN- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 469 psfaIT--FYKNDEKFKQLFTRfpGYYDSGDLGYIDQRGFYTIVSRSDDQIkISCNK-IQLNTIDTSILKHPSVLECCSI 545
Cdd:PRK03640 342 ----VTkgYLNREDATRETFQD--GWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGEnIYPAEIEEVLLSHPGVAEAGVV 414
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66822211 546 GIlsPDCR--TAPIGILVLKENPSidlnklQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQILSNLLN 618
Cdd:PRK03640 415 GV--PDDKwgQVPVAFVVKSGEVT------EEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQLVE 481
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
222-541 |
1.02e-13 |
|
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: 73.92 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 222 PTIPNTLSWYDEIKKLKENNQSPFyeyVPVESSHPLYILYTSGTTGNTKAVVRSNGPHMVGIKYYTFRKESDIPQIVFSN 301
Cdd:cd17651 107 AVELVAVTLLDQPGAAAGADAEPD---PALDADDLAYVIYTSGSTGRPKGVVMPHRSLANLVAWQARASSLGPGARTLQF 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 302 ANIGW-VSFHGFFYGLLSGGnTLVmyeggiIKNEHIEDD---LWIAIVKHKVTHTFPSPSVFRYLIK-TDPEGTIvrsky 376
Cdd:cd17651 184 AGLGFdVSVQEIFSTLCAGA-TLV------LPPEEVRTDppaLAAWLDEQRISRVFLPTVALRALAEhGRPLGVR----- 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 377 dLSNLKEIWCGGE--VIEESIPEYIEqklKIKCLRV---YGQSEigvTSFISVHAL-NIPYRATGVPSI---------YI 441
Cdd:cd17651 252 -LAALRYLLTGGEqlVLTEDLREFCA---GLPGLRLhnhYGPTE---THVVTALSLpGDPAAWPAPPPIgrpidntrvYV 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 442 -----RPSILSEEGEvLNSNEIGLVAFKLPMPPSFAITFYKNDEKFKQLftrfpgYYDSGDLGYIDQRGFYTIVSRSDDQ 516
Cdd:cd17651 325 ldaalRPVPPGVPGE-LYIGGAGLARGYLNRPELTAERFVPDPFVPGAR------MYRTGDLARWLPDGELEFLGRADDQ 397
|
330 340
....*....|....*....|....*
gi 66822211 517 IKISCNKIQLNTIDTSILKHPSVLE 541
Cdd:cd17651 398 VKIRGFRIELGEIEAALARHPGVRE 422
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
90-624 |
1.17e-13 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 73.89 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 90 TIKLTYYQLYEKVCKFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATqCTLFDGYSVKSLIDRIETITpklii 169
Cdd:PRK05857 39 TSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAI-AVMADGNLPIAAIERFCQIT----- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 170 ttnygifndeiitftpnlkeaielstfKPSNVITLFRNEVLDETKLKKVQNIPTIPntlswYDEIKKLKENNQSPFYEYV 249
Cdd:PRK05857 113 ---------------------------DPAAALVAPGSKMASSAVPEALHSIPVIA-----VDIAAVTRESEHSLDAASL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 250 PVE----SSHPLYILYTSGTTGNTKAVVRSNgphmvgikyytfRKESDIPQIVfSNANIGWVSF-------------H-G 311
Cdd:PRK05857 161 AGNadqgSEDPLAMIFTSGTTGEPKAVLLAN------------RTFFAVPDIL-QKEGLNWVTWvvgettysplpatHiG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 312 FFYGLLSGgntlVMYEGGIIKNEHIEDDLWIAIVKHKVTHTFPSPSVFRYLIKTDPEGTIvrskyDLSNLKEIWCGGEVI 391
Cdd:PRK05857 228 GLWWILTC----LMHGGLCVTGGENTTSLLEILTTNAVATTCLVPTLLSKLVSELKSANA-----TVPSLRLVGYGGSRA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 392 EESIPEYIEQKlKIKCLRVYGQSEIGVTSF-----------ISVHALNIPYraTGVpSIYIRPsilsEEG------EVLN 454
Cdd:PRK05857 299 IAADVRFIEAT-GVRTAQVYGLSETGCTALclptddgsivkIEAGAVGRPY--PGV-DVYLAA----TDGigptapGAGP 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 455 SNEIGLVAFKlpmPPSFAITFYKNDEKFKQLFTRfpGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSIL 534
Cdd:PRK05857 371 SASFGTLWIK---SPANMLGYWNNPERTAEVLID--GWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAE 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 535 KHPSVLECCSIGIlsPDcrtAPIGILV-LKENPSIDLN-----KLQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKI 608
Cdd:PRK05857 446 GVSGVREAACYEI--PD---EEFGALVgLAVVASAELDesaarALKHTIAARFRRESEPMARPSTIVIVTDIPRTQSGKV 520
|
570
....*....|....*.
gi 66822211 609 PRQILSNLLNDPNYQL 624
Cdd:PRK05857 521 MRASLAAAATADKARV 536
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
249-543 |
1.74e-13 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 74.12 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 249 VPVESSHPLYILYTSGTTGNTKAVVRSNGP---HMVGI-KYYTFRKESDIPQIvfsnANIGW-VSFHGFFYGLLSGGnTL 323
Cdd:COG1020 612 VPVTPDDLAYVIYTSGSTGRPKGVMVEHRAlvnLLAWMqRRYGLGPGDRVLQF----ASLSFdASVWEIFGALLSGA-TL 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 324 VMYEGGIIKNEhieDDLWIAIVKHKVTHTFPSPSVFRYLIKTDPEgtivrskyDLSNLKEIWCGGEVIEESIPEYIEQKL 403
Cdd:COG1020 687 VLAPPEARRDP---AALAELLARHRVTVLNLTPSLLRALLDAAPE--------ALPSLRLVLVGGEALPPELVRRWRARL 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 404 kiKCLRV---YGQSEIGVTSfiSVHALNIPYRATGVPSI---------YI-----RPSILSEEGEVLnsneIG--LVA-- 462
Cdd:COG1020 756 --PGARLvnlYGPTETTVDS--TYYEVTPPDADGGSVPIgrpiantrvYVldahlQPVPVGVPGELY----IGgaGLArg 827
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 463 -FKLPmppsfAITfyknDEKFKQLFTRFPG--YYDSGDLGYIDQRGfyTI--VSRSDDQIKISCNKIQLNTIDTSILKHP 537
Cdd:COG1020 828 yLNRP-----ELT----AERFVADPFGFPGarLYRTGDLARWLPDG--NLefLGRADDQVKIRGFRIELGEIEAALLQHP 896
|
....*.
gi 66822211 538 SVLECC 543
Cdd:COG1020 897 GVREAV 902
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
260-551 |
1.94e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 73.01 E-value: 1.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 260 LYTSGTTGNTKAVVRS---NGPH-----MVGIKYYTFRKESDipQIVFSNANIgwvsFHG----FFYGLLSGGNTLVMye 327
Cdd:PRK08276 146 LYSSGTTGRPKGIKRPlpgLDPDeapgmMLALLGFGMYGGPD--SVYLSPAPL----YHTaplrFGMSALALGGTVVV-- 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 328 ggiikNEHI--EDDLwIAIVKHKVTHTFPSPSVFRYLIKTDPEgtiVRSKYDLSNLKEIWCGG-----EV----IE---E 393
Cdd:PRK08276 218 -----MEKFdaEEAL-ALIERYRVTHSQLVPTMFVRMLKLPEE---VRARYDVSSLRVAIHAAapcpvEVkramIDwwgP 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 394 SIPEYieqklkikclrvYGQSE-IGVTSFISVHALNIPY---RA-TGVpsiyIRpsILSEEGEVLNSNEIGLVAFKLPMP 468
Cdd:PRK08276 289 IIHEY------------YASSEgGGVTVITSEDWLAHPGsvgKAvLGE----VR--ILDEDGNELPPGEIGTVYFEMDGY 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 469 PsfaITFYKNDEKFKQLFTRfPGYYDSGDLGYIDQRGFYTIVSRSDDQIkIS--CNkIQLNTIDTSILKHPSVLECCSIG 546
Cdd:PRK08276 351 P---FEYHNDPEKTAAARNP-HGWVTVGDVGYLDEDGYLYLTDRKSDMI-ISggVN-IYPQEIENLLVTHPKVADVAVFG 424
|
....*
gi 66822211 547 IlsPD 551
Cdd:PRK08276 425 V--PD 427
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
256-610 |
2.48e-13 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 71.54 E-value: 2.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 256 PLYILYTSGTTGNTKAV------VRSNGpHMVGIKYYTFRKESDIPQIVFsnanigwvsFHGFfyGLLSGGNTLVMYEGG 329
Cdd:cd05917 4 VINIQFTSGTTGSPKGAtlthhnIVNNG-YFIGERLGLTEQDRLCIPVPL---------FHCF--GSVLGVLACLTHGAT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 330 IIKNEHIEDDLWI--AIVKHKVTHTFPSPSVFRYLIkTDPEgtivRSKYDLSNLKEIWCGGEVIEESIPEYIEQKLKIKC 407
Cdd:cd05917 72 MVFPSPSFDPLAVleAIEKEKCTALHGVPTMFIAEL-EHPD----FDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMKD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 408 LRV-YGQSEIGVTSFISVHALNIPYRATGVPSI--YIRPSILSEEG-EVLNSNEIGLVAFKlpmppSFAIT--FYKNDEK 481
Cdd:cd05917 147 VTIaYGMTETSPVSTQTRTDDSIEKRVNTVGRImpHTEAKIVDPEGgIVPPVGVPGELCIR-----GYSVMkgYWNDPEK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 482 FKQLFTRfPGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGIlsPDCRTAPI--GI 559
Cdd:cd05917 222 TAEAIDG-DGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGV--PDERYGEEvcAW 298
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 66822211 560 LVLKENPSIDlnklQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPR 610
Cdd:cd05917 299 IRLKEGAELT----EEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
261-608 |
2.63e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 72.69 E-value: 2.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 261 YTSGTTGNTKAVVRSNGPHMVGIkyytfrkesdIPQIVFSNANIGWVS------FH--GFFYGLLS---GGNTLVMYEgg 329
Cdd:PRK08314 197 YTSGTTGVPKGCMHTHRTVMANA----------VGSVLWSNSTPESVVlavlplFHvtGMVHSMNApiyAGATVVLMP-- 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 330 iiknehieddLW------IAIVKHKVTH-TFPSPSVFRYLIKTDPEgtivrsKYDLSNLKEIWCGGEvieeSIPEYIEQK 402
Cdd:PRK08314 265 ----------RWdreaaaRLIERYRVTHwTNIPTMVVDFLASPGLA------ERDLSSLRYIGGGGA----AMPEAVAER 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 403 LK----IKCLRVYGQSEIgvtsfISVHALNIPYRAT----GVPSIYIRPSILS-EEGEVLNSNEIGLVAFKlpmPPSFAI 473
Cdd:PRK08314 325 LKeltgLDYVEGYGLTET-----MAQTHSNPPDRPKlqclGIPTFGVDARVIDpETLEELPPGEVGEIVVH---GPQVFK 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 474 TFYKNDEKFKQLFTRFPG--YYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGilSPD 551
Cdd:PRK08314 397 GYWNRPEATAEAFIEIDGkrFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIA--TPD 474
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66822211 552 CRTAPI--GILVLKENpsidlNKLQNEINNIITQDIESLAVLK---KIIVINQLPKTKVGKI 608
Cdd:PRK08314 475 PRRGETvkAVVVLRPE-----ARGKTTEEEIIAWAREHMAAYKyprIVEFVDSLPKSGSGKI 531
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
254-551 |
2.68e-13 |
|
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: 72.41 E-value: 2.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 254 SHPLYILYTSGTTGNTKaVVRSNGPHmvgikyytfRKESDIPQIVFSnANIGWVS----------FHG-----FFYGLLS 318
Cdd:cd05929 125 AAGWKMLYSGGTTGRPK-GIKRGLPG---------GPPDNDTLMAAA-LGFGPGAdsvylspaplYHAapfrwSMTALFM 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 319 GGNTLVMyeggiiknEHIEDDLWI-AIVKHKVTHTFPSPSVFRYLIKTdPEgtIVRSKYDLSNL--------------KE 383
Cdd:cd05929 194 GGTLVLM--------EKFDPEEFLrLIERYRVTFAQFVPTMFVRLLKL-PE--AVRNAYDLSSLkrvihaaapcppwvKE 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 384 IWC--GGEVIEEsipeyieqklkikclrVYGQSE-IGVTSFISVHALNIPyRATGVPsIYIRPSILSEEGEVLNSNEIGL 460
Cdd:cd05929 263 QWIdwGGPIIWE----------------YYGGTEgQGLTIINGEEWLTHP-GSVGRA-VLGKVHILDEDGNEVPPGEIGE 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 461 VAFKlpMPPSFAITFYKNDEKFKqlftRFPGYYDS-GDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSV 539
Cdd:cd05929 325 VYFA--NGPGFEYTNDPEKTAAA----RNEGGWSTlGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKV 398
|
330
....*....|..
