|
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: 1215.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 1 MYKLSDPFDYLNDNSYSKSNPEAFWDEVAKKNVFWDKMYDKVYSGDEIYPDWFKGGELNTCYNLLDIHIKNPAKRDQDAL 80
Cdd:PTZ00237 1 MYKLSDPFDYENDSNYANSNPESFWDEVAKKYVHWDKMYDKVYSGDEIYPDWFKGGELNTCYNVLDIHVKNPLKRDQDAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 81 IYECPFLKKTIKLTYYQLYEKVCEFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGSSVKSLIDRI 160
Cdd:PTZ00237 81 IYECPYLKKTIKLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 161 ETITPKLIITTNYGILNDEIITFTPNLKEAIELSTFKPSNVITLFRNEVLDETKLKKVQTIPTIPNTLSWYDEIKKLKEN 240
Cdd:PTZ00237 161 ETITPKLIITTNYGILNDEIITFTPNLKEAIELSTFKPSNVITLFRNDITSESDLKKIETIPTIPNTLSWYDEIKKIKEN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 241 NQSPFYEYVPVESSHPLYILYTSGTTGNTKAVVRSNGPHMVGIKY-YTFRKESDIPQIVFSHTNIGWVSFHGFFYGLLSG 319
Cdd:PTZ00237 241 NQSPFYEYVPVESSHPLYILYTSGTTGNSKAVVRSNGPHLVGLKYyWRSIIEKDIPTVVFSHSSIGWVSFHGFLYGSLSL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 320 GNTLVMYEGGIIKNKHMEDDLWIAIVKHKVTHTFPSPSVFRYLIKTDPEGTIVRSKYDLSNLKEIWCGGEVIEESIPEYI 399
Cdd:PTZ00237 321 GNTFVMFEGGIIKNKHIEDDLWNTIEKHKVTHTLTLPKTIRYLIKTDPEATIIRSKYDLSNLKEIWCGGEVIEESIPEYI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 400 EQKLKIKCLRVFGQSEIGVTSFISVHALNIPYRATGVPSIYIRPSILSEEGEVLNSNEIGLVAFKLPMPPSFTITFYKND 479
Cdd:PTZ00237 401 ENKLKIKSSRGYGQTEIGITYLYCYGHINIPYNATGVPSIFIKPSILSEDGKELNVNEIGEVAFKLPMPPSFATTFYKND 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 480 EKFKQLFTRFPGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGILSPDCHTAPIGI 559
Cdd:PTZ00237 481 EKFKQLFSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 560 LVLK---ENPSIDLNKLQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQILSNLLNDPNYQLPDDVNDSELFYK 636
Cdd:PTZ00237 561 LVLKqdqSNQSIDLNKLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQIISKFLNDSNYQLPDNVNDSEIFYK 640
|
....*..
gi 66822213 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 |
1.19e-167 |
|
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: 492.60 E-value: 1.19e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 10 YLNDNSYSKSNPEAFWDEVAKKnVFWDKMYDKVYSGDEI-YPDWFKGGELNTCYNLLDIHIKNPaKRDQDALIYECPFLK 88
Cdd:cd05967 1 YEEVYARSIAEPEAFWAEQARL-IDWFKPPEKILDNSNPpFTRWFVGGRLNTCYNALDRHVEAG-RGDQIALIYDSPVTG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 89 KTIKLTYYQLYEKVCEFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGSSVKSLIDRIETITPKLI 168
Cdd:cd05967 79 TERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKPKLI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 169 ITTNYGILNDEIITFTPNLKEAIELSTFKPSNVITLFRNEVldETKLKKVQTiptipnTLSWYDEIKklkennQSPFYEY 248
Cdd:cd05967 159 VTASCGIEPGKVVPYKPLLDKALELSGHKPHHVLVLNRPQV--PADLTKPGR------DLDWSELLA------KAEPVDC 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 249 VPVESSHPLYILYTSGTTGNTKAVVRSNGPHMVGIkYYTFRKESDIPQ--IVFSHTNIGWVSFHGFF-YGLLSGGNTLVM 325
Cdd:cd05967 225 VPVAATDPLYILYTSGTTGKPKGVVRDNGGHAVAL-NWSMRNIYGIKPgdVWWAASDVGWVVGHSYIvYGPLLHGATTVL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 326 YEGgiiKNKHMED--DLWIAIVKHKVTHTFPSPSVFRYLIKTDPEGTIVRsKYDLSNLKEIWCGGEVIEESIPEYIEQKL 403
Cdd:cd05967 304 YEG---KPVGTPDpgAFWRVIEKYQVNALFTAPTAIRAIRKEDPDGKYIK-KYDLSSLRTLFLAGERLDPPTLEWAENTL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 404 KIKCLRVFGQSEIG---VTSFISVHALNIPYRATGVPSIYIRPSILSEEGEVLNSNEIGLVAFKLPMPPSFTITFYKNDE 480
Cdd:cd05967 380 GVPVIDHWWQTETGwpiTANPVGLEPLPIKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIKLPLPPGCLLTLWKNDE 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 481 KFKQL-FTRFPGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGILSPDCHTAPIGI 559
Cdd:cd05967 460 RFKKLyLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGL 539
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66822213 560 LVLKENPSIDLNKLQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQILSNLLNDPNYQLPDDVNDSELFYKI 637
Cdd:cd05967 540 VVLKEGVKITAEELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKIADGEDYTIPSTIEDPSVLDEI 617
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
52-613 |
8.30e-122 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 372.91 E-value: 8.30e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 52 WFKGGELNTCYNLLDIHIKnpAKRDQDALIYECPfLKKTIKLTYYQLYEKVCEFSRVLLNLNVSKNDNVLIFMANTLEPL 131
Cdd:COG0365 2 WFVGGRLNIAYNCLDRHAE--GRGDKVALIWEGE-DGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 132 IAMLSCARIGATQCTLFDGSSVKSLIDRIETITPKLIITTNYGILNDEIITFTPNLKEAIELSTfKPSNVItlfrneVLD 211
Cdd:COG0365 79 IAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEALEELP-SLEHVI------VVG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 212 ETklkkvQTIPTIPNTLSWYDEIKklkenNQSPFYEYVPVESSHPLYILYTSGTTGNTKAVVRSNGPHMVGIkYYTFR-- 289
Cdd:COG0365 152 RT-----GADVPMEGDLDWDELLA-----AASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHA-ATTAKyv 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 290 ---KESDipqIVFSHTNIGWVSFHG-FFYGLLSGGNTLVMYEGgiiKNKHME-DDLWIAIVKHKVTHTFPSPSVFRYLIK 364
Cdd:COG0365 221 ldlKPGD---VFWCTADIGWATGHSyIVYGPLLNGATVVLYEG---RPDFPDpGRLWELIEKYGVTVFFTAPTAIRALMK 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 365 TDPEgtiVRSKYDLSNLKEIWCGGEVIEESIPEYIEQKLKIKCLRVFGQSEIGvTSFISvhalNIPYR-----ATGVPSI 439
Cdd:COG0365 295 AGDE---PLKKYDLSSLRLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTETG-GIFIS----NLPGLpvkpgSMGKPVP 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 440 YIRPSILSEEGEVLNSNEIGLVAFKLPMpPSFTITFYKNDEKFKQ-LFTRFPGYYDSGDLGYKDQRGFYTIVSRSDDQIK 518
Cdd:COG0365 367 GYDVAVVDEDGNPVPPGEEGELVIKGPW-PGMFRGYWNDPERYREtYFGRFPGWYRTGDGARRDEDGYFWILGRSDDVIN 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 519 -----IGfnkiqlnT--IDTSILKHPSVLECCSIGIlsPDCH--TAPIGILVLKENPSIDlNKLQNEINNIITQDIESLA 589
Cdd:COG0365 446 vsghrIG-------TaeIESALVSHPAVAEAAVVGV--PDEIrgQVVKAFVVLKPGVEPS-DELAKELQAHVREELGPYA 515
|
570 580
....*....|....*....|....