gi 66822211 540 LECCSIGILSPD 551
Cdd:cd05929 399 LDAAVVGVPDEE 410
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
256-613 |
2.68e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 72.71 E-value: 2.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 256 PLYILYTSGTTGNTKAVVRSN--GPHMVGIKYYTFrkesDIP-QIVF-SNANIGWVSFHGFFYGLLSGGnTLVMYEGgii 331
Cdd:PRK06188 170 IAGLAYTGGTTGKPKGVMGTHrsIATMAQIQLAEW----EWPaDPRFlMCTPLSHAGGAFFLPTLLRGG-TVIVLAK--- 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 332 knehIEDDLWIAIVK-HKVTHTFPSPSVFRYLIKTDPEgtivrSKYDLSNLKEIWCGGEVIEES-IPEYIEQKLKIkCLR 409
Cdd:PRK06188 242 ----FDPAEVLRAIEeQRITATFLVPTMIYALLDHPDL-----RTRDLSSLETVYYGASPMSPVrLAEAIERFGPI-FAQ 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 410 VYGQSEIGvtSFISV-----HALNIPYRAT--GVPSIYIRPSILSEEGEVLNSNEIGLVAFKLP--------MPPSFAIT 474
Cdd:PRK06188 312 YYGQTEAP--MVITYlrkrdHDPDDPKRLTscGRPTPGLRVALLDEDGREVAQGEVGEICVRGPlvmdgywnRPEETAEA 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 475 FyKNdekfkqlftrfpGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGIlsPDCR- 553
Cdd:PRK06188 390 F-RD------------GWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGV--PDEKw 454
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66822211 554 -TAPIGILVLKENPSIDLNKLQneinNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:PRK06188 455 gEAVTAVVVLRPGAAVDAAELQ----AHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKAL 511
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
375-615 |
4.36e-13 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 72.01 E-value: 4.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 375 KYDLSNLKEIWCGGEVIEESIPEYIEQKLKIKCLRVYGQSEigVTSFISVHalniPYRATG--------VPSIYIRpsIL 446
Cdd:PRK08974 321 ELDFSSLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTE--CSPLVSVN----PYDLDYysgsiglpVPSTEIK--LV 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 447 SEEGEVLNSNEIGLVAFKlpmPPSFAITFYKNDEKFKQLFTRfpGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQL 526
Cdd:PRK08974 393 DDDGNEVPPGEPGELWVK---GPQVMLGYWQRPEATDEVIKD--GWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYP 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 527 NTIDTSILKHPSVLECCSIGILSPDCRTApIGILVLKENPSIDlnklQNEINNIITQDIESLAVLKKIIVINQLPKTKVG 606
Cdd:PRK08974 468 NEIEDVVMLHPKVLEVAAVGVPSEVSGEA-VKIFVVKKDPSLT----EEELITHCRRHLTGYKVPKLVEFRDELPKSNVG 542
|
....*....
gi 66822211 607 KIPRQILSN 615
Cdd:PRK08974 543 KILRRELRD 551
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
375-613 |
9.63e-13 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 71.20 E-value: 9.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 375 KYDLSNLKEIWCGGEVIEESIPEYIEQKLKIKCLRVYGQSEigvTSfiSVHALNiPYRATG--------VPSIYIrpSIL 446
Cdd:PRK07059 323 KLDFSKLIVANGGGMAVQRPVAERWLEMTGCPITEGYGLSE---TS--PVATCN-PVDATEfsgtiglpLPSTEV--SIR 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 447 SEEGEVLNSNEIGLVAFKLP--MPPsfaitfYKN--DEKFKQLFTrfPGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCN 522
Cdd:PRK07059 395 DDDGNDLPLGEPGEICIRGPqvMAG------YWNrpDETAKVMTA--DGFFRTGDVGVMDERGYTKIVDRKKDMILVSGF 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 523 KIQLNTIDTSILKHPSVLECCSIGIlsPDCRTAP-IGILVLKENPSIDlnklQNEINNIITQDIESLAVLKKIIVINQLP 601
Cdd:PRK07059 467 NVYPNEIEEVVASHPGVLEVAAVGV--PDEHSGEaVKLFVVKKDPALT----EEDVKAFCKERLTNYKRPKFVEFRTELP 540
|
250
....*....|..
gi 66822211 602 KTKVGKIPRQIL 613
Cdd:PRK07059 541 KTNVGKILRREL 552
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
249-543 |
1.33e-12 |
|
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: 70.31 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 249 VPVESSHPLYILYTSGTTGNTK-------AVVR--SNGPHMvgikyytfrkeSDIPQIVF-SNANIGW-VSFHGFFYGLL 317
Cdd:cd12117 131 VPVSPDDLAYVMYTSGSTGRPKgvavthrGVVRlvKNTNYV-----------TLGPDDRVlQTSPLAFdASTFEIWGALL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 318 SGGnTLVMYEGGIIKNehiEDDLWIAIVKHKVTHTFPSPSVFRYLIKTDPEGtivrskydLSNLKEIWCGGEVIEesiPE 397
Cdd:cd12117 200 NGA-RLVLAPKGTLLD---PDALGALIAEEGVTVLWLTAALFNQLADEDPEC--------FAGLRELLTGGEVVS---PP 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 398 YIEQKLK----IKCLRVYGQSEigVTSFISVHALNIPYRATG-VP--------SIYI-----RPSILSEEGEVLNSNEiG 459
Cdd:cd12117 265 HVRRVLAacpgLRLVNGYGPTE--NTTFTTSHVVTELDEVAGsIPigrpiantRVYVldedgRPVPPGVPGELYVGGD-G 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 460 LVAFKLPMPpsfAITfyknDEKFKQLfTRFPG--YYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHP 537
Cdd:cd12117 342 LALGYLNRP---ALT----AERFVAD-PFGPGerLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHP 413
|
....*.
gi 66822211 538 SVLECC 543
Cdd:cd12117 414 GVREAV 419
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
529-607 |
1.55e-12 |
|
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: 62.95 E-value: 1.55e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66822211 529 IDTSILKHPSVLECCSIGILSPDCRTAPIGILVLKENPSIdlnkLQNEINNIITQDIESLAVLKKIIVINQLPKTKVGK 607
Cdd:pfam13193 2 VESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVEL----LEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
250-617 |
3.78e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 69.07 E-value: 3.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 250 PVESSHPLYILYTSGTTGNTKAVVRSngphmvgikyytfrkESDIPQIVFSNANIGWVSFHGFFY---------GLLSGG 320
Cdd:PRK09088 131 SIPPERVSLILFTSGTSGQPKGVMLS---------------ERNLQQTAHNFGVLGRVDAHSSFLcdapmfhiiGLITSV 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 321 NTLVMYEGGIIKNEHIEDDL---WIAIVKHKVTHTFPSPSVFRyLIKTDPEGTIVRskydLSNLKEIWCGGEV-IEESIP 396
Cdd:PRK09088 196 RPVLAVGGSILVSNGFEPKRtlgRLGDPALGITHYFCVPQMAQ-AFRAQPGFDAAA----LRHLTALFTGGAPhAAEDIL 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 397 EYIEQKLKIKClrVYGQSEIGVTSFISVHALNIPYRA--TGVPSIYIRPSILSEEGEVLNSNEIGLVAFKlpmPPSFAIT 474
Cdd:PRK09088 271 GWLDDGIPMVD--GFGMSEAGTVFGMSVDCDVIRAKAgaAGIPTPTVQTRVVDDQGNDCPAGVPGELLLR---GPNLSPG 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 475 FYKNDEKFKQLFTRfPGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGIlsPDCRT 554
Cdd:PRK09088 346 YWRRPQATARAFTG-DGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGM--ADAQW 422
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66822211 555 APIGILVLKENPSIDLnklqnEINNIITQDIESLA---VLKKIIVINQLPKTKVGKIPRQILSNLL 617
Cdd:PRK09088 423 GEVGYLAIVPADGAPL-----DLERIRSHLSTRLAkykVPKHLRLVDALPRTASGKLQKARLRDAL 483
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
375-613 |
4.82e-12 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 68.70 E-value: 4.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 375 KYDLSNLKEIWCGGEVIEESIPEYIEQKLKIKCLRVYGQSEIGVTSFISVHALNIPYRATGVPSIYIRPSILSEEGEVLN 454
Cdd:PRK12492 329 DLDFSALKLTNSGGTALVKATAERWEQLTGCTIVEGYGLTETSPVASTNPYGELARLGTVGIPVPGTALKVIDDDGNELP 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 455 SNEIGLVAFKlpmPPSFAITFYKNDEKFKQLFTRfPGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSIL 534
Cdd:PRK12492 409 LGERGELCIK---GPQVMKGYWQQPEATAEALDA-EGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVM 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 535 KHPSVLECCSIGIlsPDCRTA-PIGILVLKENPSIDLnklqNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:PRK12492 485 AHPKVANCAAIGV--PDERSGeAVKLFVVARDPGLSV----EELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
259-617 |
6.49e-12 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 66.97 E-value: 6.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 259 ILYTSGTTGNTKAVVRSNGPHM---VGIKyytfrkeSDIPQivfsNANIGWV----SFH--GF---FYGLLSGGNtLVMY 326
Cdd:cd17630 5 VILTSGSTGTPKAVVHTAANLLasaAGLH-------SRLGF----GGGDSWLlslpLYHvgGLailVRSLLAGAE-LVLL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 327 EGgiiknehiEDDLWIAIVKHKVTHTFPSPSVFRYLIkTDPEGTivrskYDLSNLKEIWCGGEVIEESIPEYIEQkLKIK 406
Cdd:cd17630 73 ER--------NQALAEDLAPPGVTHVSLVPTQLQRLL-DSGQGP-----AALKSLRAVLLGGAPIPPELLERAAD-RGIP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 407 CLRVYGQSEIGvtSFISVHALNIPYRAT-GVPSIYIRPSILSEEgevlnsnEIGLVAFKLPMPpsfaitfYKNDEKFKQL 485
Cdd:cd17630 138 LYTTYGMTETA--SQVATKRPDGFGRGGvGVLLPGRELRIVEDG-------EIWVGGASLAMG-------YLRGQLVPEF 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 486 FTrfPGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGIlsPDCR--TAPIGILVLK 563
Cdd:cd17630 202 NE--DGWFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGV--PDEElgQRPVAVIVGR 277
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 66822211 564 ENPSIDlnklqnEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQILSNLL 617
Cdd:cd17630 278 GPADPA------ELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
246-610 |
6.71e-12 |
|
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: 68.46 E-value: 6.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 246 YEYVPVESSHPLYILYTSGTTGNTKAVV--------RSNGphmVGIKYYTFRKEsdipqiVFSNanigWVSFHG----FF 313
Cdd:cd05906 159 HDLPQSRPDDLALLMLTSGSTGFPKAVPlthrnilaRSAG---KIQHNGLTPQD------VFLN----WVPLDHvgglVE 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 314 YGLLSggntlvMYEGGI---IKNEHIEDD--LWIA-IVKHKVTHTFpSPSVFRYLIKTDPEgTIVRSKYDLSNLKEIWCG 387
Cdd:cd05906 226 LHLRA------VYLGCQqvhVPTEEILADplRWLDlIDRYRVTITW-APNFAFALLNDLLE-EIEDGTWDLSSLRYLVNA 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 388 GE-VIEESIPEYIEQ----KLKIKCLR-VYGQSEI--GVT--------------SFISVHAlniPYratgvPSIYIRpsI 445
Cdd:cd05906 298 GEaVVAKTIRRLLRLlepyGLPPDAIRpAFGMTETcsGVIysrsfptydhsqalEFVSLGR---PI-----PGVSMR--I 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 446 LSEEGEVLNSNEIGLVAFKLPMppsfaIT--FYKNDEKFKQLFTRfPGYYDSGDLGYIDQrGFYTIVSRSDDQIKISCNK 523
Cdd:cd05906 368 VDDEGQLLPEGEVGRLQVRGPV-----VTkgYYNNPEANAEAFTE-DGWFRTGDLGFLDN-GNLTITGRTKDTIIVNGVN 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 524 IQLNTIDTSILK----HPSVLECCSIgilspdcRTAPIGI--LVLKENPSIDLNKLQNEINNIITQDIESLAVLKKIIVI 597
Cdd:cd05906 441 YYSHEIEAAVEEvpgvEPSFTAAFAV-------RDPGAETeeLAIFFVPEYDLQDALSETLRAIRSVVSREVGVSPAYLI 513
|
410
....*....|....*..
gi 66822211 598 ----NQLPKTKVGKIPR 610
Cdd:cd05906 514 plpkEEIPKTSLGKIQR 530
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
259-613 |
6.82e-12 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 68.25 E-value: 6.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 259 ILYTSGTTGNTKAVVRSNGPHMVGIKYYTFRKESDIPQIVFSNANIgwvsFH--GF----FYGLLSggNTLVMYeggiiK 332
Cdd:PRK13382 201 ILLTSGTTGTPKGARRSGPGGIGTLKAILDRTPWRAEEPTVIVAPM----FHawGFsqlvLAASLA--CTIVTR-----R 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 333 NEHIEDDLWIaIVKHKVTHTFPSPSVFRYLIKTDPEgtiVRSKYDLSNLKEIWCGGEVIEESIPEYIEQKLKIKCLRVYG 412
Cdd:PRK13382 270 RFDPEATLDL-IDRHRATGLAVVPVMFDRIMDLPAE---VRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYN 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 413 QSEIGVTSFISVHALNIPYRATGVPSIYIRPSILSEEGEVLNSNEIGLVafklpmppsfaitFYKNDEKFKQlFTR---- 488
Cdd:PRK13382 346 ATEAGMIATATPADLRAAPDTAGRPAEGTEIRILDQDFREVPTGEVGTI-------------FVRNDTQFDG-YTSgstk 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 489 --FPGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGILSPDCRTAPIGILVLKEnp 566
Cdd:PRK13382 412 dfHDGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKP-- 489
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 66822211 567 siDLNKLQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:PRK13382 490 --GASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRREL 534
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
76-614 |
6.96e-12 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 68.17 E-value: 6.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 76 DQDALIYEcPYLKKTIKLTYYQLYEKVCKFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGYSVKS 155
Cdd:PRK08008 22 HKTALIFE-SSGGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 156 ---LIDRIETitpKLIITTNygifndeiiTFTPnLKEAIELSTFKPSNVITLFRnevldetklkkvQNIPTIPNTLSWYD 232
Cdd:PRK08008 101 sawILQNSQA---SLLVTSA---------QFYP-MYRQIQQEDATPLRHICLTR------------VALPADDGVSSFTQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 233 eikkLKENNQSPFYEYVPVESSHPLYILYTSGTTGNTKAVV------RSNGphmvgikYYT-----FRkESDIPQIVFSN 301
Cdd:PRK08008 156 ----LKAQQPATLCYAPPLSTDDTAEILFTSGTTSRPKGVVithynlRFAG-------YYSawqcaLR-DDDVYLTVMPA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 302 anigwvsFHGFF-----YGLLSGGNTLVMYEggiiknEHIEDDLWIAIVKHKVTHTFPSPSVFRYLIKTDPegtivrSKY 376
Cdd:PRK08008 224 -------FHIDCqctaaMAAFSAGATFVLLE------KYSARAFWGQVCKYRATITECIPMMIRTLMVQPP------SAN 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 377 DLSNlkeiwCGGEV-----IEESIPEYIEQKLKIKCLRVYGQSE-----IGVTSFISVHalnipYRATGVPSIYIRPSIL 446
Cdd:PRK08008 285 DRQH-----CLREVmfylnLSDQEKDAFEERFGVRLLTSYGMTEtivgiIGDRPGDKRR-----WPSIGRPGFCYEAEIR 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 447 SEEGEVLNSNEIGLVAFK-LPMPPSFAiTFYKNDEKFKQLFTRfPGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQ 525
Cdd:PRK08008 355 DDHNRPLPAGEIGEICIKgVPGKTIFK-EYYLDPKATAKVLEA-DGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVS 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 526 LNTIDTSILKHPSVLECCSIGILSPDCRTAPIGILVLKENPSIDlnklQNEINNIITQDIESLAVLKKIIVINQLPKTKV 605
Cdd:PRK08008 433 CVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLS----EEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCS 508
|
....*....
gi 66822211 606 GKIPRQILS 614
Cdd:PRK08008 509 GKIIKKNLK 517
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
251-613 |
8.31e-12 |
|
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: 67.74 E-value: 8.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 251 VESSHP--LYILYTSGTTGNTKAVVRSNGPHmvgikYYTFRKESDI----PQIVFSNANIGwvsFHGFfyGLLSGGNTLV 324
Cdd:cd05920 134 LAESIPevALFLLSGGTTGTPKLIPRTHNDY-----AYNVRASAEVcgldQDTVYLAVLPA---AHNF--PLACPGVLGT 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 325 MYEGG--IIKNEHIEDDLWIAIVKHKVTHTFPSPSVFRYLIktdpeGTIVRSKYDLSNLKEIWCGGEVIEESIPEYIEQK 402
Cdd:cd05920 204 LLAGGrvVLAPDPSPDAAFPLIEREGVTVTALVPALVSLWL-----DAAASRRADLSSLRLLQVGGARLSPALARRVPPV 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 403 LKIKCLRVYGQSE--IGVTSF-----ISVHALNIPYRatgvPSIYIRpsILSEEGEVLNSNEIGLVAFKLPMPPSfaiTF 475
Cdd:cd05920 279 LGCTLQQVFGMAEglLNYTRLddpdeVIIHTQGRPMS----PDDEIR--VVDEEGNPVPPGEEGELLTRGPYTIR---GY 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 476 YKNDEKFKQLFTRfPGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGILSPDCRTA 555
Cdd:cd05920 350 YRAPEHNARAFTP-DGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGER 428
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 66822211 556 PIGILVLKeNPSIDLNKLQNEINNiitQDIESLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:cd05920 429 SCAFVVLR-DPPPSAAQLRRFLRE---RGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
257-613 |
8.53e-12 |
|
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: 67.85 E-value: 8.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 257 LYILYTSGTTGNTKAVV---RSNGPHMVGIKYYTFRKESDIpqiVFSNANIGW-VSFHGFFYGLLSGGnTLVMYEGGIIK 332
Cdd:cd17644 109 AYVIYTSGSTGKPKGVMiehQSLVNLSHGLIKEYGITSSDR---VLQFASIAFdVAAEEIYVTLLSGA-TLVLRPEEMRS 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 333 NEHiedDLWIAIVKHKVTHTFPSPSVFRYLIKTdpegtIVRSKYDL-SNLKEIWCGGEVIEESIPEYIEQKL--KIKCLR 409
Cdd:cd17644 185 SLE---DFVQYIQQWQLTVLSLPPAYWHLLVLE-----LLLSTIDLpSSLRLVIVGGEAVQPELVRQWQKNVgnFIQLIN 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 410 VYGQSEIGVTSfiSVHALNIPYRATgVPSIYIRPSILSEEGEVLNSNeiglvafKLPMPPSFAITF----------YKN- 478
Cdd:cd17644 257 VYGPTEATIAA--TVCRLTQLTERN-ITSVPIGRPIANTQVYILDEN-------LQPVPVGVPGELhiggvglargYLNr 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 479 ----DEKFKQ-LFTRFPG--YYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGILSPD 551
Cdd:cd17644 327 peltAEKFIShPFNSSESerLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQP 406
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66822211 552 CRTAPIGILVLKENPSIDLNKLQneinNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:cd17644 407 GNKRLVAYIVPHYEESPSTVELR----QFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
259-613 |
9.03e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 67.79 E-value: 9.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 259 ILYTSGTTGNTKAVVR---SNGPH------MVGIKYYTFRKESDI--PQIVFSNANIGWVSFhgffyGLLSGGNTLVMye 327
Cdd:PRK13391 159 MLYSSGTTGRPKGIKRplpEQPPDtplpltAFLQRLWGFRSDMVYlsPAPLYHSAPQRAVML-----VIRLGGTVIVM-- 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 328 ggiiknEHIEDDLWIAIV-KHKVTHTFPSPSVFRYLIKTdPEGtiVRSKYDLSNLKEIW-----CGGEVIEESI----P- 396
Cdd:PRK13391 232 ------EHFDAEQYLALIeEYGVTHTQLVPTMFSRMLKL-PEE--VRDKYDLSSLEVAIhaaapCPPQVKEQMIdwwgPi 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 397 --EYieqklkikclrvYGQSE-IGVTSFISVHALNipYRATGVPSIYIRPSILSEEGEVLNSNEIGLVAFKLPMPpsfaI 473
Cdd:PRK13391 303 ihEY------------YAATEgLGFTACDSEEWLA--HPGTVGRAMFGDLHILDDDGAELPPGEPGTIWFEGGRP----F 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 474 TFYKNDEKFKQLFTRFPGYYDSGDLGYIDQRGFYTIVSRSDDQIkISCN-KIQLNTIDTSILKHPSVLECCSIGILSPDC 552
Cdd:PRK13391 365 EYLNDPAKTAEARHPDGTWSTVGDIGYVDEDGYLYLTDRAAFMI-ISGGvNIYPQEAENLLITHPKVADAAVFGVPNEDL 443
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66822211 553 RTAPIGILVLKE--NPSIDLNKlqnEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:PRK13391 444 GEEVKAVVQPVDgvDPGPALAA---ELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLL 503
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
256-613 |
1.32e-11 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 67.11 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 256 PLYILYTSGTTGNTKAVV--RSNGPHMvgikYYTFRKESDI---PQIVFSNANIGWVSFHGFFYGLLSGGNTLVmyeggI 330
Cdd:cd17650 95 LAYVIYTSGTTGKPKGVMveHRNVAHA----AHAWRREYELdsfPVRLLQMASFSFDVFAGDFARSLLNGGTLV-----I 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 331 IKNEHIED--DLWIAIVKHKVTHTFPSPSVFRYLIKtdpegTIVRSKYDLSNLKEIWCGGEVIEESIP----EYIEQKLK 404
Cdd:cd17650 166 CPDEVKLDpaALYDLILKSRITLMESTPALIRPVMA-----YVYRNGLDLSAMRLLIVGSDGCKAQDFktlaARFGQGMR 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 405 IkcLRVYGQSEIGV-TSFISVHALNIPYRAT---GVPSIYIRPSILSEEgevLNSNEIGlVAFKLPMPPSFAITFYKNDE 480
Cdd:cd17650 241 I--INSYGVTEATIdSTYYEEGRDPLGDSANvpiGRPLPNTAMYVLDER---LQPQPVG-VAGELYIGGAGVARGYLNRP 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 481 KF-KQLFTRFP-----GYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLEccSIGILSPDcRT 554
Cdd:cd17650 315 ELtAERFVENPfapgeRMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDE--AVVAVRED-KG 391
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 66822211 555 APIGiLVLKENPSIDLNklQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:cd17650 392 GEAR-LCAYVVAAATLN--TAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
448-613 |
2.51e-11 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 66.44 E-value: 2.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 448 EEGEVLNSNEIGLVAFKLP--------MPpsfaitfykndEKFKQLFTRfPGYYDSGDLGYIDQRGFYTIVSRSDDQIkI 519
Cdd:PRK07514 338 ETGAELPPGEIGMIEVKGPnvfkgywrMP-----------EKTAEEFRA-DGFFITGDLGKIDERGYVHIVGRGKDLI-I 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 520 S--CNkIQLNTIDTSILKHPSVLECCSIGILSPDCRTAPIGILVLKENPSIDLNKLQNEINniitqdiESLA---VLKKI 594
Cdd:PRK07514 405 SggYN-VYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALDEAAILAALK-------GRLArfkQPKRV 476
|
170
....*....|....*....
gi 66822211 595 IVINQLPKTKVGKIPRQIL 613
Cdd:PRK07514 477 FFVDELPRNTMGKVQKNLL 495
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
92-512 |
2.72e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 66.45 E-value: 2.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 92 KLTYYQLYEKVCKFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCT------------LFDGYSVKSLI-- 157
Cdd:PRK07798 28 RLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNvnyryvedelryLLDDSDAVALVye 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 158 ----DRIETITPKLiittnygifndeiitftPNLKEAIElstfkpsnvitlfrneVLDETklkkvqNIPTIPNTLSWYDE 233
Cdd:PRK07798 108 refaPRVAEVLPRL-----------------PKLRTLVV----------------VEDGS------GNDLLPGAVDYEDA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 234 IKklkenNQSPfyEYVPVE-SSHPLYILYTSGTTGNTKAVV-------RSNgphMVGIKYYTFRKESDIPQIV-FSNANI 304
Cdd:PRK07798 149 LA-----AGSP--ERDFGErSPDDLYLLYTGGTTGMPKGVMwrqedifRVL---LGGRDFATGEPIEDEEELAkRAAAGP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 305 GWVSF------HG-----FFYGLLSGGnTLVMYEggiiKNEHIEDDLWIAIVKHKVThtfpspSVF-------RYLIKT- 365
Cdd:PRK07798 219 GMRRFpapplmHGagqwaAFAALFSGQ-TVVLLP----DVRFDADEVWRTIEREKVN------VITivgdamaRPLLDAl 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 366 DPEGTivrskYDLSNLKEIWCGGEVIEESIPE-YIEQKLKIKCLRVYGQSEIGVTSFISVHALNIPyraTGVPSIYIRPS 444
Cdd:PRK07798 288 EARGP-----YDLSSLFAIASGGALFSPSVKEaLLELLPNVVLTDSIGSSETGFGGSGTVAKGAVH---TGGPRFTIGPR 359
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66822211 445 --ILSEEGEVL--NSNEIGLVAFKLPMPpsfaITFYKNDEKFKQLFTRFPG--YYDSGDLGYIDQRGFYTIVSR 512
Cdd:PRK07798 360 tvVLDEDGNPVepGSGEIGWIARRGHIP----LGYYKDPEKTAETFPTIDGvrYAIPGDRARVEADGTITLLGR 429
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
93-546 |
3.61e-11 |
|
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: 65.69 E-value: 3.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 93 LTYYQLYEKVCKFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDgysvkslidrieTITPKLIittN 172
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYP------------TSSAEQI---A 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 173 YgIFNDeiitftpnlkeaielstfkpSNVITLFrnevldetklkkvqniptipntLSWYDEIKKlkennqspfyeyvpve 252
Cdd:cd05907 71 Y-ILND--------------------SEAKALF----------------------VEDPDDLAT---------------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 253 sshplyILYTSGTTGNTKAVVRSNGPHMVGIKYYTFRKE-SDIPQI--------VFsnANIGWvsfhgfFYGLLSGGNTL 323
Cdd:cd05907 92 ------IIYTSGTTGRPKGVMLSHRNILSNALALAERLPaTEGDRHlsflplahVF--ERRAG------LYVPLLAGARI 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 324 VmyeggiikneHIEDDLWIAIVKHKVT-HTFPS-PSVFR--YL-IKTDPEGTIVRSKYDL---SNLKEIWCGGEVIEESI 395
Cdd:cd05907 158 Y----------FASSAETLLDDLSEVRpTVFLAvPRVWEkvYAaIKVKAVPGLKRKLFDLavgGRLRFAASGGAPLPAEL 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 396 PEYIeQKLKIKCLRVYGQSEigvTSfiSVHALNIP--YRATGVPSIYIRPSI-LSEEGEVLNSneiglvafklpmPPSFA 472
Cdd:cd05907 228 LHFF-RALGIPVYEGYGLTE---TS--AVVTLNPPgdNRIGTVGKPLPGVEVrIADDGEILVR------------GPNVM 289
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66822211 473 ITFYKNDEKFKQLFTRfPGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNK-IQLNTIDTSILKHPSVLECCSIG 546
Cdd:cd05907 290 LGYYKNPEATAEALDA-DGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKnISPEPIENALKASPLISQAVVIG 363
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
93-517 |
3.68e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 66.10 E-value: 3.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 93 LTYYQLYEKVCKFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGYSVKSLIDRIETITPKLIIttn 172
Cdd:PRK07788 75 LTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVAAREGVKALV--- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 173 ygiFNDEiitFTPNLKEAielstfkPSNVITLfrnevldETKLKKVQNIPTIPNTLSWYDEIkkLKENNQSPFyeyvPVE 252