gi 66822213 590 VLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:COG0365 516 YPREIEFVDELPKTRSGKIMRRLL 539
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
17-613 |
3.83e-108 |
|
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: 339.15 E-value: 3.83e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 17 SKSNPEAFWDEVAKKnVFWDKMYDKV--YSGDEIYPDWFKGGELNTCYNLLDIHIKNpaKRDQDALIYECPFLKKTIKLT 94
Cdd:cd05966 10 SIEDPEEFWGEIAKE-LDWFKPWDKVldWSKGPPFIKWFEGGKLNISYNCLDRHLKE--RGDKVAIIWEGDEPDQSRTIT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 95 YYQLYEKVCEFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGSSVKSLIDRIETITPKLIITTNYG 174
Cdd:cd05966 87 YRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRINDAQCKLVITADGG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 175 ILNDEIITFTPNLKEAIELsTFKPSNVITLFRNEvlDETKLKKVQTIptipntlsWYDEIKKlkenNQSPFYEYVPVESS 254
Cdd:cd05966 167 YRGGKVIPLKEIVDEALEK-CPSVEKVLVVKRTG--GEVPMTEGRDL--------WWHDLMA----KQSPECEPEWMDSE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 255 HPLYILYTSGTTGNTKAVVRSNGPHMVGIkYYTFR-----KESDipqIVFSHTNIGWVSFHGFF-YGLLSGGNTLVMYEG 328
Cdd:cd05966 232 DPLFILYTSGSTGKPKGVVHTTGGYLLYA-ATTFKyvfdyHPDD---IYWCTADIGWITGHSYIvYGPLANGATTVMFEG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 329 giIKNKHMEDDLWIAIVKHKVTHTFPSPSVFRYLIKtdpEGTIVRSKYDLSNLKEIWCGGEVIEesiPE----YIEQKLK 404
Cdd:cd05966 308 --TPTYPDPGRYWDIVEKHKVTIFYTAPTAIRALMK---FGDEWVKKHDLSSLRVLGSVGEPIN---PEawmwYYEVIGK 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 405 IKCLRV--FGQSEIG---VTSFISVHALNiPYRATgVPSIYIRPSILSEEGEVLNSNEIGLVAFKLPMpPSFTITFYKND 479
Cdd:cd05966 380 ERCPIVdtWWQTETGgimITPLPGATPLK-PGSAT-RPFFGIEPAILDEEGNEVEGEVEGYLVIKRPW-PGMARTIYGDH 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 480 EKFKQL-FTRFPGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGIlsPDCHT--AP 556
Cdd:cd05966 457 ERYEDTyFSKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGR--PHDIKgeAI 534
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 66822213 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 |
1.58e-102 |
|
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: 323.76 E-value: 1.58e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 17 SKSNPEAFWDEvAKKNVFWDKMYDKV----YSGDEIYPDWFKGGELNTCYNLLDIHIKNpaKRDQDALIYECPFLKKTIK 92
Cdd:cd17634 8 SINDPDTFWGE-AGKILDWITPYQKVkntsFAPGAPSIKWFEDATLNLAANALDRHLRE--NGDRTAIIYEGDDTSQSRT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 93 LTYYQLYEKVCEFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGSSVKSLIDRIETITPKLIITTN 172
Cdd:cd17634 85 ISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITAD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 173 YGILNDEIITFTPNLKEAIELSTFKPSNVITLFRNEVldetklkKVQTIPTipNTLSWYDEIKKlkennQSPFYEYVPVE 252
Cdd:cd17634 165 GGVRAGRSVPLKKNVDDALNPNVTSVEHVIVLKRTGS-------DIDWQEG--RDLWWRDLIAK-----ASPEHQPEAMN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 253 SSHPLYILYTSGTTGNTKAVVRSNGPHMVGIKyYTFRKESDI--PQIVFSHTNIGWVSFHGFF-YGLLSGGNTLVMYEGg 329
Cdd:cd17634 231 AEDPLFILYTSGTTGKPKGVLHTTGGYLVYAA-TTMKYVFDYgpGDIYWCTADVGWVTGHSYLlYGPLACGATTLLYEG- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 330 iIKNKHMEDDLWIAIVKHKVTHTFPSPSVFRYLIKTDPEGTivrSKYDLSNLKEIWCGGEVIE-ESIPEYIEQKLKIKCL 408
Cdd:cd17634 309 -VPNWPTPARMWQVVDKHGVNILYTAPTAIRALMAAGDDAI---EGTDRSSLRILGSVGEPINpEAYEWYWKKIGKEKCP 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 409 RV--FGQSEIGvTSFISVHALNIPYRA--TGVPSIYIRPSILSEEGEVLNSNEIGLVAFKLPMPPSfTITFYKNDEKFKQ 484
Cdd:cd17634 385 VVdtWWQTETG-GFMITPLPGAIELKAgsATRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPWPGQ-TRTLFGDHERFEQ 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 485 -LFTRFPGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGILSPDCHTAPIGILVLK 563
Cdd:cd17634 463 tYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLN 542
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 66822213 564 ENpSIDLNKLQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKI 608
Cdd:cd17634 543 HG-VEPSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
16-610 |
7.37e-100 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 318.05 E-value: 7.37e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 16 YSKSNPEAFWDEVAKKnVFWDKMYDKV--YSgDEIYPDWFKGGELNTCYNLLDIHIknPAKRDQDALIYECPFLKKTIKL 93
Cdd:PRK10524 10 RSIDDPEAFWAEQARR-IDWQTPFTQVldYS-NPPFARWFVGGRTNLCHNAVDRHL--AKRPEQLALIAVSTETDEERTY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 94 TYYQLYEKVCEFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGSSVKSLIDRIETITPKLIITTNY 173
Cdd:PRK10524 86 TFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAARIDDAKPVLIVSADA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 174 GILNDEIITFTPNLKEAIELSTFKPSNVITLFRNevLDEtklkkvqtIPTIPNTLSWYDEIKKLKENNQspfyeyVPV-- 251
Cdd:PRK10524 166 GSRGGKVVPYKPLLDEAIALAQHKPRHVLLVDRG--LAP--------MARVAGRDVDYATLRAQHLGAR------VPVew 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 252 -ESSHPLYILYTSGTTGNTKAVVRSNGPHMVGIKY---YTFRKESdiPQIVFSHTNIGWVSFHGFF-YGLLSGGNTLVMY 326
Cdd:PRK10524 230 lESNEPSYILYTSGTTGKPKGVQRDTGGYAVALATsmdTIFGGKA--GETFFCASDIGWVVGHSYIvYAPLLAGMATIMY 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 327 EG-------GIiknkhmeddlWIAIV-KHKVTHTFPSPSVFRYLIKTDPEgtiVRSKYDLSNLKEIWCGGEVIEESIPEY 398
Cdd:PRK10524 308 EGlptrpdaGI----------WWRIVeKYKVNRMFSAPTAIRVLKKQDPA---LLRKHDLSSLRALFLAGEPLDEPTASW 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 399 IEQKLKIKCLRVFGQSEIG---VTSFISVHALNIPYRATGVPSIYIRPSILSEE-GEVLNSNEIGLVAFKLPMPPSFTIT 474
Cdd:PRK10524 375 ISEALGVPVIDNYWQTETGwpiLAIARGVEDRPTRLGSPGVPMYGYNVKLLNEVtGEPCGPNEKGVLVIEGPLPPGCMQT 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 475 FYKNDEKF-KQLFTRF-PGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGILSPDC 552
Cdd:PRK10524 455 VWGDDDRFvKTYWSLFgRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALK 534
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66822213 553 HTAPIGILVLKENPSID----LNKLQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPR 610
Cdd:PRK10524 535 GQVAVAFVVPKDSDSLAdreaRLALEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLR 596
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
17-613 |
5.77e-92 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 297.44 E-value: 5.77e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 17 SKSNPEAFWDEVAKKnVFWDKMYDKVYSGDEIYPDWFKGGELNTCYNLLDIHIKNpaKRDQDALIYECPFLKKTIKLTYY 96
Cdd:PRK00174 26 SVEDPEGFWAEQAKR-LDWFKPFDTVLDWNAPFIKWFEDGELNVSYNCLDRHLKT--RGDKVAIIWEGDDPGDSRKITYR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 97 QLYEKVCEFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGSSVKSLIDRIETITPKLIITTNYGIL 176
Cdd:PRK00174 103 ELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVVFGGFSAEALADRIIDAGAKLVITADEGVR 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 177 NDEIITFTPNLKEAIELStfkPS--NVITLFRNEvldetklkkvQTIPTIPNTLSWYDEIKKlkenNQSPFYEYVPVESS 254
Cdd:PRK00174 183 GGKPIPLKANVDEALANC---PSveKVIVVRRTG----------GDVDWVEGRDLWWHELVA----GASDECEPEPMDAE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 255 HPLYILYTSGTTGNTKAVVRSNGPHMVGIkYYTFR-----KESDipqiVFSHT-NIGWVSFHGFF-YGLLSGGNTLVMYE 327
Cdd:PRK00174 246 DPLFILYTSGSTGKPKGVLHTTGGYLVYA-AMTMKyvfdyKDGD----VYWCTaDVGWVTGHSYIvYGPLANGATTLMFE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 328 GgiIKNKHMEDDLWIAIVKHKVTHTFPSPSVFRYLIKtdpEGTIVRSKYDLSNLKEIWCGGEVIEesiPE----YIEQKL 403
Cdd:PRK00174 321 G--VPNYPDPGRFWEVIDKHKVTIFYTAPTAIRALMK---EGDEHPKKYDLSSLRLLGSVGEPIN---PEawewYYKVVG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 404 KIKCLRV--FGQSEIG---VTSFISVHALNiPYRATgVPSIYIRPSILSEEGEVLNSNEIGLVAFKLPMpPSFTITFYKN 478