Cdd:PRK07788 152 ---YDDE---FTDLLSAL-------PPDLGRL-------RAWGGNPDDDEPSGSTDETLDDL--IAGSSTAPL----PKP 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 253 SSHPLYILYTSGTTGNTKAVVRS--NGPHMVG--IKYYTFRKESDIpQIV--------FSNANIGWvsfhgffyGLlsgG 320
Cdd:PRK07788 206 PKPGGIVILTSGTTGTPKGAPRPepSPLAPLAglLSRVPFRAGETT-LLPapmfhatgWAHLTLAM--------AL---G 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 321 NTLVMYEggIIKNEHIEDDlwiaIVKHKVTHTFPSPSVFRYLIKTDPEgtiVRSKYDLSNLKEIWCGGEVIEesiPEYIE 400
Cdd:PRK07788 274 STVVLRR--RFDPEATLED----IAKHKATALVVVPVMLSRILDLGPE---VLAKYDTSSLKIIFVSGSALS---PELAT 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 401 QKLK----IKClRVYGQSEIGVTSFISVHALNIPYRATGVPSIYIRPSILSEEGEVLNSNEIGLVafklpmppsfaitFY 476
Cdd:PRK07788 342 RALEafgpVLY-NLYGSTEVAFATIATPEDLAEAPGTVGRPPKGVTVKILDENGNEVPRGVVGRI-------------FV 407
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 66822211 477 KNDEKFKQlFT------RFPGYYDSGDLGYIDQRGFYTIVSRSDDQI 517
Cdd:PRK07788 408 GNGFPFEG-YTdgrdkqIIDGLLSSGDVGYFDEDGLLFVDGRDDDMI 453
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
68-615 |
4.55e-11 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 65.41 E-value: 4.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 68 HIKNPAKRDQDALIYEcpylKKTIKLTYYQLYEKVCKFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTL 147
Cdd:cd17653 2 AFERIAAAHPDAVAVE----SLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 148 fDGysvKSLIDRIETItpkliittnygifndeiitftpnlkeaieLSTFKPSNVITlfrnevldetklkkvqniPTIPNT 227
Cdd:cd17653 78 -DA---KLPSARIQAI-----------------------------LRTSGATLLLT------------------TDSPDD 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 228 LSwydeikklkennqspfyeyvpvesshplYILYTSGTTGNTKAV---------VRSNGPHMVGIkyytfRKESDIPQIv 298
Cdd:cd17653 107 LA----------------------------YIIFTSGSTGIPKGVmvphrgvlnYVSQPPARLDV-----GPGSRVAQV- 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 299 fsnANIGWVSFHGFFYGLLSGGNTLVMYEggiiknehiEDDLWIAIVKhKVTHTFPSPSVfryLIKTDPEgtivrskyDL 378
Cdd:cd17653 153 ---LSIAFDACIGEIFSTLCNGGTLVLAD---------PSDPFAHVAR-TVDALMSTPSI---LSTLSPQ--------DF 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 379 SNLKEIWCGGEVIEESIpeyIEQKLKIKCL-RVYGQSEigvTSFISVHALNIPYRAT--GVP----SIYI-----RPSIL 446
Cdd:cd17653 209 PNLKTIFLGGEAVPPSL---LDRWSPGRRLyNAYGPTE---CTISSTMTELLPGQPVtiGKPipnsTCYIldadlQPVPE 282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 447 SEEGEVLNSNeIGLvafklpmppsfAITFYKNDE----KFKqLFTRFPG--YYDSGDLGYIDQRGFYTIVSRSDDQIKIS 520
Cdd:cd17653 283 GVVGEICISG-VQV-----------ARGYLGNPAltasKFV-PDPFWPGsrMYRTGDYGRWTEDGGLEFLGREDNQVKVR 349
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 521 CNKIQLNTIDTSILKHPSVLECCSIgILSPDCRTApigiLVLKEnpSIDLNKLQNEinniITQDIESLAVLKKIIVINQL 600
Cdd:cd17653 350 GFRINLEEIEEVVLQSQPEVTQAAA-IVVNGRLVA----FVTPE--TVDVDGLRSE----LAKHLPSYAVPDRIIALDSF 418
|
570
....*....|....*
gi 66822211 601 PKTKVGKIPRQILSN 615
Cdd:cd17653 419 PLTANGKVDRKALRE 433
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
242-613 |
5.01e-11 |
|
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: 65.40 E-value: 5.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 242 QSPFYEYVPVESSH-PLYILYTSGTTGNTKAVVRSngpH-------MVGIKYYTFRKES----DIPqiVFsNANiGWvsf 309
Cdd:cd12118 120 GDPDFEWIPPADEWdPIALNYTSGTTGRPKGVVYH---HrgaylnaLANILEWEMKQHPvylwTLP--MF-HCN-GW--- 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 310 hGFFYGLLSGGNTLVMYEggiikneHIEDDL-WIAIVKHKVTHTFPSPSVFRYLIKTDPEgtivrSKYDLSNLKEIWCGG 388
Cdd:cd12118 190 -CFPWTVAAVGGTNVCLR-------KVDAKAiYDLIEKHKVTHFCGAPTVLNMLANAPPS-----DARPLPHRVHVMTAG 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 389 EVIEESIPEYIEQkLKIKCLRVYGQSEigVTSFISV-------HALNIPYRA-----TGVPSIyirpsiLSEEGEVLNSN 456
Cdd:cd12118 257 APPPAAVLAKMEE-LGFDVTHVYGLTE--TYGPATVcawkpewDELPTEERArlkarQGVRYV------GLEEVDVLDPE 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 457 ----------EIGLVAFKLPMppsFAITFYKNDEKFKQLFTRfpGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQL 526
Cdd:cd12118 328 tmkpvprdgkTIGEIVFRGNI---VMKGYLKNPEATAEAFRG--GWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISS 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 527 NTIDTSILKHPSVLECCSIGIlsPDCR--TAPIGILVLKEnpsiDLNKLQNEInniITQDIESLAVLK--KIIVINQLPK 602
Cdd:cd12118 403 VEVEGVLYKHPAVLEAAVVAR--PDEKwgEVPCAFVELKE----GAKVTEEEI---IAFCREHLAGFMvpKTVVFGELPK 473
|
410
....*....|.
gi 66822211 603 TKVGKIPRQIL 613
Cdd:cd12118 474 TSTGKIQKFVL 484
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
91-613 |
6.06e-11 |
|
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: 65.14 E-value: 6.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 91 IKLTYYQLYEKVCKFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGYSVKSLIDRIETITPKLIIT 170
Cdd:cd05915 23 HRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 171 tnygifNDEIITFTpnlkeaielstfkpsnvitlfrnevldETKLKKVQNIPTIPNTLSWYDEIKKLKENNQSPFYEYVP 250
Cdd:cd05915 103 ------DPNLLPLV---------------------------EAIRGELKTVQHFVVMDEKAPEGYLAYEEALGEEADPVR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 251 VESSHPLYILYTSGTTGNTKAVVRSN-GPHMVGIKYYTFRKESDIPQIVFSnANIGWVSFHGFFYGLlsggnTLVMYEGG 329
Cdd:cd05915 150 VPERAACGMAYTTGTTGLPKGVVYSHrALVLHSLAASLVDGTALSEKDVVL-PVVPMFHVNAWCLPY-----AATLVGAK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 330 IIKNEHIEDD--LWIAIVKHKVTHTFPSPSVFRYLIKTDPEgtiVRSKYDLSnlKEIWCGGevieeSIPEYIEQKLK--- 404
Cdd:cd05915 224 QVLPGPRLDPasLVELFDGEGVTFTAGVPTVWLALADYLES---TGHRLKTL--RRLVVGG-----SAAPRSLIARFerm 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 405 -IKCLRVYGQSEI---GVTSFISVHALNIPYRATGVPSIYIRPSILSEEGEVLNSNEI-----GLVAFKLPMPPSFAITF 475
Cdd:cd05915 294 gVEVRQGYGLTETspvVVQNFVKSHLESLSEEEKLTLKAKTGLPIPLVRLRVADEEGRpvpkdGKALGEVQLKGPWITGG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 476 YKNDEKFKQLFTRFPGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGILSPDCRTA 555
Cdd:cd05915 374 YYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQER 453
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 66822211 556 PIGILVLKENPSidlnkLQNEINNIITQDIESLAVLKKIIVINQ-LPKTKVGKIPRQIL 613
Cdd:cd05915 454 PLAVVVPRGEKP-----TPEELNEHLLKAGFAKWQLPDAYVFAEeIPRTSAGKFLKRAL 507
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
249-613 |
7.20e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 65.95 E-value: 7.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 249 VPVESSHPLYILYTSGTTGNTKAVVRSNGP--HMVGI--KYYTFRKESDIPQIVFSNANIgwvsFHGFFYGLLSGGNTLV 324
Cdd:PRK12467 651 VALDPDNLAYVIYTSGSTGQPKGVAISHGAlaNYVCViaERLQLAADDSMLMVSTFAFDL----GVTELFGALASGATLH 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 325 MYEGGIIKNehiEDDLWIAIVKHKVTHTFPSPSVFRYLIKtDPEGTIVRSkydlsnLKEIWCGGEVIEESIPEYIEQK-L 403
Cdd:PRK12467 727 LLPPDCARD---AEAFAALMADQGVTVLKIVPSHLQALLQ-ASRVALPRP------QRALVCGGEALQVDLLARVRALgP 796
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 404 KIKCLRVYGQSE--IGVTSF-ISVHALNIPYRATGVP----SIYIRPSILSeegevlnsneiglvafklPMPPSFAITFY 476
Cdd:PRK12467 797 GARLINHYGPTEttVGVSTYeLSDEERDFGNVPIGQPlanlGLYILDHYLN------------------PVPVGVVGELY 858
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 477 KNDEKFKQLFTRFPG-----------------YYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSV 539
Cdd:PRK12467 859 IGGAGLARGYHRRPAltaerfvpdpfgadggrLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGV 938
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66822211 540 LECCSIGIlSPDCRTAPIGILVLKENPSIDLNKLQN-EINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:PRK12467 939 REAVVLAQ-PGDAGLQLVAYLVPAAVADGAEHQATRdELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKAL 1012
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
92-541 |
8.79e-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: 64.42 E-value: 8.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 92 KLTYYQLYEKVCKFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGYSVKSLIDRIETITPKLIITT 171
Cdd:cd17656 13 KLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVLTQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 172 NygifndeiitftpnlkeaielstfkpsnvitlfrnevldETKLKKVQNIPTIpnTLSWYDEIKKLKENNQSPfyeyvpV 251
Cdd:cd17656 93 R---------------------------------------HLKSKLSFNKSTI--LLEDPSISQEDTSNIDYI------N 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 252 ESSHPLYILYTSGTTGNTKAVVRsngPH--MVGIKYYTFRKEsdipQIVFSNANIGW------VSFHGFFYGLLSGGnTL 323
Cdd:cd17656 126 NSDDLLYIIYTSGTTGKPKGVQL---EHknMVNLLHFEREKT----NINFSDKVLQFatcsfdVCYQEIFSTLLSGG-TL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 324 VmyeggIIKNEHIED-DLWIAIVKHKVTHTFPSPSVFRYLIKTDPEgtivrSKYDL-SNLKEIWCGGE--VIEESIPEYI 399
Cdd:cd17656 198 Y-----IIREETKRDvEQLFDLVKRHNIEVVFLPVAFLKFIFSERE-----FINRFpTCVKHIITAGEqlVITNEFKEML 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 400 EQKlKIKCLRVYGQSEIGVTSFISV-HALNIP-YRATGVPSIYIRPSILSEEGEVlnsNEIGLVAFKLPMPPSFAITFYK 477
Cdd:cd17656 268 HEH-NVHLHNHYGPSETHVVTTYTInPEAEIPeLPPIGKPISNTWIYILDQEQQL---QPQGIVGELYISGASVARGYLN 343
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66822211 478 NDEKFKQLFTRFP-----GYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLE 541
Cdd:cd17656 344 RQELTAEKFFPDPfdpneRMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSE 412
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
375-613 |
9.38e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 64.78 E-value: 9.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 375 KYDLSNLKEIWCGGEVIEESIPEYIEQKLKIKCLRVYGQSEIG-VTSFISVHALNIPYRATGVPSIYIRpsILSEEGEVL 453
Cdd:PRK05677 322 KLDFSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSpVVSVNPSQAIQVGTIGIPVPSTLCK--VIDDDGNEL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 454 NSNEIGLVAFKlpmPPSFAITFYKNDEKFKQLFTRfPGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSI 533
Cdd:PRK05677 400 PLGEVGELCVK---GPQVMKGYWQRPEATDEILDS-DGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVL 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 534 LKHPSVLECCSIGIlsPDCRTAP-IGI-LVLKENPSIDLNKLQNEINNIITqdieSLAVLKKIIVINQLPKTKVGKIPRQ 611
Cdd:PRK05677 476 AALPGVLQCAAIGV--PDEKSGEaIKVfVVVKPGETLTKEQVMEHMRANLT----GYKVPKAVEFRDELPTTNVGKILRR 549
|
..