Cdd:PRK00174 393 GERCPIVdtWWQTETGgimITPLPGATPLK-PGSAT-RPLPGIQPAVVDEEGNPLEGGEGGNLVIKDPW-PGMMRTIYGD 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 479 DEKFKQ-LFTRFPGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGIlsPDCHT--A 555
Cdd:PRK00174 470 HERFVKtYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGR--PDDIKgqG 547
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 556 PIGILVLK--ENPSIDLNKlqnEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:PRK00174 548 IYAFVTLKggEEPSDELRK---ELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRIL 604
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
255-608 |
2.01e-76 |
|
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: 247.20 E-value: 2.01e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 255 HPLYILYTSGTTGNTKAVVRSNGPHMVGIKYYTFRKESDIPQIVFSHTNIGWVSFHGFFYGLLSGGNTLVMYEGGIIknk 334
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDP--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 335 hmeDDLWIAIVKHKVTHTFPSPSVFRYLIKTDPegtivRSKYDLSNLKEIWCGGEVIEESIPEYIEQKLKIKCLRVFGQS 414
Cdd:cd04433 78 ---EAALELIEREKVTILLGVPTLLARLLKAPE-----SAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 415 EIG-VTSFISVHALNIPYRATGVPSIYIRPSILSEEGEVLNSNEIGLVAFKLPMPPSFtitfYKNDEKFKQLFTRfPGYY 493
Cdd:cd04433 150 ETGgTVATGPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKG----YWNNPEATAAVDE-DGWY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 494 DSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGILSPDCHTAPIGILVLKENPSIDLnkl 573
Cdd:cd04433 225 RTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDA--- 301
|
330 340 350
....*....|....*....|....*....|....*
gi 66822213 574 qNEINNIITQDIESLAVLKKIIVINQLPKTKVGKI 608
Cdd:cd04433 302 -EELRAHVRERLAPYKVPRRVVFVDALPRTASGKI 335
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
9-613 |
4.11e-63 |
|
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: 220.05 E-value: 4.11e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 9 DYLNDNSYSKSNPEAFWDEVAKKNVF-WDKMYDKV--YSGDEIYPDWFKGGELNTCYNLLDIHIKNpaKRDQDALIYECP 85
Cdd:cd05968 8 DLEAFLERSAEDNAWFWGEFVKDVGIeWYEPPYQTldLSGGKPWAAWFVGGRMNIVEQLLDKWLAD--TRTRPALRWEGE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 86 flKKTIK-LTYYQLYEKVCEFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGSSVKSLIDRIETIT 164
Cdd:cd05968 86 --DGTSRtLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 165 PKLIITTNYGILNDEIITFTPNLKEAIElSTFKPSNVItlfrneVLDETKLKkvqtIPTIPNTLSWYDEIKKlkennqSP 244
Cdd:cd05968 164 AKALITADGFTRRGREVNLKEEADKACA-QCPTVEKVV------VVRHLGND----FTPAKGRDLSYDEEKE------TA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 245 FYEYVPVESSHPLYILYTSGTTGNTKAVVRSngpHM-VGIK-----YYTFR-KESDIpqiVFSHTNIGWVSFHGFFYGLL 317
Cdd:cd05968 227 GDGAERTESEDPLMIIYTSGTTGKPKGTVHV---HAgFPLKaaqdmYFQFDlKPGDL---LTWFTDLGWMMGPWLIFGGL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 318 SGGNTLVMYEGgiIKNKHMEDDLWIAIVKHKVTHTFPSPSVFRYLIktdPEGTIVRSKYDLSNLKEIWCGGEVIE-ESIP 396
Cdd:cd05968 301 ILGATMVLYDG--APDHPKADRLWRMVEDHEITHLGLSPTLIRALK---PRGDAPVNAHDLSSLRVLGSTGEPWNpEPWN 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 397 EYIEQKLKIKC--LRVFGQSEIGVTSFISVHALNIPYRATGVPSIYIRPSILSEEGEVLnSNEIGLVAFKLPMPpSFTIT 474
Cdd:cd05968 376 WLFETVGKGRNpiINYSGGTEISGGILGNVLIKPIKPSSFNGPVPGMKADVLDESGKPA-RPEVGELVLLAPWP-GMTRG 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 475 FYKNDEKF-KQLFTRFPGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGILSPDCH 553
Cdd:cd05968 454 FWRDEDRYlETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKG 533
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 554 TAPIGILVLKENPSiDLNKLQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:cd05968 534 EAIVCFVVLKPGVT-PTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVI 592
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
4-613 |
9.61e-61 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 214.76 E-value: 9.61e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 4 LSDPFDYLNDNSYSKSNPEAFWDEVAKKnVFWDKMY--DKVYSGD------EIYPDWFKGGELNTCYNLLDIHIKNpAKR 75
Cdd:PLN02654 26 VSSPQQYMEMYKRSVDDPAGFWSDIASQ-FYWKQKWegDEVCSENldvrkgPISIEWFKGGKTNICYNCLDRNVEA-GNG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 76 DQDALIYECPFLKKTIKLTYYQLYEKVCEFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGSSVKS 155
Cdd:PLN02654 104 DKIAIYWEGNEPGFDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAES 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 156 LIDRIETITPKLIITTNYGILNDEIITFTPNLKEAIELSTFKPSNVITLFRNEvlDETKLKKVQTIPTIPNTLSWYDEIK 235
Cdd:PLN02654 184 LAQRIVDCKPKVVITCNAVKRGPKTINLKDIVDAALDESAKNGVSVGICLTYE--NQLAMKREDTKWQEGRDVWWQDVVP 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 236 KLKENNQspfYEYVPVESshPLYILYTSGTTGNTKAVVRSNGPHMV----GIKYYTFRKESDipqIVFSHTNIGWVSFHG 311
Cdd:PLN02654 262 NYPTKCE---VEWVDAED--PLFLLYTSGSTGKPKGVLHTTGGYMVytatTFKYAFDYKPTD---VYWCTADCGWITGHS 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 312 FF-YGLLSGGNTLVMYEGgiIKNKHMEDDLWIAIVKHKVTHTFPSPSVFRYLIKtdpEGTIVRSKYDLSNLKEIWCGGEV 390
Cdd:PLN02654 334 YVtYGPMLNGATVLVFEG--APNYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMR---DGDEYVTRHSRKSLRVLGSVGEP 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 391 IEESIPEYI-----EQKLKIKclRVFGQSEIG---VTSFISVHALNiPYRATgVPSIYIRPSILSEEGEVLNSNEIGLVA 462
Cdd:PLN02654 409 INPSAWRWFfnvvgDSRCPIS--DTWWQTETGgfmITPLPGAWPQK-PGSAT-FPFFGVQPVIVDEKGKEIEGECSGYLC 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 463 FKLPMPPSFTiTFYKNDEKFK-QLFTRFPGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLE 541
Cdd:PLN02654 485 VKKSWPGAFR-TLYGDHERYEtTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAE 563
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66822213 542 CCSIGIlspDCHTAPIGI-----LVLKENPSIDLNKlqnEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:PLN02654 564 AAVVGI---EHEVKGQGIyafvtLVEGVPYSEELRK---SLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRIL 634
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
91-520 |
1.46e-55 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 194.45 E-value: 1.46e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 91 IKLTYYQLYEKVCEFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGSSVKSLIDRIETITPKLIIT 170
Cdd:pfam00501 20 RRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAKVLIT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 171 TNygilndeiitfTPNLKEAIElstfkpsnvitlfrnevlDETKLKKVQTIPTI-PNTLSWYDEIKKLKENNQSPFYEYV 249
Cdd:pfam00501 100 DD-----------ALKLEELLE------------------ALGKLEVVKLVLVLdRDPVLKEEPLPEEAKPADVPPPPPP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 250 PVESSHPLYILYTSGTTGNTKAVVRSngpH------MVGIKYYTFRKESDIPQIVFSHT-NIGWV-SFHGFFYGLLSGGN 321
Cdd:pfam00501 151 PPDPDDLAYIIYTSGTTGKPKGVMLT---HrnlvanVLSIKRVRPRGFGLGPDDRVLSTlPLFHDfGLSLGLLGPLLAGA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 322 TLVMYEGGiikNKHMEDDLWIAIVKHKVTHTFPSPSVFRYLIKTDPEgtivrSKYDLSNLKEIWCGGEVIEESIPEYIEQ 401
Cdd:pfam00501 228 TVVLPPGF---PALDPAALLELIERYKVTVLYGVPTLLNMLLEAGAP-----KRALLSSLRLVLSGGAPLPPELARRFRE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 402 KLKIKCLRVFGQSEigvTSFISVHALNIPYRATGVPSI-----YIRPSILSEE-GEVLNSNEIGLVAFKlpmPPSFTITF 475
Cdd:pfam00501 300 LFGGALVNGYGLTE---TTGVVTTPLPLDEDLRSLGSVgrplpGTEVKIVDDEtGEPVPPGEPGELCVR---GPGVMKGY 373
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 66822213 476 YKNDEKFKQLFTRfPGYYDSGDLGYKDQRGFYTIVSRSDDQIKIG 520
Cdd:pfam00501 374 LNDPELTAEAFDE-DGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