gi 66822211 612 IL 613
Cdd:PRK05677 550 EL 551
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
255-613 |
9.47e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 65.36 E-value: 9.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 255 HPLYILYTSGTTGNTKAVVRSNGPHMVGIKYYTFRKESDIPQIVFSNANIGW-VSFHGFFYGLLSGGNTLVMYEGgiikn 333
Cdd:PRK12316 656 NLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFdVSVWEFFWPLMSGARLVVAAPG----- 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 334 EHIE-DDLWIAIVKHKVTHTFPSPSVFRYLIktdPEGTIVrskyDLSNLKEIWCGGEVIEESIPEYIEQKLKIKCL-RVY 411
Cdd:PRK12316 731 DHRDpAKLVELINREGVDTLHFVPSMLQAFL---QDEDVA----SCTSLRRIVCSGEALPADAQEQVFAKLPQAGLyNLY 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 412 GQSE--IGVTSFISVHAL--NIPyraTGVPSIYIRPSILSEEGEvlnsneiglvafklPMPPSFAITFYKNDEKFKQLFT 487
Cdd:PRK12316 804 GPTEaaIDVTHWTCVEEGgdSVP---IGRPIANLACYILDANLE--------------PVPVGVLGELYLAGRGLARGYH 866
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 488 RFPGY----------------YDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCsigILSPD 551
Cdd:PRK12316 867 GRPGLtaerfvpspfvagermYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAA---VLAVD 943
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66822211 552 CRTApIGILVLkENPSIDlnkLQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:PRK12316 944 GKQL-VGYVVL-ESEGGD---WREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKAL 1000
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
259-613 |
9.89e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 64.64 E-value: 9.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 259 ILYTSGTTGNTKAV--------VRSNGPHMVGIKYYTFR-KESDIpqiVFSNANIgwvsFH-------GFFYGLlsgGNT 322
Cdd:PRK13390 153 MLYSSGTTGFPKGIqpdlpgrdVDAPGDPIVAIARAFYDiSESDI---YYSSAPI----YHaaplrwcSMVHAL---GGT 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 323 LVMyeggiIKNEHIEDDLWiAIVKHKVTHTFPSPSVFRYLIKTDPEgtiVRSKYDLSNLKEiwcggeVIEESIPEYIEQK 402
Cdd:PRK13390 223 VVL-----AKRFDAQATLG-HVERYRITVTQMVPTMFVRLLKLDAD---VRTRYDVSSLRA------VIHAAAPCPVDVK 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 403 ------LKIKCLRVYGQSEIGVTSFISVHALnIPYRATGVPSIYIRPSILSEEGEVLNSNEIGLVAFKLPMPPsfaITFY 476
Cdd:PRK13390 288 hamidwLGPIVYEYYSSTEAHGMTFIDSPDW-LAHPGSVGRSVLGDLHICDDDGNELPAGRIGTVYFERDRLP---FRYL 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 477 KNDEKFKQL-FTRFPGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGILSPDCRTA 555
Cdd:PRK13390 364 NDPEKTAAAqHPAHPFWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQ 443
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 556 PIGILVLKE--NPSidlNKLQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:PRK13390 444 VKAVIQLVEgiRGS---DELARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLL 500
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
248-542 |
1.57e-10 |
|
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: 63.57 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 248 YVPVESSHP-----------------------LYILYTSGTTGNTKAVVRSNGP----HMVGIKYYTFRKESDIPQIVFS 300
Cdd:cd17648 65 YVPIDPSYPderiqfiledtgarvvitnstdlAYAIYTSGTTGKPKGVLVEHGSvvnlRTSLSERYFGRDNGDEAVLFFS 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 301 NanigWVsFHGFFYGL---LSGGNTLVmyeggIIKNEHIEDD--LWIAIVKHKVTHTFPSPSVFryliktdpegtivrSK 375
Cdd:cd17648 145 N----YV-FDFFVEQMtlaLLNGQKLV-----VPPDEMRFDPdrFYAYINREKVTYLSGTPSVL--------------QQ 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 376 YDLS---NLKEIWCGGEVIEESIPEYIEQKLKIKCLRVYGQSEIGVTSFISVHALNIPY-RATGVPSIYIRPSILSEEGE 451
Cdd:cd17648 201 YDLArlpHLKRVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTETTVTNHKRFFPGDQRFdKSLGRPVRNTKCYVLNDAMK 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 452 VLNSNEIG------------------LVAFKLPMPPsfaitFYKNDEKfkqLFTRFPGYYDSGDLGYIDQRGFYTIVSRS 513
Cdd:cd17648 281 RVPVGAVGelylggdgvargylnrpeLTAERFLPNP-----FQTEQER---ARGRNARLYKTGDLVRWLPSGELEYLGRN 352
|
330 340
....*....|....*....|....*....
gi 66822211 514 DDQIKISCNKIQLNTIDTSILKHPSVLEC 542
Cdd:cd17648 353 DFQVKIRGQRIEPGEVEAALASYPGVREC 381
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
249-613 |
2.70e-10 |
|
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: 63.12 E-value: 2.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 249 VPVESSHPLYILYTSGTTGNTKAVVR-----SNGPHMVGIKYYTFRKeSDIPQIvfsnANIgwvSFHGF----FYGLLSg 319
Cdd:cd17655 132 PVSKSDDLAYVIYTSGSTGKPKGVMIehrgvVNLVEWANKVIYQGEH-LRVALF----ASI---SFDASvteiFASLLS- 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 320 GNTLVMYEGGIIKNEHIeddLWIAIVKHKVTHTFPSPSVFRYLIKTDpegtivrsKYDLSNLKEIWCGGEVIEESIPEYI 399
Cdd:cd17655 203 GNTLYIVRKETVLDGQA---LTQYIRQNRITIIDLTPAHLKLLDAAD--------DSEGLSLKHLIVGGEALSTELAKKI 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 400 EQKLKIKC--LRVYGQSE--IGVTSF-ISVHALNIPYRATGVP----SIYI-----RPSILSEEGEVLNSNEiGLVAFKL 465
Cdd:cd17655 272 IELFGTNPtiTNAYGPTEttVDASIYqYEPETDQQVSVPIGKPlgntRIYIldqygRPQPVGVAGELYIGGE-GVARGYL 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 466 PMPpsfAITfyknDEKFKQlfTRF-PG--YYDSGDL------GYIDQRGfytivsRSDDQIKISCNKIQLNTIDTSILKH 536
Cdd:cd17655 351 NRP---ELT----AEKFVD--DPFvPGerMYRTGDLarwlpdGNIEFLG------RIDHQVKIRGYRIELGEIEARLLQH 415
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66822211 537 PSVLEccSIGILSPDCRTAPIGILVLKENPSIDLNKLQNEinniITQDIESLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:cd17655 416 PDIKE--AVVIARKDEQGQNYLCAYIVSEKELPVAQLREF----LARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
259-608 |
3.27e-10 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 63.40 E-value: 3.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 259 ILYTSGTTGNTKAVVRSNGPHMVGIKyytfrkesDIPQIVFSNANIGWVS----FHGF------FYGLLSGgnTLVMY-- 326
Cdd:PRK08633 787 IIFSSGSEGEPKGVMLSHHNILSNIE--------QISDVFNLRNDDVILSslpfFHSFgltvtlWLPLLEG--IKVVYhp 856
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 327 ---EG-GIIKnehieddlwiAIVKHKVTHTFPSPSVFR-YL--IKTDPEgtivrskyDLSNLKEIWCGGEVIEESIPEYI 399
Cdd:PRK08633 857 dptDAlGIAK----------LVAKHRATILLGTPTFLRlYLrnKKLHPL--------MFASLRLVVAGAEKLKPEVADAF 918
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 400 EQKLKIKCLRVYGQSEigvTSfiSVHALNIP-------YRATG---------VPSIYIRpsILS-EEGEVLNSNEIGLVA 462
Cdd:PRK08633 919 EEKFGIRILEGYGATE---TS--PVASVNLPdvlaadfKRQTGskegsvgmpLPGVAVR--IVDpETFEELPPGEDGLIL 991
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 463 FKLP--MppsfaITFYKNDEKFKQLFT--RFPGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILK--H 536
Cdd:PRK08633 992 IGGPqvM-----KGYLGDPEKTAEVIKdiDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKalG 1066
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66822211 537 PSVLECCSIGIlsPDCRTapiG--ILVLKENPSIDLNKLQNEINNiitQDIESLAVLKKIIVINQLPKTKVGKI 608
Cdd:PRK08633 1067 GEEVVFAVTAV--PDEKK---GekLVVLHTCGAEDVEELKRAIKE---SGLPNLWKPSRYFKVEALPLLGSGKL 1132
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
73-518 |
5.59e-10 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 62.43 E-value: 5.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 73 AKRDQDALIYECPYLKKTIKLTYYQLYEKVCKFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFdgys 152
Cdd:COG1022 21 AARFPDRVALREKEDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPIY---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 153 vkslidriETITPKLIIttnYgIFNDeiitftpnlkeaielstfkpSNVITLFrneVLDETKLKKV----QNIPTI---- 224
Cdd:COG1022 97 --------PTSSAEEVA---Y-ILND--------------------SGAKVLF---VEDQEQLDKLlevrDELPSLrhiv 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 225 ----------PNTLSWyDEIKKLKENNQSP-FYEYVP--VESSHPLYILYTSGTTGNTKAVVRSNGP--HMV--GIKYYT 287
Cdd:COG1022 142 vldprglrddPRLLSL-DELLALGREVADPaELEARRaaVKPDDLATIIYTSGTTGRPKGVMLTHRNllSNAraLLERLP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 288 FRKESDipqivfsnanigWVSF--------HGFFYGLLSGGNTLVMYEGGiiknEHIEDDLwiAIVKhkvTHTFPSP--- 356
Cdd:COG1022 221 LGPGDR------------TLSFlplahvfeRTVSYYALAAGATVAFAESP----DTLAEDL--REVK---PTFMLAVprv 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 357 --------------------SVFRYLIKT-----------DPEGTIVRSKYDL--------------SNLKEIWCGGEVI 391
Cdd:COG1022 280 wekvyagiqakaeeagglkrKLFRWALAVgrryararlagKSPSLLLRLKHALadklvfsklrealgGRLRFAVSGGAAL 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 392 EESIPEYIeQKLKIKCLRVYGQSEigvTS-FISVHALNIPYRAT-G--VPSIYIRpsiLSEEGEVLnsneiglvaFKLPM 467
Cdd:COG1022 360 GPELARFF-RALGIPVLEGYGLTE---TSpVITVNRPGDNRIGTvGppLPGVEVK---IAEDGEIL---------VRGPN 423
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 66822211 468 ppsfaiTF---YKNDEKFKQLFTRfPGYYDSGDLGYIDQRGFYTIVSRSDDQIK 518
Cdd:COG1022 424 ------VMkgyYKNPEATAEAFDA-DGWLHTGDIGELDEDGFLRITGRKKDLIV 470
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
251-613 |
6.51e-10 |
|
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: 61.55 E-value: 6.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 251 VESSHPLYILYTSGTTGNTKAVVRSNGpHMVGIKYYTFRKESDIPQIVfsnanigWVSFHGF--------FYGLLSGGNT 322
Cdd:cd17643 90 TDPDDLAYVIYTSGSTGRPKGVVVSHA-NVLALFAATQRWFGFNEDDV-------WTLFHSYafdfsvweIWGALLHGGR 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 323 LVMYEGGIIKNEhieDDLWIAIVKHKVTHTFPSPSVFRYLIKTDPEGTIvrskyDLSNLKEIWCGGEVIEESIPEYIEQK 402
Cdd:cd17643 162 LVVVPYEVARSP---EDFARLLRDEGVTVLNQTPSAFYQLVEAADRDGR-----DPLALRYVIFGGEALEAAMLRPWAGR 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 403 LKIKCLRV---YGQSEIGV-TSFISVHALNIPYRAT---GVP----SIYI-----RPSILSEEGEVLNS---------NE 457
Cdd:cd17643 234 FGLDRPQLvnmYGITETTVhVTFRPLDAADLPAAAAspiGRPlpglRVYVldadgRPVPPGVVGELYVSgagvargylGR 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 458 IGLVAFKLPMPPSFAITfykndekfkqlfTRfpgYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHP 537
Cdd:cd17643 314 PELTAERFVANPFGGPG------------SR---MYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHP 378
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66822211 538 SVLECCSIGILSPDCRTAPIGILVLKENPSIDLNKLQNEINniitqdiESLA---VLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:cd17643 379 SVRDAAVIVREDEPGDTRLVAYVVADDGAAADIAELRALLK-------ELLPdymVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
93-542 |
1.45e-09 |
|
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: 60.77 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 93 LTYYQLYEKVCKFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGYSVksliDRIETI----TPKLI 168
Cdd:cd12116 13 LSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPA----DRLRYIledaEPALV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 169 ITTnygifndeiitftpnlkeaielstfkpsnvitlfrnevlDETKLKKVQNIPTIPNTLswydEIKKLKENNQSPfyey 248
Cdd:cd12116 89 LTD---------------------------------------DALPDRLPAGLPVLLLAL----AAAAAAPAAPRT---- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 249 vPVESSHPLYILYTSGTTGNTKAVVRSN----------------GP--HMVGIKYYTFrkesDIpqivfsnanigwvSFH 310
Cdd:cd12116 122 -PVSPDDLAYVIYTSGSTGRPKGVVVSHrnlvnflhsmrerlglGPgdRLLAVTTYAF----DI-------------SLL 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 311 GFFYGLLSGGnTLVMYEGGIIKNEHiedDLWIAIVKHKVTHTFPSPSVFRYLIKTDPEGtivrskydLSNLKeIWCGGEV 390
Cdd:cd12116 184 ELLLPLLAGA-RVVIAPRETQRDPE---ALARLIEAHSITVMQATPATWRMLLDAGWQG--------RAGLT-ALCGGEA 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 391 IEESIPEYIeqKLKIKCL-RVYGQSEIGVTSfiSVHALNIPYRAT--GVP----SIYI-----RPSILSEEGEVLnsneI 458
Cdd:cd12116 251 LPPDLAARL--LSRVGSLwNLYGPTETTIWS--TAARVTAAAGPIpiGRPlantQVYVldaalRPVPPGVPGELY----I 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 459 GlvafklpmPPSFAITFYKNDEKFKQLFTRFPGY------YDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTS 532
Cdd:cd12116 323 G--------GDGVAQGYLGRPALTAERFVPDPFAgpgsrlYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAA 394
|
490
....*....|
gi 66822211 533 ILKHPSVLEC 542
Cdd:cd12116 395 LAAHPGVAQA 404
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
258-613 |
1.71e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 61.51 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 258 YILYTSGTTGNTKAVVRSNGPHMVGIKYYTFRKE--SDIPQIVFSNanigwVSFHGF---FYGLLSGGNTLVMYEGGIik 332
Cdd:PRK12316 4698 YVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYEltPDDRVLQFMS-----FSFDGShegLYHPLINGASVVIRDDSL-- 4770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 333 neHIEDDLWIAIVKHKVTHTFPSPSVFRYLIKTDPEgtivrsKYDLSNLKEIWCGGEVIEESIPEYIEQKLKIKCL-RVY 411
Cdd:PRK12316 4771 --WDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAER------DGEPPSLRVYCFGGEAVAQASYDLAWRALKPVYLfNGY 4842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 412 GQSEIGVTsfiSVHALNIPYRATGVPSIYIRPSILSEEGEVLNsNEIGlvafklPMPPSFAITFYKNDEKFKQLFTRFPG 491
Cdd:PRK12316 4843 GPTETTVT---VLLWKARDGDACGAAYMPIGTPLGNRSGYVLD-GQLN------PLPVGVAGELYLGGEGVARGYLERPA 4912