76-613 |
7.92e-51 |
|
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: 182.32 E-value: 7.92e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 76 DQDALIYEcpflkkTIKLTYYQLYEKVCEFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGSSVKS 155
Cdd:COG0318 14 DRPALVFG------GRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 156 LIDRIETITPKLIITtnygilndeiitftpnlkeaielstfkpsnvitlfrnevldetklkkvqtiptipntlswydeik 235
Cdd:COG0318 88 LAYILEDSGARALVT----------------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 236 klkennqspfyeyvpvesshpLYILYTSGTTGNTKAVVRSNGP---HMVGIKYYTFRKESDI-----PqivFSHTNiGWV 307
Cdd:COG0318 103 ---------------------ALILYTSGTTGRPKGVMLTHRNllaNAAAIAAALGLTPGDVvlvalP---LFHVF-GLT 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 308 sfHGFFYGLLSGGnTLVMYEggiiknKHMEDDLWIAIVKHKVTHTFPSPSVFRYLIKTDPegtivRSKYDLSNLKEIWCG 387
Cdd:COG0318 158 --VGLLAPLLAGA-TLVLLP------RFDPERVLELIERERVTVLFGVPTMLARLLRHPE-----FARYDLSSLRLVVSG 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 388 GEVIEESIPEYIEQKLKIKCLRVFGQSEIGVTSFISVHALNIPYRAT-GVPSIYIRPSILSEEGEVLNSNEIGLVAFKlp 466
Cdd:COG0318 224 GAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPEDPGERRPGSvGRPLPGVEVRIVDEDGRELPPGEVGEIVVR-- 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 467 mPPSFTITFYKNDEKFKQLFTrfPGYYDSGDLGYKDQRGFYTIVSRSDDQIKI-GFNkIQLNTIDTSILKHPSVLECCSI 545
Cdd:COG0318 302 -GPNVMKGYWNDPEATAEAFR--DGWLRTGDLGRLDEDGYLYIVGRKKDMIISgGEN-VYPAEVEEVLAAHPGVAEAAVV 377
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66822213 546 GILSPDCHTAPIGILVLKENPSIDLNKLQNEINNIITqdieSLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:COG0318 378 GVPDEKWGERVVAFVVLRPGAELDAEELRAFLRERLA----RYKVPRRVEFVDELPRTASGKIDRRAL 441
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
93-613 |
8.01e-51 |
|
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: 182.32 E-value: 8.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 93 LTYYQLYEKVCEFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGSSVKSLIDRIETITPKLIITTn 172
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITT- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 173 ygilndeiitftPNLKEAIELSTfkpsnvitlfrnevldetklkkvqtiptipntlswydeikklkennqspfyeyvpve 252
Cdd:cd05969 80 ------------EELYERTDPED--------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 253 sshPLYILYTSGTTGNTKAVVRSngpHMVGIKYY-TFRKESDI-PQIVFSHT-NIGWVSfhGFFYGLLS---GGNTLVMY 326
Cdd:cd05969 91 ---PTLLHYTSGTTGTPKGVLHV---HDAMIFYYfTGKYVLDLhPDDIYWCTaDPGWVT--GTVYGIWApwlNGVTNVVY 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 327 EGGIIKNKhmeddlWIAIVK-HKVTHTFPSPSVFRYLIKtdpEGTIVRSKYDLSNLKEIWCGGEVIEESIPEYIEQKLKI 405
Cdd:cd05969 163 EGRFDAES------WYGIIErVKVTVWYTAPTAIRMLMK---EGDELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGV 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 406 KCLRVFGQSEIGVTSFISVHALNIPYRATGVPSIYIRPSILSEEGEVLNSNEIGLVAFKlPMPPSFTITFYKNDEKFKQL 485
Cdd:cd05969 234 PIHDTWWQTETGSIMIANYPCMPIKPGSMGKPLPGVKAAVVDENGNELPPGTKGILALK-PGWPSMFRGIWNDEERYKNS 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 486 FTRfpGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGILSPDCHTAPIGILVLKEN 565
Cdd:cd05969 313 FID--GWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEG 390
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 66822213 566 --PSidlNKLQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:cd05969 391 fePS---DELKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVL 437
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
16-608 |
5.04e-43 |
|
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: 163.98 E-value: 5.04e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 16 YSKSNPEAFWDEVAK-KNVFWDKMYDKVYSGDEIYPD--WFKGGELNTCYNLLdihikNPAKRDQDALIYECPFLKKTiK 92
Cdd:cd05943 25 WSVDDPGAFWAAVWDfSGVRGSKPYDVVVVSGRIMPGarWFPGARLNYAENLL-----RHADADDPAAIYAAEDGERT-E 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 93 LTYYQLYEKVCEFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGSSVKSLIDRIETITPKLIITTN 172
Cdd:cd05943 99 VTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPGVLDRFGQIEPKVLFAVD 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 173 YGILND----------EIITFTPNLKEAIelstfkpsnvitlfrneVLDETKLKKVQTIPTIPNTLSWYDEIkkLKENNQ 242
Cdd:cd05943 179 AYTYNGkrhdvrekvaELVKGLPSLLAVV-----------------VVPYTVAAGQPDLSKIAKALTLEDFL--ATGAAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 243 SPFYEYVPVesSHPLYILYTSGTTGNTKAVVRSNG----PHMvgikyytfrKE----SDIP--QIVFSHTNIGWVSFHGF 312
Cdd:cd05943 240 ELEFEPLPF--DHPLYILYSSGTTGLPKCIVHGAGgtllQHL---------KEhilhCDLRpgDRLFYYTTCGWMMWNWL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 313 FYGLLSGGnTLVMYEGGIIKNKhmEDDLWIAIVKHKVTHTFPSPSVFRYLIKTdpeGTIVRSKYDLSNLKEIWCGGEVIE 392
Cdd:cd05943 309 VSGLAVGA-TIVLYDGSPFYPD--TNALWDLADEEGITVFGTSAKYLDALEKA---GLKPAETHDLSSLRTILSTGSPLK 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 393 ESIPEYIEQKLKikcLRVFGQSEIGVTSFISVHALnipyratGVPSIYIRPS------------ILSEEGEVLnSNEIG- 459
Cdd:cd05943 383 PESFDYVYDHIK---PDVLLASISGGTDIISCFVG-------GNPLLPVYRGeiqcrglgmaveAFDEEGKPV-WGEKGe 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 460 LVAFKlPMpPSFTITFYkNDE---KFKQ-LFTRFPGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILK 535
Cdd:cd05943 452 LVCTK-PF-PSMPVGFW-NDPdgsRYRAaYFAKYPGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEK 528
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66822213 536 HPSVLECCSIGILSPDCHTAPIGILVLKENPSIDlNKLQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKI 608
Cdd:cd05943 529 IPEVEDSLVVGQEWKDGDERVILFVKLREGVELD-DELRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKK 600
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
93-613 |
1.30e-40 |
|
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: 153.65 E-value: 1.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 93 LTYYQLYEKVCEFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGSSVKSLIDRIETITPKLIITtn 172
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 173 ygilndeiitftpnlkeaielstfkpsnvitlfrnevldetklkkvqtiptipntlswydeikklkennqspfyeyvpvE 252
Cdd:cd05972 79 -------------------------------------------------------------------------------D 79
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 253 SSHPLYILYTSGTTGNTKAVVRSNG---PHMVGIKYYTFRKESDIpqiVFSHTNIGWVSFHGF-FYGLLSGGNTLVMYEG 328
Cdd:cd05972 80 AEDPALIYFTSGTTGLPKGVLHTHSyplGHIPTAAYWLGLRPDDI---HWNIADPGWAKGAWSsFFGPWLLGATVFVYEG 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 329 giiknKHMEDDLWIAIV-KHKVTHTFPSPSVFRYLIKTDPEGtivrskYDLSNLKEIWCGGEVIEESIPEYIEQKLKIKC 407
Cdd:cd05972 157 -----PRFDAERILELLeRYGVTSFCGPPTAYRMLIKQDLSS------YKFSHLRLVVSAGEPLNPEVIEWWRAATGLPI 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 408 LRVFGQSEIGVTsFISVHALNIPYRATGVPSIYIRPSILSEEGEVLNSNEIGLVAFKLPmPPSFTITFYKNDEKFKQLFT 487
Cdd:cd05972 226 RDGYGQTETGLT-VGNFPDMPVKPGSMGRPTPGYDVAIIDDDGRELPPGEEGDIAIKLP-PPGLFLGYVGDPEKTEASIR 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 488 RfpGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGilSPDchtaPI------GILV 561
Cdd:cd05972 304 G--DYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVG--SPD----PVrgevvkAFVV 375
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 66822213 562 LKENpSIDLNKLQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:cd05972 376 LTSG-YEPSEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVEL 426
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
39-613 |
1.89e-39 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 152.74 E-value: 1.89e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 39 YDKVYSG---DEI--YPDWFKGGELNTCYNLLDIHIKNPaKRDQDALIYECPflKKTIKLTYYQLYEKVCEFSRVLLNLN 113
Cdd:PRK04319 18 YEETYATfswEEVekEFSWLETGKVNIAYEAIDRHADGG-RKDKVALRYLDA--SRKEKYTYKELKELSNKFANVLKELG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 114 VSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGSSVKSLIDRIETITPKLIITTNygilndeiitftpnlkeaiel 193
Cdd:PRK04319 95 VEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTP--------------------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 194 stfkpsnviTLFRNEVLDET-KLKKV----QTIPTIPNTLSWYDEIkklkeNNQSPFYEYVPVESSHPLYILYTSGTTGN 268
Cdd:PRK04319 154 ---------ALLERKPADDLpSLKHVllvgEDVEEGPGTLDFNALM-----EQASDEFDIEWTDREDGAILHYTSGSTGK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 269 TKAVVRSNGP---HMVGIKYYTFRKESDI------PqivfshtniGWVSfhGFFYGL---LSGGNTLVMYEGgiiknkHM 336
Cdd:PRK04319 220 PKGVLHVHNAmlqHYQTGKYVLDLHEDDVywctadP---------GWVT--GTSYGIfapWLNGATNVIDGG------RF 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 337 EDDLWIAIV-KHKVTHTFPSPSVFRYLIKTDPEgtiVRSKYDLSNLKEIWCGGEVIEesiPEYIEQKLKIKCLRV---FG 412
Cdd:PRK04319 283 SPERWYRILeDYKVTVWYTAPTAIRMLMGAGDD---LVKKYDLSSLRHILSVGEPLN---PEVVRWGMKVFGLPIhdnWW 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 413 QSEIGVTSFISVHALNIPYRATGVPSIYIRPSILSEEGEVLNSNEIGLVAFKLPMPPSFTiTFYKNDEKFKQLFtrFPGY 492
Cdd:PRK04319 357 MTETGGIMIANYPAMDIKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAIKKGWPSMMR-GIWNNPEKYESYF--AGDW 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 493 YDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGIlsPDCHTAPI--GILVLKEN--PSi 568
Cdd:PRK04319 434 YVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGK--PDPVRGEIikAFVALRPGyePS- 510
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 66822213 569 dlNKLQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:PRK04319 511 --EELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVL 553
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
92-608 |
6.17e-39 |
|
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: 150.06 E-value: 6.17e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 92 KLTYYQLYEKVCEFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGSSVKSLIDRIETITPKLIITT 171
Cdd:cd05911 10 ELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 172 NYGIlndeiitftPNLKEAIELSTFKPSnvITLFRNevldetklkKVQTIPTIPNTLSWYDEIKKlkennqsPFYEYVPV 251
Cdd:cd05911 90 PDGL---------EKVKEAAKELGPKDK--IIVLDD---------KPDGVLSIEDLLSPTLGEED-------EDLPPPLK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 252 ES-SHPLYILYTSGTTGNTKAVVRS------NGPHMVGIKYYTFRKESdipqIVFSHTNIGWVSfhGFFYGLLSggntlv 324
Cdd:cd05911 143 DGkDDTAAILYSSGTTGLPKGVCLShrnliaNLSQVQTFLYGNDGSND----VILGFLPLYHIY--GLFTTLAS------ 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 325 MYEG--GIIKNKhMEDDLWIAIV-KHKVTHTFPSPSVFRYLIKtDPEGTivrsKYDLSNLKEIWCGGEVIEESIPEYIEQ 401
Cdd:cd05911 211 LLNGatVIIMPK-FDSELFLDLIeKYKITFLYLVPPIAAALAK-SPLLD----KYDLSSLRVILSGGAPLSKELQELLAK 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 402 KLKIKCLRV-FGQSEIGVTSFISVHALNIPyRATG--VPSIYIRpsILSEEG-EVLNSNEIGLVAFKLP--MPPsftitF 475
Cdd:cd05911 285 RFPNATIKQgYGMTETGGILTVNPDGDDKP-GSVGrlLPNVEAK--IVDDDGkDSLGPNEPGEICVRGPqvMKG-----Y 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 476 YKNDEKFKQLFTRfPGYYDSGDLGYKDQRGFYTIVSRSDDQIKigFNKIQL--NTIDTSILKHPSVLECCSIGILSPDCH 553
Cdd:cd05911 357 YNNPEATKETFDE-DGWLHTGDIGYFDEDGYLYIVDRKKELIK--YKGFQVapAELEAVLLEHPGVADAAVIGIPDEVSG 433
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 66822213 554 TAPIGILVLKENPSIDLNKLQNEINniitqdiESLAVLKK----IIVINQLPKTKVGKI 608
Cdd:cd05911 434 ELPRAYVVRKPGEKLTEKEVKDYVA-------KKVASYKQlrggVVFVDEIPKSASGKI 485
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
112-610 |
4.22e-34 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 136.86 E-value: 4.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 112 LNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGSSVKSLIDRIETITPKLIITTNYGILNDEIitftpnlKEAI 191
Cdd:cd05970 67 MGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIAEDNIPEEI-------EKAA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 192 ELSTfkpsnvitlfrnevldeTKLKKVQTIPTIPNtlSWYDEIKKLKenNQSPFYEYVPVESSH----PLYILYTSGTTG 267
Cdd:cd05970 140 PECP-----------------SKPKLVWVGDPVPE--GWIDFRKLIK--NASPDFERPTANSYPcgedILLVYFSSGTTG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 268 NTKAVVRSNG-P--HMVGIKYYTFRKESDIPQIVfshTNIGWV-SFHGFFYGLLSGGNTLVMYEGGIIKNKHMEDdlwiA 343
Cdd:cd05970 199 MPKMVEHDFTyPlgHIVTAKYWQNVREGGLHLTV---ADTGWGkAVWGKIYGQWIAGAAVFVYDYDKFDPKALLE----K 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 344 IVKHKVTHTFPSPSVFRYLIKTDpegtivRSKYDLSNLKEIWCGGEVIEESIPEYIEQKLKIKCLRVFGQSEIGVTsFIS 423
Cdd:cd05970 272 LSKYGVTTFCAPPTIYRFLIRED------LSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETTLT-IAT 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 424 VHALNIPYRATGVPSIYIRPSILSEEGEVLNSNEIGLVAFKLP--MPPSFTITFYKNDEKFKQLFtrFPGYYDSGDLGYK 501
Cdd:cd05970 345 FPWMEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSkgKPVGLFGGYYKDAEKTAEVW--HDGYYHTGDAAWM 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 502 DQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGIlsPDchtaPIGILVLKenPSIDLNK-------LQ 574
Cdd:cd05970 423 DEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGV--PD----PIRGQVVK--ATIVLAKgyepseeLK 494
|
490 500 510
....*....|....*....|....*....|....*.
gi 66822213 575 NEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPR 610
Cdd:cd05970 495 KELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRR 530
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
92-613 |
7.75e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 135.70 E-value: 7.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 92 KLTYYQLYEKVCEFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGAtqctlfdgssvkslidrietitpkLIITT 171
Cdd:PRK06187 31 RTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGA------------------------VLHPI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 172 NYgILNDEIITFTPNLKEAielstfkpsnVITLFRNEVLDET-----KLKKVQTI------PTIPNTLSW--YDEIKklk 238
Cdd:PRK06187 87 NI-RLKPEEIAYILNDAED----------RVVLVDSEFVPLLaailpQLPTVRTVivegdgPAAPLAPEVgeYEELL--- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 239 eNNQSPFYEYVPVESSHPLYILYTSGTTGNTKAVvrsngphmvgikYYTFRkesdipQIvFSHTN-----IGWVS----- 308
Cdd:PRK06187 153 -AAASDTFDFPDIDENDAAAMLYTSGTTGHPKGV------------VLSHR------NL-FLHSLavcawLKLSRddvyl 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 309 -----FH----GFFY-GLLSGGNtlvmyegGIIKNKHMEDDLWIAIVKHKVTHTFPSPSVFRYLIKtDPEgtivRSKYDL 378
Cdd:PRK06187 213 vivpmFHvhawGLPYlALMAGAK-------QVIPRRFDPENLLDLIETERVTFFFAVPTIWQMLLK-APR----AYFVDF 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 379 SNLKEIWCGGEVIEESIPEYIEQKLKIKCLRVFGQSE---IGVTSFISVHALN-IPYR-ATG--VPSIYIRpsILSEEGE 451
Cdd:PRK06187 281 SSLRLVIYGGAALPPALLREFKEKFGIDLVQGYGMTEtspVVSVLPPEDQLPGqWTKRrSAGrpLPGVEAR--IVDDDGD 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 452 VL--NSNEIGLVAFKlpmPPSFTITFYKNDEKFKQLFTrfPGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTI 529
Cdd:PRK06187 359 ELppDGGEVGEIIVR---GPWLMQGYWNRPEATAETID--GGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPREL 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 530 DTSILKHPSVLECCSIGIlsPDCHT--APIGILVLKENPSIDlnklQNEINNIITQDIESLAVLKKIIVINQLPKTKVGK 607
Cdd:PRK06187 434 EDALYGHPAVAEVAVIGV--PDEKWgeRPVAVVVLKPGATLD----AKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGK 507
|
....*.