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 492 Y-----------------YDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGILSPDCRT 554
Cdd:PRK12316 4913 LtaerfvpdpfgapggrlYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQ 4992
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66822211 555 ApIGILVLKENPSIDLNKLQ----NEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:PRK12316 4993 L-VGYVVPQDPALADADEAQaelrDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKAL 5054
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
94-613 |
2.01e-09 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 60.38 E-value: 2.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 94 TYYQLYEKVCKFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGAtqctLFDGYSVKSLIDRI----ETITPKLII 169
Cdd:PLN02330 57 TYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGG----VFSGANPTALESEIkkqaEAAGAKLIV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 170 T--TNYGIFndeiitftpnlkEAIELSTFkpsnvitlfrneVLDETKlkkvqniptIPNTLSWYDEIKKLKENNQSPFYE 247
Cdd:PLN02330 133 TndTNYGKV------------KGLGLPVI------------VLGEEK---------IEGAVNWKELLEAADRAGDTSDNE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 248 yvPVESSHPLYILYTSGTTGNTKAVVRSNGPHMVGIKYYTFrkeSDIPQIVFSNANIGWVSFHgFFYGLLSGGNTLVMYE 327
Cdd:PLN02330 180 --EILQTDLCALPFSSGTTGISKGVMLTHRNLVANLCSSLF---SVGPEMIGQVVTLGLIPFF-HIYGITGICCATLRNK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 328 GGIIKNEHIEDDLWI-AIVKHKVTHTFPSPSVFRYLIKtDPegtiVRSKYDLSNLK--EIWCGGEVIEESIPEYIEQKL- 403
Cdd:PLN02330 254 GKVVVMSRFELRTFLnALITQEVSFAPIVPPIILNLVK-NP----IVEEFDLSKLKlqAIMTAAAPLAPELLTAFEAKFp 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 404 KIKCLRVYGQSEigvTSFISVHALNiPYRATGVP---SI-YIRPS-----ILSEEGEVLNSNEIGLVAFKlpmPPSFAIT 474
Cdd:PLN02330 329 GVQVQEAYGLTE---HSCITLTHGD-PEKGHGIAkknSVgFILPNlevkfIDPDTGRSLPKNTPGELCVR---SQCVMQG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 475 FYKNDEKFKQLFTRfPGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGILSPDCRT 554
Cdd:PLN02330 402 YYNNKEETDRTIDE-DGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGE 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 66822211 555 APIGILVLkeNPSIdlNKLQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:PLN02330 481 IPAACVVI--NPKA--KESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLL 535
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
344-619 |
4.12e-09 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 59.39 E-value: 4.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 344 IVKHKVTHTFPSPSVFRYLIKTDPegtivRSKYDLSNLKEIWCGGEVIEESIPEYIEQKLKIKCLRVYGQSEiGVTSF-- 421
Cdd:COG1021 270 IERERVTVTALVPPLALLWLDAAE-----RSRYDLSSLRVLQVGGAKLSPELARRVRPALGCTLQQVFGMAE-GLVNYtr 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 422 ------ISVHalnipyraT-GVP-SIY--IRpsILSEEGEVLNSNEIGLVAFKLPmppsFAIT-FYKNDEKFKQLFTRfP 490
Cdd:COG1021 344 lddpeeVILT--------TqGRPiSPDdeVR--IVDEDGNPVPPGEVGELLTRGP----YTIRgYYRAPEHNARAFTP-D 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 491 GYYDSGDLGYIDQRGFYTIVSRSDDQI-----KISCNKIQLNtidtsILKHPSVLECCSIGIlsPD-------C-----R 553
Cdd:COG1021 409 GFYRTGDLVRRTPDGYLVVEGRAKDQInrggeKIAAEEVENL-----LLAHPAVHDAAVVAM--PDeylgersCafvvpR 481
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66822211 554 TAPIGILVLKENpsidlnkLQNeinniitqdiESLAVLK---KIIVINQLPKTKVGKIPRQILSNLLND 619
Cdd:COG1021 482 GEPLTLAELRRF-------LRE----------RGLAAFKlpdRLEFVDALPLTAVGKIDKKALRAALAA 533
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
259-614 |
5.42e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 58.85 E-value: 5.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 259 ILYTSGTTGNTKAVVRSngPHM---VGIkYYTFRKESDIPqiVFSNANIGWVSFHGFFYGLLsggnTLVMYEGG-IIKNE 334
Cdd:PRK13383 179 VLLTSGTTGKPKGVPRA--PQLrsaVGV-WVTILDRTRLR--TGSRISVAMPMFHGLGLGML----MLTIALGGtVLTHR 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 335 HIEDDLWIAIVK-HKVTHTFPSPSVFRYLIKTDPEgtiVRSKYDLSNLKEIWCGGEVIEESIPEYIEQKLKIKCLRVYGQ 413
Cdd:PRK13383 250 HFDAEAALAQASlHRADAFTAVPVVLARILELPPR---VRARNPLPQLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGS 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 414 SEIGVTsfisvhALNIPYRATGVPSIYIRPsILSEEGEVLNSNeiglvafKLPMPPSFAITFYKNDEKFKQLFTR----- 488
Cdd:PRK13383 327 TEVGIG------ALATPADLRDAPETVGKP-VAGCPVRILDRN-------NRPVGPRVTGRIFVGGELAGTRYTDgggka 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 489 -FPGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGIlsPDCRTAP--IGILVLKEN 565
Cdd:PRK13383 393 vVDGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGV--PDERFGHrlAAFVVLHPG 470
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 66822211 566 PSIDLNKLQNEINNIITQdiesLAVLKKIIVINQLPKTKVGKIPRQILS 614
Cdd:PRK13383 471 SGVDAAQLRDYLKDRVSR----FEQPRDINIVSSIPRNPTGKVLRKELP 515
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
445-619 |
1.80e-08 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 57.31 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 445 ILSEEGEVLNSNEIGLVAFKLPMppsfaiTF---YKNDEKFKQLFTRfPGYYDSGDLGYIDQRGFYTIVSRSDDQIKISC 521
Cdd:PRK10946 367 VADADGNPLPQGEVGRLMTRGPY------TFrgyYKSPQHNASAFDA-NGFYCSGDLVSIDPDGYITVVGREKDQINRGG 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 522 NKIQLNTIDTSILKHPSVLECCSIGIlsPDCRtapIG-----ILVLKEnP--SIDLNKLQNEinniitQDIESLAVLKKI 594
Cdd:PRK10946 440 EKIAAEEIENLLLRHPAVIHAALVSM--EDEL---MGekscaFLVVKE-PlkAVQLRRFLRE------QGIAEFKLPDRV 507
|
170 180
....*....|....*....|....*
gi 66822211 595 IVINQLPKTKVGKIPRQILSNLLND 619
Cdd:PRK10946 508 ECVDSLPLTAVGKVDKKQLRQWLAS 532
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
257-574 |
2.18e-08 |
|
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: 56.62 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 257 LYILYTSGTTGNTKAVVRSNGP----HMVGIKYYTFRKESDIPQIVFSNANIGWVSF------HG----FFYGLLSGGNT 322
Cdd:cd05924 6 LYILYTGGTTGMPKGVMWRQEDifrmLMGGADFGTGEFTPSEDAHKAAAAAAGTVMFpapplmHGtgswTAFGGLLGGQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 323 LVmyeggIIKNEHIEDDLWIAIVKHKVTHTFPSPSVF-RYLIKT-DPEGTivrskYDLSNLKEIWCGGEVIEESIPE-YI 399
Cdd:cd05924 86 VV-----LPDDRFDPEEVWRTIEKHKVTSMTIVGDAMaRPLIDAlRDAGP-----YDLSSLFAISSGGALLSPEVKQgLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 400 EQKLKIKCLRVYGQSEIGVTSFiSVHALNIPYRAtgvPSIYIRPS--ILSEEGEVL--NSNEIGLVAFKLPMPpsfaITF 475
Cdd:cd05924 156 ELVPNITLVDAFGSSETGFTGS-GHSAGSGPETG---PFTRANPDtvVLDDDGRVVppGSGGVGWIARRGHIP----LGY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 476 YKNDEKFKQLFTRFPG--YYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGILSPDCR 553
Cdd:cd05924 228 YGDEAKTAETFPEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWG 307
|
330 340
....*....|....*....|.
gi 66822211 554 TAPIGILVLKENPSIDLNKLQ 574
Cdd:cd05924 308 QEVVAVVQLREGAGVDLEELR 328
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
258-613 |
2.71e-08 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 56.71 E-value: 2.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 258 YILYTSGTTGNTKAV---VRSNGPHMVGikyytFRKESDIPQ---IVFSNANIGWVSFHGFFYGLLSGGnTLVMYEGGII 331
Cdd:cd17654 122 YVIHTSGTTGTPKIVavpHKCILPNIQH-----FRSLFNITSediLFLTSPLTFDPSVVEIFLSLSSGA-TLLIVPTSVK 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 332 KNEHIEDDlwIAIVKHKVTHTFPSPSVFRYLIKTDPEGTiVRSKydLSNLKEIWCGGE-----VIEESipeYIEQKLKIK 406
Cdd:cd17654 196 VLPSKLAD--ILFKRHRITVLQATPTLFRRFGSQSIKST-VLSA--TSSLRVLALGGEpfpslVILSS---WRGKGNRTR 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 407 CLRVYGQSEigVTSFISVHalNIPYRATGVP--------SIYIRPSILSE-EGEVlnsnEIGLVAFKLPMPpsfaitfyk 477
Cdd:cd17654 268 IFNIYGITE--VSCWALAY--KVPEEDSPVQlgspllgtVIEVRDQNGSEgTGQV----FLGGLNRVCILD--------- 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 478 nDEkfkqLFTRFPGYYDSGDLGYIDQRGFYtIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSigILSPDCRTapI 557
Cdd:cd17654 331 -DE----VTVPKGTMRATGDFVTVKDGELF-FLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAV--TLSDQQRL--I 400
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 66822211 558 GILVLKENPSIDLNKLQneinniiTQDIESLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:cd17654 401 AFIVGESSSSRIHKELQ-------LTLLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
93-277 |
5.09e-08 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 56.28 E-value: 5.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 93 LTYYQLYEKVCKFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGYSVKSLIDRI-ETitpklIITT 171
Cdd:PLN02387 107 ITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLnET-----EVTT 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 172 nygifndeIITFTPNLKEAIELS----TFKpsNVITLFRNEVLDETKLKKVQNIptipnTLSWYDEIKKLKENNqspfye 247
Cdd:PLN02387 182 --------VICDSKQLKKLIDISsqleTVK--RVIYMDDEGVDSDSSLSGSSNW-----TVSSFSEVEKLGKEN------ 240
|
170 180 190
....*....|....*....|....*....|....*
gi 66822211 248 yvPVESSHPL-----YILYTSGTTGNTKAVVRSNG 277
Cdd:PLN02387 241 --PVDPDLPSpndiaVIMYTSGSTGLPKGVMMTHG 273
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
89-610 |
1.50e-07 |
|
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: 54.37 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 89 KTIKLTYYQLYEKVCKFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGYSVKSLIDRIETITPKLI 168
Cdd:cd05914 4 GGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 169 ITTNygifNDEIitftpnlkeAIelstfkpsnvitlfrnevldetklkkvqniptipntlswydeikklkennqspfyey 248
Cdd:cd05914 84 FVSD----EDDV---------AL--------------------------------------------------------- 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 249 vpvesshplyILYTSGTTGNTKAVV---RSNGPHMVGIKYYTFRKESDIpqivfsnaNIGWVSFHgFFYGLLSGGNTLVM 325
Cdd:cd05914 94 ----------INYTSGTTGNSKGVMltyRNIVSNVDGVKEVVLLGKGDK--------ILSILPLH-HIYPLTFTLLLPLL 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 326 YEGGIIKNEHIEDDLWIAIVKHKVTHTF--PSPSVFRYLIKTD--PEGTIVRSKYDLS---------------------- 379
Cdd:cd05914 155 NGAHVVFLDKIPSAKIIALAFAQVTPTLgvPVPLVIEKIFKMDiiPKLTLKKFKFKLAkkinnrkirklafkkvheafgg 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 380 NLKEIWCGGEVIEESIPEYIeQKLKIKCLRVYGQSEIGVTSFISVHAlNIPYRATGVPSIYIRPSILSEEGEVlNSNEIg 459
Cdd:cd05914 235 NIKEFVIGGAKINPDVEEFL-RTIGFPYTIGYGMTETAPIISYSPPN-RIRLGSAGKVIDGVEVRIDSPDPAT-GEGEI- 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 460 LVAFKLPMppsfaITFYKNDEKFKQLFTRfPGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNK-IQLNTIDTSILKHPS 538
Cdd:cd05914 311 IVRGPNVM-----KGYYKNPEATAEAFDK-DGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKnIYPEEIEAKINNMPF 384
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66822211 539 VLEccSIGILSPDCRTAPIGI-----LVLKENPSIDLNKLQNEINNIITQDIESLAVLKKIIVINQ-LPKTKVGKIPR 610
Cdd:cd05914 385 VLE--SLVVVQEKKLVALAYIdpdflDVKALKQRNIIDAIKWEVRDKVNQKVPNYKKISKVKIVKEeFEKTPKGKIKR 460
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
60-613 |
1.65e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 54.36 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 60 TCYNLLDIHiknpAKRDQDALiyecPYLKKTIKLTYYQLYEKVCKFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCAR 139
Cdd:PRK06164 11 TLASLLDAH----ARARPDAV----ALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 140 IGATQCTLFDGYSVKSLIDRIETITPKLIITtnYGIFNDeiITFTPNLKEAielstfKPSNVITLFRNEVLDETKlkkvq 219
Cdd:PRK06164 83 LGATVIAVNTRYRSHEVAHILGRGRARWLVV--WPGFKG--IDFAAILAAV------PPDALPPLRAIAVVDDAA----- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 220 niPTIPNTLSWYDEIKKLKENNQSPFYEYVPVESSHPLYILYT-SGTTGNTKAVVRSNGphmvgikyyTFRKESDIPQIV 298
Cdd:PRK06164 148 --DATPAPAPGARVQLFALPDPAPPAAAGERAADPDAGALLFTtSGTTSGPKLVLHRQA---------TLLRHARAIARA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 299 FSNAN----IGWVSFHGFF-----YGLLSGGNTLVM---YEGGIIKNehieddlwiAIVKHKVTHTFPSPSVFRYLIKTD 366
Cdd:PRK06164 217 YGYDPgavlLAALPFCGVFgfstlLGALAGGAPLVCepvFDAARTAR---------ALRRHRVTHTFGNDEMLRRILDTA 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 367 PEgtivrsKYDLSNLKeiWCGGEVIEESIPEYIEQKLK--IKCLRVYGQSEigVTSFISVHALNIPYR----ATGVPsiy 440
Cdd:PRK06164 288 GE------RADFPSAR--LFGFASFAPALGELAALARArgVPLTGLYGSSE--VQALVALQPATDPVSvrieGGGRP--- 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 441 IRPSIL-----SEEGEVLNSNEIGLVAFKlpmPPSFAITFYKNDEKFKQLFTRfPGYYDSGDLGYIDQRGFYTIVSRSDD 515
Cdd:PRK06164 355 ASPEARvrardPQDGALLPDGESGEIEIR---APSLMRGYLDNPDATARALTD-DGYFRTGDLGYTRGDGQFVYQTRMGD 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 516 QIKISCNKIQLNTIDTSILKHPSVLECCSIGILSpDCRTAPIGILVLKENPSIDLNKLqneinniITQDIESLAVLK--- 592
Cdd:PRK06164 431 SLRLGGFLVNPAEIEHALEALPGVAAAQVVGATR-DGKTVPVAFVIPTDGASPDEAGL-------MAACREALAGFKvpa 502
|
570 580
....*....|....*....|....