gi 66822213 608 IPRQIL 613
Cdd:PRK06187 508 ILKRVL 513
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
252-613 |
1.19e-30 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 125.24 E-value: 1.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 252 ESSHPLYILYTSGTTGNTKAVVRSN----GpHMVGIKYY--TFRKESDIpqiVFSHTNIGWVSfhGFFYGLLSG---GNT 322
Cdd:cd05971 86 GSDDPALIIYTSGTTGPPKGALHAHrvllG-HLPGVQFPfnLFPRDGDL---YWTPADWAWIG--GLLDVLLPSlyfGVP 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 323 LVMYeggiiKNKHMEDDLWIAIVK-HKVTHTFPSPSVFRyLIKTDPEGtivRSKYDLsNLKEIWCGGEVIEESIPEYIEQ 401
Cdd:cd05971 160 VLAH-----RMTKFDPKAALDLMSrYGVTTAFLPPTALK-MMRQQGEQ---LKHAQV-KLRAIATGGESLGEELLGWARE 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 402 KLKIKCLRVFGQSEigvTSFISVHALNI-PYR--ATGVPSIYIRPSILSEEGEVLNSNEIGLVAFKLPMPPSFtITFYKN 478
Cdd:cd05971 230 QFGVEVNEFYGQTE---CNLVIGNCSALfPIKpgSMGKPIPGHRVAIVDDNGTPLPPGEVGEIAVELPDPVAF-LGYWNN 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 479 DEKFKQLFTRfpGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGIlsPDchtaPIG 558
Cdd:cd05971 306 PSATEKKMAG--DWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGI--PD----PIR 377
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 559 ILVLKE----NPSI-DLNKLQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:cd05971 378 GEIVKAfvvlNPGEtPSDALAREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRREL 437
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
16-608 |
1.28e-28 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 121.44 E-value: 1.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 16 YSKSNPEAFWDEVakknvfWD------KMYDKVYSGDEIYPD--WFKGGELNTCYNLLDIHiknpaKRDQDALIYECPfL 87
Cdd:PRK03584 42 WSVEDLEAFWQSV------WDffgvigSTPYTVVLAGRRMPGarWFPGARLNYAENLLRHR-----RDDRPAIIFRGE-D 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 88 KKTIKLTYYQLYEKVCEFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQctlfdgSS------VKSLIDRIE 161
Cdd:PRK03584 110 GPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIW------SScspdfgVQGVLDRFG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 162 TITPKLIITTN---YG-----ILND--EIITFTPNLKEAIELStfkpsnvitlfrnevldetKLKKVQTIPTIPNTLSWY 231
Cdd:PRK03584 184 QIEPKVLIAVDgyrYGgkafdRRAKvaELRAALPSLEHVVVVP-------------------YLGPAAAAAALPGALLWE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 232 DeikkLKENNQSPFYEYVPVESSHPLYILYTSGTTGNTKAVVRSNG----PHMvgikyytfrKE----SDI-PQ-IVFSH 301
Cdd:PRK03584 245 D----FLAPAEAAELEFEPVPFDHPLWILYSSGTTGLPKCIVHGHGgillEHL---------KElglhCDLgPGdRFFWY 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 302 TNIGW------VSfhgffyGLLSGGnTLVMYEGGIIKNKHmeDDLWIAIVKHKVTHTFPSPSVFRYLIKtdpEGTIVRSK 375
Cdd:PRK03584 312 TTCGWmmwnwlVS------GLLVGA-TLVLYDGSPFYPDP--NVLWDLAAEEGVTVFGTSAKYLDACEK---AGLVPGET 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 376 YDLSNLKEIWCGGEVIEESIPEYIEQKLKiKCLRVFGQSeiG----VTSFI------SVHALNIPYRATGVpsiyiRPSI 445
Cdd:PRK03584 380 HDLSALRTIGSTGSPLPPEGFDWVYEHVK-ADVWLASIS--GgtdiCSCFVggnpllPVYRGEIQCRGLGM-----AVEA 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 446 LSEEGEVLnSNEIG-LVAFKlPMpPSFTITFYkNDEKFKQL----FTRFPGYYDSGDLGYKDQRGFYTIVSRSDDQI--- 517
Cdd:PRK03584 452 WDEDGRPV-VGEVGeLVCTK-PF-PSMPLGFW-NDPDGSRYrdayFDTFPGVWRHGDWIEITEHGGVVIYGRSDATLnrg 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 518 --KIGFNKI--QLNTIdtsilkhPSVLECCSIGILSPDchtapiG----IL--VLKENPSIDlNKLQNEINNIITQDIES 587
Cdd:PRK03584 528 gvRIGTAEIyrQVEAL-------PEVLDSLVIGQEWPD------GdvrmPLfvVLAEGVTLD-DALRARIRTTIRTNLSP 593
|
650 660
....*....|....*....|.
gi 66822213 588 LAVLKKIIVINQLPKTKVGKI 608
Cdd:PRK03584 594 RHVPDKIIAVPDIPRTLSGKK 614
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
91-613 |
5.65e-28 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 118.40 E-value: 5.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 91 IKLTYYQLYEKVCEFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGSSVKSLIDRIETITPKLIIT 170
Cdd:cd17642 43 VNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFC 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 171 TNYGIlnDEIITFtpnlkeaielstfkpsnvitlfrnevldETKLKKVQTIPTIPNT--LSWYDEIKKLKENNQSP---F 245
Cdd:cd17642 123 SKKGL--QKVLNV----------------------------QKKLKIIKTIIILDSKedYKGYQCLYTFITQNLPPgfnE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 246 YEYVPVESSHP---LYILYTSGTTGNTKAVVRsngPHMVGIKYYTFRKESDIPQIVFSHTNIGWVS--FHGF----FYGL 316
Cdd:cd17642 173 YDFKPPSFDRDeqvALIMNSSGSTGLPKGVQL---THKNIVARFSHARDPIFGNQIIPDTAILTVIpfHHGFgmftTLGY 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 317 LSGGNTLVMYEggiiknkHMEDDLWI-AIVKHKVTHTFPSPSVFRYLIKTdpegTIVrSKYDLSNLKEIWCGGEVIEESI 395
Cdd:cd17642 250 LICGFRVVLMY-------KFEEELFLrSLQDYKVQSALLVPTLFAFFAKS----TLV-DKYDLSNLHEIASGGAPLSKEV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 396 PEYIEQKLKIKCLRV-FGQSEIGVTSFISVHALNIPyRATG--VPSIYIRpSILSEEGEVLNSNEIGLVAFKLPMppsfT 472
Cdd:cd17642 318 GEAVAKRFKLPGIRQgYGLTETTSAILITPEGDDKP-GAVGkvVPFFYAK-VVDLDTGKTLGPNERGELCVKGPM----I 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 473 ITFYKNDEKFKQLFTRFPGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGILSPDC 552
Cdd:cd17642 392 MKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDA 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66822213 553 HTAPIGILVLKENPSIDlnklQNEINNIITQDIESLAVLK-KIIVINQLPKTKVGKIPRQIL 613
Cdd:cd17642 472 GELPAAVVVLEAGKTMT----EKEVMDYVASQVSTAKRLRgGVKFVDEVPKGLTGKIDRRKI 529
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
93-610 |
4.03e-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: 114.63 E-value: 4.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 93 LTYYQLYEKVCEFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLfdgssvkslidrietitpkliittN 172
Cdd:cd17631 21 LTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPL------------------------N 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 173 YGILNDEIitftpnlkeaielstfkpSNVITLFRNEVLdetklkkvqtiptipntlswYDEikklkennqspfyeyvpve 252
Cdd:cd17631 77 FRLTPPEV------------------AYILADSGAKVL--------------------FDD------------------- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 253 sshPLYILYTSGTTGNTKAVVRSNGphMVGIKYYTfrkesdipQIVFSHTNIGWVSFHGF--FYGLLSGGNTL-VMYEGG 329
Cdd:cd17631 100 ---LALLMYTSGTTGRPKGAMLTHR--NLLWNAVN--------ALAALDLGPDDVLLVVAplFHIGGLGVFTLpTLLRGG 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 330 --IIKNKHMEDDLWIAIVKHKVTHTFPSPSVFrYLIKTDPEgtivRSKYDLSNLKEIWCGGE-VIEESIPEYIEQKLKIk 406
Cdd:cd17631 167 tvVILRKFDPETVLDLIERHRVTSFFLVPTMI-QALLQHPR----FATTDLSSLRAVIYGGApMPERLLRALQARGVKF- 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 407 cLRVFGQSEI--GVTSFISVHALNIPyRATGVPSIYIRPSILSEEGEVLNSNEIGLVAFKLP--MPpsftiTFYKNDEKF 482
Cdd:cd17631 241 -VQGYGMTETspGVTFLSPEDHRRKL-GSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPhvMA-----GYWNRPEAT 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 483 KQLFtrFPGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGILSPDCHTAPIGILVL 562
Cdd:cd17631 314 AAAF--RDGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVP 391
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 66822213 563 KENPSIDLNKLqneinniITQDIESLA---VLKKIIVINQLPKTKVGKIPR 610