gi 66822211 593 KIIVINQLPKTKVG---KIPRQIL 613
Cdd:PRK06164 503 RVQVVEAFPVTESAngaKIQKHRL 526
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
490-613 |
1.05e-06 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 51.53 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 490 PGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGILSPDCRTAPIGILVLKeNPSID 569
Cdd:PRK07445 323 QGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPK-DPSIS 401
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 66822211 570 LNKLQNEinniITQDIESLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:PRK07445 402 LEELKTA----IKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQL 441
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
249-613 |
1.32e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 51.88 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 249 VPVESSHPLYILYTSGTTGNTKAVVRSNGPHMVGIKYYTFRKESDIPQIVFSNANIGWVSFHGFFYGLLSGGNTLVMYEG 328
Cdd:PRK12316 3191 IRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGP 3270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 329 GIIKNEHIEDDLwIAIVKHKVTHTFPSpsvfryLIKTDPEGTIVRskyDLSNLKEIWCGGEvieeSIPEYIEQKL--KIK 406
Cdd:PRK12316 3271 EDWRDPALLVEL-INSEGVDVLHAYPS------MLQAFLEEEDAH---RCTSLKRIVCGGE----ALPADLQQQVfaGLP 3336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 407 CLRVYGQSEIGVTSfiSVHALNIPY-------RATGVPSIYI-----RPSILSEEGEVLNSNEiGLVAFKLPMPPSFAIT 474
Cdd:PRK12316 3337 LYNLYGPTEATITV--THWQCVEEGkdavpigRPIANRACYIldgslEPVPVGALGELYLGGE-GLARGYHNRPGLTAER 3413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 475 FYKNDekfkqlFTRFPGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCsigILSPDCRT 554
Cdd:PRK12316 3414 FVPDP------FVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAV---VLAVDGRQ 3484
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 66822211 555 apigiLVLKENPSIDLNKLQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:PRK12316 3485 -----LVAYVVPEDEAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKAL 3538
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
254-541 |
2.20e-06 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 50.33 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 254 SHPLYILYTSGTTGNTKAVV--RSNGPHMVG--IKYYTFRKESDIPQivFSNanigwVSFHGFFY----GLLSGGnTLVM 325
Cdd:cd17652 93 DNLAYVIYTSGSTGRPKGVVvtHRGLANLAAaqIAAFDVGPGSRVLQ--FAS-----PSFDASVWellmALLAGA-TLVL 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 326 YEGG-IIKNEHIEDdlwiAIVKHKVTHTFPSPSVFRYLiktdPEGtivrskyDLSNLKEIWCGGEVIEesiPEYIEQKLK 404
Cdd:cd17652 165 APAEeLLPGEPLAD----LLREHRITHVTLPPAALAAL----PPD-------DLPDLRTLVVAGEACP---AELVDRWAP 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 405 IKC-LRVYGQSEIGVTSFISVhalniPYRATGVPSIYiRPsILSEEGEVLNSNeiglvafkL-PMPPSFAITFY------ 476
Cdd:cd17652 227 GRRmINAYGPTETTVCATMAG-----PLPGGGVPPIG-RP-VPGTRVYVLDAR--------LrPVPPGVPGELYiagagl 291
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66822211 477 ---------KNDEKFKQLFTRFPG--YYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLE 541
Cdd:cd17652 292 argylnrpgLTAERFVADPFGAPGsrMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAE 367
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
93-277 |
5.10e-06 |
|
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: 49.52 E-value: 5.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 93 LTYYQLYEKVCKFSRVLLNLNV--SKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDgysvkslidrieTITPKLIIT 170
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPLYD------------TLGPEAIEY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 171 tnygIFND---EIITFTPNLKeaielstfkpsnVITLfrNEVLDETKLKKVQNIPTIPNTLSwydeikklkennqspfye 247
Cdd:cd05927 74 ----ILNHaeiSIVFCDAGVK------------VYSL--EEFEKLGKKNKVPPPPPKPEDLA------------------ 117
|
170 180 190
....*....|....*....|....*....|
gi 66822211 248 yvpvesshplYILYTSGTTGNTKAVVRSNG 277
Cdd:cd05927 118 ----------TICYTSGTTGNPKGVMLTHG 137
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
92-618 |
6.10e-06 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 49.12 E-value: 6.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 92 KLTYYQLYEKVCKFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGAtqctlfdGY---SVKSLIDRIETIT---- 164
Cdd:PRK04813 27 KLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGH-------AYipvDVSSPAERIEMIIevak 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 165 PKLIITTNygifndeiitftpnlkeaiELSTfkpsnvitlfrneVLDETKLKKVQNIPTIPNTLSWYDEIKKLKENNQsp 244
Cdd:PRK04813 100 PSLIIATE-------------------ELPL-------------EILGIPVITLDELKDIFATGNPYDFDHAVKGDDN-- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 245 fyeyvpvesshpLYILYTSGTTGNTKAVVRS------------------NGPHMVGIKYYTFrkesDIPqiVFSnanigw 306
Cdd:PRK04813 146 ------------YYIIFTSGTTGKPKGVQIShdnlvsftnwmledfalpEGPQFLNQAPYSF----DLS--VMD------ 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 307 vsfhgFFYGLLSGGnTLVMYEGGIIKNEhieDDLWIAIVKHKVTHTFPSPSvFRYLIKTDPEgtivRSKYDLSNLKE-IW 385
Cdd:PRK04813 202 -----LYPTLASGG-TLVALPKDMTANF---KQLFETLPQLPINVWVSTPS-FADMCLLDPS----FNEEHLPNLTHfLF 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 386 CGgevieESIPEYIEQKL-----KIKCLRVYGQSE--IGVTSF-ISVHALNipyRATGVPSIYIRP----SILSEEGEVL 453
Cdd:PRK04813 268 CG-----EELPHKTAKKLlerfpSATIYNTYGPTEatVAVTSIeITDEMLD---QYKRLPIGYAKPdsplLIIDEEGTKL 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 454 NSNEIG--LVAfklpmPPSFAITFYKNDEKFKQLFTRFPGY--YDSGDLGYIDQrGFYTIVSRSDDQIKISCNKIQLNTI 529
Cdd:PRK04813 340 PDGEQGeiVIS-----GPSVSKGYLNNPEKTAEAFFTFDGQpaYHTGDAGYLED-GLLFYQGRIDFQIKLNGYRIELEEI 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 530 DTSILKHPSVLECCSIGILSPDCRTAPIGILVLKENPSIDLNKLQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIP 609
Cdd:PRK04813 414 EQNLRQSSYVESAVVVPYNKDHKVQYLIAYVVPKEEDFEREFELTKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKID 493
|
....*....
gi 66822211 610 RQILSNLLN 618
Cdd:PRK04813 494 RKALIEEVN 502
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
493-608 |
8.62e-06 |
|
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: 48.67 E-value: 8.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 493 YDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLEccSIGILSPDCRTAP--IGILVLKENPSIDL 570
Cdd:cd17647 374 YRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRE--NITLVRRDKDEEPtlVSYIVPRFDKPDDE 451
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66822211 571 N-----------------------KLQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKI 608
Cdd:cd17647 452 SfaqedvpkevstdpivkgligyrKLIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKV 512
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
249-613 |
9.74e-06 |
|
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: 48.47 E-value: 9.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 249 VPVESSHPLYILYTSGTTGNTKAVVRSNGPHMVGIKYYTFRKESDIPQIVFSNANIGW-VSFHGFFyGLLSGGNTLVMYE 327
Cdd:cd12115 100 VLTDPDDLAYVIYTSGSTGRPKGVAIEHRNAAAFLQWAAAAFSAEELAGVLASTSICFdLSVFELF-GPLATGGKVVLAD 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 328 GGIiknehiedDLWIAIVKHKVTHTFPSPSVFRYLIKTDPEGTIVRSkydlSNLkeiwcGGEVIEESIPEYIEQKLKIKC 407
Cdd:cd12115 179 NVL--------ALPDLPAAAEVTLINTVPSAAAELLRHDALPASVRV----VNL-----AGEPLPRDLVQRLYARLQVER 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 408 LR-VYGQSEigVTSFISVHALniPYRATGVPSIYiRP------SILSEEGEVLNSNEIGlvafKLPMPPSFAITFYKND- 479
Cdd:cd12115 242 VVnLYGPSE--DTTYSTVAPV--PPGASGEVSIG-RPlantqaYVLDRALQPVPLGVPG----ELYIGGAGVARGYLGRp 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 480 ----EKFkqLFTRF-PG--YYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGILSPDC 552
Cdd:cd12115 313 gltaERF--LPDPFgPGarLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAG 390
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66822211 553 RTAPIGILVLKENPSIDLnklqNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:cd12115 391 ERRLVAYIVAEPGAAGLV----EDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
344-536 |
1.79e-05 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 47.89 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 344 IVKHKVTHTFPSPSVFRYLIKTDPegtivRSKYDLSNLKEIWCGGEVIEESIPEYIEQKLKIKCLRV-YGQSEigVTSFI 422
Cdd:PRK06334 269 IDEAKVTFLGSTPVFFDYILKTAK-----KQESCLPSLRFVVIGGDAFKDSLYQEALKTFPHIQLRQgYGTTE--CSPVI 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 423 SVHALNIPY--RATGVPSIYIRPSILSEEGEV-LNSNEIGLVafkLPMPPSFAITFYKNDekFKQLFTRFPG--YYDSGD 497
Cdd:PRK06334 342 TINTVNSPKheSCVGMPIRGMDVLIVSEETKVpVSSGETGLV---LTRGTSLFSGYLGED--FGQGFVELGGetWYVTGD 416
|
170 180 190
....*....|....*....|....*....|....*....
gi 66822211 498 LGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKH 536
Cdd:PRK06334 417 LGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEG 455
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
262-418 |
2.09e-05 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 47.45 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 262 TSGTTGNTKAVVRS------------NGPHMVGikyytFRKEsDIPQIVFSnanIG-WVSFHGFFYGL---------LSG 319
Cdd:COG1541 91 SSGTTGKPTVVGYTrkdldrwaelfaRSLRAAG-----VRPG-DRVQNAFG---YGlFTGGLGLHYGAerlgatvipAGG 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 320 GNTlvmyeggiiknehieDDLWIAIVKHKVTHTFPSPSVFRYLIKTDPEGTIvrsKYDLSNLKEIWCGGEVIEESIPEYI 399
Cdd:COG1541 162 GNT---------------ERQLRLMQDFGPTVLVGTPSYLLYLAEVAEEEGI---DPRDLSLKKGIFGGEPWSEEMRKEI 223
|
170
....*....|....*....
gi 66822211 400 EQKLKIKCLRVYGQSEIGV 418
Cdd:COG1541 224 EERWGIKAYDIYGLTEVGP 242
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
373-515 |
2.19e-05 |
|
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: 47.42 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 373 RSKYDLSNLKEIWCGGEVIEESIPEYIeQKLKIKCLRVYGQSEIGVtsFISVHAL-NIPYRATGVPS--IYIRpsiLSEE 449
Cdd:cd17641 318 RDRLGFSRLRSAATGGAALGPDTFRFF-HAIGVPLKQLYGQTELAG--AYTVHRDgDVDPDTVGVPFpgTEVR---IDEV 391
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66822211 450 GEVLNSNeiglvafklpmpPSFAITFYKNDEKFKQLFTRfPGYYDSGDLGYIDQRGFYTIVSRSDD 515
Cdd:cd17641 392 GEILVRS------------PGVFVGYYKNPEATAEDFDE-DGWLHTGDAGYFKENGHLVVIDRAKD 444
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
249-613 |
2.24e-05 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 47.45 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 249 VPVESSHPLYILYTSGTTGNTKAVV---------RSNGPHMVGIK----YYTFrkesdIPqIVFSNAnigwvsFHGFFYG 315
Cdd:PRK06155 175 AAVQPGDTAAILYTSGTTGPSKGVCcphaqfywwGRNSAEDLEIGaddvLYTT-----LP-LFHTNA------LNAFFQA 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 316 LLSGGnTLVMYEggiiknEHIEDDLWIAIVKHKVTHTFPSPSVFRYLIKTdPEGTIVRSkydlSNLKEIWCGGevIEESI 395
Cdd:PRK06155 243 LLAGA-TYVLEP------RFSASGFWPAVRRHGATVTYLLGAMVSILLSQ-PARESDRA----HRVRVALGPG--VPAAL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 396 PEYIEQKLKIKCLRVYGQSEigvTSFisVHALNIPYRATGV-----PSIYIRpsILSEEGEVLNSNEIGLVAFKLPMPPS 470
Cdd:PRK06155 309 HAAFRERFGVDLLDGYGSTE---TNF--VIAVTHGSQRPGSmgrlaPGFEAR--VVDEHDQELPDGEPGELLLRADEPFA 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 471 FAITFYKNDEK----FKQLftrfpgYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIG 546
Cdd:PRK06155 382 FATGYFGMPEKtveaWRNL------WFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFP 455
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66822211 547 ILSPDCRTAPIGILVLKENPSIDLNKLQNEINNIITQdiesLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:PRK06155 456 VPSELGEDEVMAAVVLRDGTALEPVALVRHCEPRLAY----FAVPRYVEFVAALPKTENGKVQKFVL 518
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
491-616 |
2.40e-05 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 47.49 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 491 GYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGIlsPDCRTAPIGILV--LKENPSI 568
Cdd:PLN02860 414 GWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGV--PDSRLTEMVVACvrLRDGWIW 491
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66822211 569 DLNKLQNEINNIITQDIE--------SLAVLK--KIIVINQ--LPKTKVGKIPR-----QILSNL 616
Cdd:PLN02860 492 SDNEKENAKKNLTLSSETlrhhcrekNLSRFKipKLFVQWRkpFPLTTTGKIRRdevrrEVLSHL 556
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
249-610 |
2.56e-05 |
|
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: 47.27 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 249 VPVESSHPLYILYTSGTTGNTKAVVRSNGPHMVGIkyytfrkeSDIPQ--IVFSNANIGWVSFHGF------FYGLLSGG 320
Cdd:cd12114 121 VDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTI--------LDINRrfAVGPDDRVLALSSLSFdlsvydIFGALSAG 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 321 NTLVMYEGgiikNEHIEDDLWI-AIVKHKVTHTFPSPSVFRYLIKTDPEGTIvrskyDLSNLKEIWCGGEVIEESIPEYI 399
Cdd:cd12114 193 ATLVLPDE----ARRRDPAHWAeLIERHGVTLWNSVPALLEMLLDVLEAAQA-----LLPSLRLVLLSGDWIPLDLPARL 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 400 eQKLKIKClRVY---GQSEIGVTS-FISVHALN-----IPYratGVP----SIYIRPSILSE-----EGEVLnsneIGLV 461
Cdd:cd12114 264 -RALAPDA-RLIslgGATEASIWSiYHPIDEVPpdwrsIPY---GRPlanqRYRVLDPRGRDcpdwvPGELW----IGGR 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 462 AFKLPmppsfaitfYKNDEKFKQlfTRFP------GYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILK 535
Cdd:cd12114 335 GVALG---------YLGDPELTA--ARFVthpdgeRLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQA 403
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66822211 536 HPSVLECCSIGILSPDCRTApIGILVLKENPSIDlnkLQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPR 610
Cdd:cd12114 404 HPGVARAVVVVLGDPGGKRL-AAFVVPDNDGTPI---APDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDR 474
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
491-617 |
2.62e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 47.34 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 491 GYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGILSPDCRTAPIGILVLKENPSIDL 570
Cdd:PRK06178 442 GWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTA 521
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 66822211 571 NKLQNEINniitqdiESLAVLK--KIIVINQLPKTKVGKIPRQILSNLL 617
Cdd:PRK06178 522 AALQAWCR-------ENMAVYKvpEIRIVDALPMTATGKVRKQDLQALA 563
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
475-613 |
3.56e-05 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 46.76 E-value: 3.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 475 FYKNDEKFKQLFTRfpGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGilSPDCR- 553
Cdd:PLN02479 416 YLKNPKANEEAFAN--GWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVA--RPDERw 491
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66822211 554 -TAPIGILVLKEN-PSIDLNKLQNEINNIITQDIESLAVLKKiIVINQLPKTKVGKIPRQIL 613
Cdd:PLN02479 492 gESPCAFVTLKPGvDKSDEAALAEDIMKFCRERLPAYWVPKS-VVFGPLPKTATGKIQKHVL 552
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
490-617 |
4.20e-05 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 46.19 E-value: 4.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 490 PGYYDSGDLGYIDQrGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGIlsPDCR--TAPIGILVLKENPS 567
Cdd:PRK07824 233 PGWFRTDDLGALDD-GVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGL--PDDRlgQRVVAAVVGDGGPA 309
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 66822211 568 IDLNKLQNEinniITQDIESLAVLKKIIVINQLPKTKVGKIPRQILSNLL 617
Cdd:PRK07824 310 PTLEALRAH----VARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRRF 355
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
76-286 |
4.79e-05 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 46.41 E-value: 4.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 76 DQDALIYEcpylKKTIklTYYQLYEKVCKFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGAtqCTLFDGYSV-- 153
Cdd:PRK08279 52 DRPALLFE----DQSI--SYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGA--VVALLNTQQrg 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 154 KSLIDRIETITPKLIITtnygifndeiitfTPNLKEAIE--LSTFKPSNVITLFRNEVLDETKLkkvqniptipntlswY 231
Cdd:PRK08279 124 AVLAHSLNLVDAKHLIV-------------GEELVEAFEeaRADLARPPRLWVAGGDTLDDPEG---------------Y 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66822211 232 DEIKKLkennQSPFYEYVPVESSHP------LYIlYTSGTTGNTKAVVRSngpHMVGIKYY 286
Cdd:PRK08279 176 EDLAAA----AAGAPTTNPASRSGVtakdtaFYI-YTSGTTGLPKAAVMS---HMRWLKAM 228
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
343-569 |
6.94e-05 |
|
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: 45.37 E-value: 6.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 343 AIVKHKVTHTFPSPSVFRYLIKTDPEGtivrsKYDLSNL-----KEIWCGGEVIEESIPEYieqklkikCLRVYGQSEig 417
Cdd:cd17636 83 LIEAERCTHAFLLPPTIDQIVELNADG-----LYDLSSLrsspaAPEWNDMATVDTSPWGR--------KPGGYGQTE-- 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 418 VTSFISVHALNIPYRAT-GVPSIYIRPSILSEEGEVLNSNEIGLVAFKLPMppsfAITFYKNDEKFKQLFTRFpGYYDSG 496
Cdd:cd17636 148 VMGLATFAALGGGAIGGaGRPSPLVQVRILDEDGREVPDGEVGEIVARGPT----VMAGYWNRPEVNARRTRG-GWHHTN 222
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66822211 497 DLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGIlsPDCR--TAPIGILVLKENPSID 569
Cdd:cd17636 223 DLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGV--PDPRwaQSVKAIVVLKPGASVT 295
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
493-541 |
1.29e-04 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 45.44 E-value: 1.29e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 66822211 493 YDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLE 541
Cdd:TIGR03443 680 YRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRE 728
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
344-610 |
1.30e-04 |
|
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: 44.57 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 344 IVKHKVTH--TFPsPSVFRYLIKTDpegtivRSKYDLSNLKEIwCGGEVieesiPEYIEQKLKI---KCLRVYGQSEigv 418
Cdd:cd17637 84 IEEEKVTLmgSFP-PILSNLLDAAE------KSGVDLSSLRHV-LGLDA-----PETIQRFEETtgaTFWSLYGQTE--- 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 419 TS-FISVHalniPYR----ATGVPSIYIRPSILSEEGEVLNSNEIGLVAFKLPMppsfaiTF--YKNDEKFKQLFTRfPG 491
Cdd:cd17637 148 TSgLVTLS----PYRerpgSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPL------VFqgYWNLPELTAYTFR-NG 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 492 YYDSGDLGYIDQRGFYTIVSRS--DDQIKISCNKIQLNTIDTSILKHPSVLECCSIGILSPDCRTAPIGILVLKENPSID 569
Cdd:cd17637 217 WHHTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGATLT 296
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 66822211 570 lnklQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPR 610
Cdd:cd17637 297 ----ADELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
92-169 |
1.41e-04 |
|
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: 44.65 E-value: 1.41e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66822211 92 KLTYYQLYEKVCKFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGYSVKSLIDRIETITPKLII 169
Cdd:cd05940 3 ALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV 80
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
248-554 |
2.04e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 44.25 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 248 YVPVESSHPLYILYTSGTTGNTKAVVRSNGphMVgikyyTFRKESDIPQIVFSNANIGWVS---FHGffygllsggNTLV 324
Cdd:PRK13388 144 HREVDAMDPFMLIFTSGTTGAPKAVRCSHG--RL-----AFAGRALTERFGLTRDDVCYVSmplFHS---------NAVM 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 325 MyeggiiknehieddLWIAIVKHKVTHTFP---SPSVF-------------------RYLIKTdPEgtivrSKYDLSNLK 382
Cdd:PRK13388 208 A--------------GWAPAVASGAAVALPakfSASGFlddvrrygatyfnyvgkplAYILAT-PE-----RPDDADNPL 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 383 EIWCGGEVIEESIPEYiEQKLKIKCLRVYGQSEIGVtsfISVHALNIPYRATGVP----SIY-------IRPSILSEEGE 451
Cdd:PRK13388 268 RVAFGNEASPRDIAEF-SRRFGCQVEDGYGSSEGAV---IVVREPGTPPGSIGRGapgvAIYnpetlteCAVARFDAHGA 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 452 VLNSNE-IG-LVAfklPMPPSFAITFYKND----EKFKQlftrfpGYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQ 525
Cdd:PRK13388 344 LLNADEaIGeLVN---TAGAGFFEGYYNNPeataERMRH------GMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLS 414
|
330 340
....*....|....*....|....*....
gi 66822211 526 LNTIDTSILKHPSVLECCSIGIlsPDCRT 554
Cdd:PRK13388 415 AAPIERILLRHPAINRVAVYAV--PDERV 441
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
491-625 |
2.88e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 43.93 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 491 GYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGILSPDCRTAPIGILVLKenPSIDL 570
Cdd:PRK07008 409 GWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKR--PGAEV 486
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 66822211 571 NKlqNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQILSNLLNDpnYQLP 625
Cdd:PRK07008 487 TR--EELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLREQFRD--YVLP 537
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
491-624 |
2.90e-04 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 44.00 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 491 GYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGILSPDCRTAPIGILVLKEN--PSI 568
Cdd:PRK05620 430 GWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGiePTR 509
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66822211 569 DL-----NKLQNEINNIITQdiESLAVLKKIivinqlPKTKVGKIPRQILSNLLNDPNYQL 624
Cdd:PRK05620 510 ETaerlrDQLRDRLPNWMLP--EYWTFVDEI------DKTSVGKFDKKDLRQHLADGDFEI 562
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
231-541 |
4.01e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 43.10 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 231 YDEIKKLKEnnqspfyEYVPVESSHPLYILYTSGTTGNTKAVVRSNGPHMVGIKYYT--FRKESDIPQIVFSNANigwvs 308
Cdd:PRK08308 85 YGESDFTKL-------EAVNYLAEEPSLLQYSSGTTGEPKLIRRSWTEIDREIEAYNeaLNCEQDETPIVACPVT----- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 309 fHGffYGLLSGgnTLVMYEGGIiknehieddlwiaiVKHKVTHTFPspsvfRYLIK--TDPEGTIVRSK----YDLSNLK 382
Cdd:PRK08308 153 -HS--YGLICG--VLAALTRGS--------------KPVIITNKNP-----KFALNilRNTPQHILYAVplmlHILGRLL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 383 EiwcGGEVIEES------IPEYIEQKLKIKCLRV---YGQSEIGVtsfISVHALNIPYRATGVPSIYIRPSILSEEGevl 453
Cdd:PRK08308 209 P---GTFQFHAVmtsgtpLPEAWFYKLRERTTYMmqqYGCSEAGC---VSICPDMKSHLDLGNPLPHVSVSAGSDEN--- 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 454 NSNEIGLvafklpmppsfaitfyKNDEKfkQLFTRfpgyydsgDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSI 533
Cdd:PRK08308 280 APEEIVV----------------KMGDK--EIFTK--------DLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVM 333
|
....*...
gi 66822211 534 LKHPSVLE 541
Cdd:PRK08308 334 LRLPGVQE 341
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
493-633 |
5.56e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 43.23 E-value: 5.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 493 YDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGILSPDCRTApIGILVLK--ENPSIDL 570
Cdd:PRK05691 2570 YRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPSGKQL-AGYLVSAvaGQDDEAQ 2648
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66822211 571 NKLQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQILSN---LLNDPNYQLPDDVNDSEL 633
Cdd:PRK05691 2649 AALREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPApdpELNRQAYQAPRSELEQQL 2714
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
491-614 |
1.98e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 41.20 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 491 GYYDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGILSPDCRTAPIGILVLKENPSIDL 570
Cdd:PRK07867 381 GVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPGAKFDP 460
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 66822211 571 NKLQNEINNiiTQDIESLAVLKKIIVINQLPKTKVGKIPRQILS 614
Cdd:PRK07867 461 DAFAEFLAA--QPDLGPKQWPSYVRVCAELPRTATFKVLKRQLS 502
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
493-613 |
3.19e-03 |
|
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: 40.23 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 493 YDSGDLGYIDQRGFYTIVSRSDDQIKISCNKIQLNTIDTSILKHPSVLECCSIGILSPDCRTAPIGILVLKENPSIDlnk 572
Cdd:cd17645 325 YRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPEEIPHE--- 401
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 66822211 573 lqnEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:cd17645 402 ---ELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
475-613 |
7.86e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 39.16 E-value: 7.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822211 475 FYKNDEKFKQLFTrfPGYYDSGDLGYIDQRGFYTIVSRSDDQIkISCNK-IQLNTIDTSILKHPSVLECCSIGILSPDCR 553
Cdd:PRK08162 402 YLKNPKATEEAFA--GGWFHTGDLAVLHPDGYIKIKDRSKDII-ISGGEnISSIEVEDVLYRHPAVLVAAVVAKPDPKWG 478
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66822211 554 TAPIGILVLKENPSIDlnklQNEInniITQDIESLAVLK--KIIVINQLPKTKVGKIPRQIL 613
Cdd:PRK08162 479 EVPCAFVELKDGASAT----EEEI---IAHCREHLAGFKvpKAVVFGELPKTSTGKIQKFVL 533
|
|
| |