Cdd:cd17631 392 RPGAELDEDEL-------IAHCRERLArykIPKSVEFVDALPRNATGKILK 435
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
61-613 |
1.43e-26 |
|
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: 113.43 E-value: 1.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 61 CYNLLDIHIKNPakrDQDALIyecpFLKKtiKLTYYQLYEKVCEFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARI 140
Cdd:cd05936 2 ADLLEEAARRFP---DKTALI----FMGR--KLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 141 GATqctlfdgssvkslidrietitpklIITTNYGILNDEIitftpnlkEAIelstFKPSNVITLFRNEVLdETKLKKvqt 220
Cdd:cd05936 73 GAV------------------------VVPLNPLYTPREL--------EHI----LNDSGAKALIVAVSF-TDLLAA--- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 221 iptipntlswydeikklkennQSPFYEYVPVESSHPLYILYTSGTTGNTKAVVRSNGpHMV-----GIKYYTFRKESD-- 293
Cdd:cd05936 113 ---------------------GAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHR-NLVanalqIKAWLEDLLEGDdv 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 294 ----IPqivFSHTnigwvsfhgffYGLLSGGNtLVMYEGG--IIKNKHMEDDLWIAIVKHKVTHtFPS-PSVFRYLIKTd 366
Cdd:cd05936 171 vlaaLP---LFHV-----------FGLTVALL-LPLALGAtiVLIPRFRPIGVLKEIRKHRVTI-FPGvPTMYIALLNA- 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 367 PEgtivRSKYDLSNLKEIWCGGEVIEESIPEYIEQKLKIKCLRVFGQSEigvTS-FISVHALNIPYRA----TGVPSIYI 441
Cdd:cd05936 234 PE----FKKRDFSSLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTE---TSpVVAVNPLDGPRKPgsigIPLPGTEV 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 442 RpsILSEEGEVLNSNEIGLVAFKlpmPPSFTITFYKNDEKFKQLFTRfpGYYDSGDLGYKDQRGFYTIVSRSDDQIkI-- 519
Cdd:cd05936 307 K--IVDDDGEELPPGEVGELWVR---GPQVMKGYWNRPEETAEAFVD--GWLRTGDIGYMDEDGYFFIVDRKKDMI-Ivg 378
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 520 GFNkIQLNTIDTSILKHPSVLECCSIGILSPDCHTAPIGILVLKENPSIDLNKlqneinnIITQDIESLA---VLKKIIV 596
Cdd:cd05936 379 GFN-VYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTEEE-------IIAFCREQLAgykVPRQVEF 450
|
570
....*....|....*..
gi 66822213 597 INQLPKTKVGKIPRQIL 613
Cdd:cd05936 451 RDELPKSAVGKILRREL 467
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
94-608 |
1.99e-25 |
|
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: 110.41 E-value: 1.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 94 TYYQLYEKVCEFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATqctlfdgssvkslidrIETITPKL----II 169
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAV----------------LHTINPRLfpeqIA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 170 ttnYgILN---DEIITFTPNLKEAIE--LSTFKP-SNVITLFRNEVLDEtklkkvqtiPTIPNTLSWYDEIkklkeNNQS 243
Cdd:cd12119 91 ---Y-IINhaeDRVVFVDRDFLPLLEaiAPRLPTvEHVVVMTDDAAMPE---------PAGVGVLAYEELL-----AAES 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 244 PFYEYVPVESSHPLYILYTSGTTGNTKAVV---RSNGPHMVGIKYYTFR--KESDI--PQIVFSHTNiGWvsfhGFFYGL 316
Cdd:cd12119 153 PEYDWPDFDENTAAAICYTSGTTGNPKGVVyshRSLVLHAMAALLTDGLglSESDVvlPVVPMFHVN-AW----GLPYAA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 317 LSGGNTLVMyeggiiKNKHMEDDLWIAIVK-HKVTHTFPSPSVFRYLIKTdPEGTivrsKYDLSNLKEIWCGGEVIEESI 395
Cdd:cd12119 228 AMVGAKLVL------PGPYLDPASLAELIErEGVTFAAGVPTVWQGLLDH-LEAN----GRDLSSLRRVVIGGSAVPRSL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 396 PEYIEQKLkIKCLRVFGQSE---IGVTSFISVHALNIP------YRA-TGVPSIYIRPSILSEEGEVL--NSNEIG-LVA 462
Cdd:cd12119 297 IEAFEERG-VRVIHAWGMTEtspLGTVARPPSEHSNLSedeqlaLRAkQGRPVPGVELRIVDDDGRELpwDGKAVGeLQV 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 463 fklpMPPSFTITFYKNDEKfKQLFTRfPGYYDSGDLGYKDQRGFYTIVSRSDDQIKIG---FNKIQLNTIdtsILKHPSV 539
Cdd:cd12119 376 ----RGPWVTKSYYKNDEE-SEALTE-DGWLRTGDVATIDEDGYLTITDRSKDVIKSGgewISSVELENA---IMAHPAV 446
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66822213 540 LECCSIGILSPDCHTAPIGILVLKENPSIDlnklQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKI 608
Cdd:cd12119 447 AEAAVIGVPHPKWGERPLAVVVLKEGATVT----AEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKI 511
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
258-610 |
3.01e-24 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 106.01 E-value: 3.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 258 YILYTSGTTGNTKAVVRSNGphmvgiKYYTFR----------KESD----IPQIVFshtniGWVSFHGFFYGLLSGGNTL 323
Cdd:cd05919 95 YLLYSSGTTGPPKGVMHAHR------DPLLFAdamarealglTPGDrvfsSAKMFF-----GYGLGNSLWFPLAVGASAV 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 324 VMYEggiiknKHMEDDLWIAIVKHKVTHTFPSPSVFRYLIktdPEGTIvrSKYDLSNLKEIWCGGEVIEESIPEYIEQKL 403
Cdd:cd05919 164 LNPG------WPTAERVLATLARFRPTVLYGVPTFYANLL---DSCAG--SPDALRSLRLCVSAGEALPRGLGERWMEHF 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 404 KIKCLRVFGQSEIGVTsFISVHALNIPYRATG--VPSIYIRpsILSEEGEVLNSNEIGLVAFKLPmppSFTITFYKNDEK 481
Cdd:cd05919 233 GGPILDGIGATEVGHI-FLSNRPGAWRLGSTGrpVPGYEIR--LVDEEGHTIPPGEEGDLLVRGP---SAAVGYWNNPEK 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 482 FKQLFTRfpGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGILSPDCHTAPIGILV 561
Cdd:cd05919 307 SRATFNG--GWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVV 384
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 66822213 562 LKeNPSIDLNKLQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPR 610
Cdd:cd05919 385 LK-SPAAPQESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQR 432
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
62-613 |
1.14e-23 |
|
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: 105.14 E-value: 1.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 62 YNLLDIHIKNPAKR--DQDALIYecpflkKTIKLTYYQLYEKVCEFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCAR 139
Cdd:cd05959 3 YNAATLVDLNLNEGrgDKTAFID------DAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 140 IGATQC---TLFDGSSVKSLID----RIETITPKliittnygilndeiitFTPNLKEAIELStfkpsnvitlfrnEVLDE 212
Cdd:cd05959 77 AGIVPVpvnTLLTPDDYAYYLEdsraRVVVVSGE----------------LAPVLAAALTKS-------------EHTLV 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 213 TkLKKVQTIPTIPNTLSWYDEIKKLkennqSPFYEYVPVESSHPLYILYTSGTTGNTKAVVrsngpHMVGIKYYTFR--- 289
Cdd:cd05959 128 V-LIVSGGAGPEAGALLLAELVAAE-----AEQLKPAATHADDPAFWLYSSGSTGRPKGVV-----HLHADIYWTAElya 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 290 ------KESDIpqiVFSHTNIgwvsfhgFF-YGL-------LSGGNTLVMYEGgiiknKHMEDDLWIAIVKHKVTHTFPS 355
Cdd:cd05959 197 rnvlgiREDDV---CFSAAKL-------FFaYGLgnsltfpLSVGATTVLMPE-----RPTPAAVFKRIRRYRPTVFFGV 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 356 PSVFRYLIKTDpegtiVRSKYDLSNLKEIWCGGEVIEESIPEYIEQKLKIKCLRVFGQSEIGVTsFISVHALNIPYRATG 435
Cdd:cd05959 262 PTLYAAMLAAP-----NLPSRDLSSLRLCVSAGEALPAEVGERWKARFGLDILDGIGSTEMLHI-FLSNRPGRVRYGTTG 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 436 VPSIYIRPSILSEEGEVLNSNEIGLVAFKlpmPPSFTITFYKNDEKFKQLFTrfPGYYDSGDLGYKDQRGFYTIVSRSDD 515
Cdd:cd05959 336 KPVPGYEVELRDEDGGDVADGEPGELYVR---GPSSATMYWNNRDKTRDTFQ--GEWTRTGDKYVRDDDGFYTYAGRADD 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 516 QIKIGFNKIQLNTIDTSILKHPSVLECCSIGILSPDCHTAPIGILVLKENpSIDLNKLQNEINNIITQDIESLAVLKKII 595
Cdd:cd05959 411 MLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPG-YEDSEALEEELKEFVKDRLAPYKYPRWIV 489
|
570
....*....|....*...
gi 66822213 596 VINQLPKTKVGKIPRQIL 613
Cdd:cd05959 490 FVDELPKTATGKIQRFKL 507
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
255-610 |
8.75e-23 |
|
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: 99.79 E-value: 8.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 255 HPLYILYTSGTTGNTKAVVRSNGPHMVgikyyTFRKESDIPQIvfSHTNI----GWVSFHGFFYGLLSggntlVMYEGG- 329
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIE-----SFVCNEDLFNI--SGEDAilapGPLSHSLFLYGAIS-----ALYLGGt 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 330 -IIKNKHMEDDLWIAIVKHKVTHTFPSPSVFRYLIKTD-PEGTIvrskydlsnlKEIWCGGEVIEESIPEYIEQKL-KIK 406
Cdd:cd17633 69 fIGQRKFNPKSWIRKINQYNATVIYLVPTMLQALARTLePESKI----------KSIFSSGQKLFESTKKKLKNIFpKAN 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 407 CLRVFGQSEigvTSFISVHALN--IPYRATGVPSIYIRPSILSEEGevlnsNEIGLVAFKLPMPPSFTIT--FYKNDekf 482
Cdd:cd17633 139 LIEFYGTSE---LSFITYNFNQesRPPNSVGRPFPNVEIEIRNADG-----GEIGKIFVKSEMVFSGYVRggFSNPD--- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 483 kqlftrfpGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGIlsPDCHTAPIGILVL 562
Cdd:cd17633 208 --------GWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGI--PDARFGEIAVALY 277
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 66822213 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 |
1.42e-22 |
|
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: 101.07 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 76 DQDALIYEcpflkkTIKLTYYQLYEKVCEFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATqCTLFDgssVKS 155
Cdd:cd05930 2 DAVAVVDG------DQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAA-YVPLD---PSY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 156 LIDRIETI----TPKLIITtnygilndeiitftpnlkeaielstfkpsnvitlfrnevldetklkkvqtiptipntlswy 231
Cdd:cd05930 72 PAERLAYIledsGAKLVLT------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 232 deikklkennqspfyeyvpvESSHPLYILYTSGTTGNTKAVVrsnGPHMvGIKYYTFRKESDIP----QIVFSHTNIGW- 306
Cdd:cd05930 91 --------------------DPDDLAYVIYTSGSTGKPKGVM---VEHR-GLVNLLLWMQEAYPltpgDRVLQFTSFSFd 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 307 VSFHGFFYGLLSGGnTLVMYEGGIIKNkhmEDDLWIAIVKHKVTHTFPSPSVFRYLIKTDPEGtivrskyDLSNLKEIWC 386
Cdd:cd05930 147 VSVWEIFGALLAGA-TLVVLPEEVRKD---PEALADLLAEEGITVLHLTPSLLRLLLQELELA-------ALPSLRLVLV 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 387 GGEVIEESIPEYIEQKLkiKCLRVF---GQSE--IGVTSFiSVHALNIPYRAT--GVP----SIYI-----RPSILSEEG 450
Cdd:cd05930 216 GGEALPPDLVRRWRELL--PGARLVnlyGPTEatVDATYY-RVPPDDEEDGRVpiGRPipntRVYVldenlRPVPPGVPG 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 451 EV-----------LNSNEigLVAFKlpmppsFTITFYKNDEKfkqlftrfpgYYDSGDLGYKDQRGfyTIV--SRSDDQI 517
Cdd:cd05930 293 ELyiggaglargyLNRPE--LTAER------FVPNPFGPGER----------MYRTGDLVRWLPDG--NLEflGRIDDQV 352
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 518 KI-GFnKIQLNTIDTSILKHPSVLECCSIGILSPDCHTAPIGILVLKENPSIDLNKLQNEINniitqdiESL---AVLKK 593
Cdd:cd05930 353 KIrGY-RIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDEEELRAHLA-------ERLpdyMVPSA 424
|
570
....*....|....*..
gi 66822213 594 IIVINQLPKTKVGKIPR 610
Cdd:cd05930 425 FVVLDALPLTPNGKVDR 441
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
93-619 |
2.55e-22 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 100.70 E-value: 2.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 93 LTYYQLYEKVCEFSRVLLN-LNVSKNDNVLIFMANTLEPLIAMLSCARIGATqctlfdgssvkslidrietITPkliitt 171
Cdd:PRK06839 28 MTYKQLHEYVSKVAAYLIYeLNVKKGERIAILSQNSLEYIVLLFAIAKVECI-------------------AVP------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 172 nygiLNdeiITFTPNlkeaiELS-TFKPSNVITL-----FRNEVLDETKLKKVQtiPTIpntlswydEIKKLKENNQSPF 245
Cdd:PRK06839 83 ----LN---IRLTEN-----ELIfQLKDSGTTVLfvektFQNMALSMQKVSYVQ--RVI--------SITSLKEIEDRKI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 246 YEYVPVESSHPLYILYTSGTTGNTKAVVRS------NGPHMVGIKYYTFRKESDIPQIVFSHTNIGWVSFHGFFYGllsg 319
Cdd:PRK06839 141 DNFVEKNESASFIICYTSGTTGKPKGAVLTqenmfwNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAFPTLFAG---- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 320 gntlvmyeGGIIKNKHMEDDLWIAIV-KHKVTHTFPSPSVFRYLIKtdpegTIVRSKYDLSNLKEIWCGGE-VIEESIPE 397
Cdd:PRK06839 217 --------GVIIVPRKFEPTKALSMIeKHKVTVVMGVPTIHQALIN-----CSKFETTNLQSVRWFYNGGApCPEELMRE 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 398 YIEQKLKIKclRVFGQSEIGVTSF-ISVHALNIPYRATGVPSIYIRPSILSEEGEVLNSNEIGLVAFKLPMppsfTITFY 476
Cdd:PRK06839 284 FIDRGFLFG--QGFGMTETSPTVFmLSEEDARRKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPN----VMKEY 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 477 KNDEKFKQLFTRfPGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGILSPDCHTAP 556
Cdd:PRK06839 358 WNRPDATEETIQ-DGWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIP 436
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66822213 557 IGILVLKENPSIdlnkLQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQILSNLLND 619
Cdd:PRK06839 437 IAFIVKKSSSVL----IEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQLKS 495
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
93-615 |
1.02e-21 |
|
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: 98.36 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 93 LTYYQLYEKVCEFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGSSVKSLIDRIETITPKLIITtn 172
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 173 ygilndeiitftpnlkeaielstfkpsnvitlfrnevlDETKLKKVqtiptipntlswydeikklkennqspfyeyvpve 252
Cdd:cd05973 79 --------------------------------------DAANRHKL---------------------------------- 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 253 SSHPLYILYTSGTTGNTKAVVRSNGPHMVGIKYYTF----RKESdipqIVFSHTNIGWVsfHGFFY---GLLSGGNTLVM 325
Cdd:cd05973 87 DSDPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDavdlRPED----SFWNAADPGWA--YGLYYaitGPLALGHPTIL 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 326 YEGGIiknkhMEDDLWIAIVKHKVTHTFPSPSVFRYLIkTDPEGTIVRSKydlSNLKEIWCGGEVIEESIPEYIEQKLKI 405
Cdd:cd05973 161 LEGGF-----SVESTWRVIERLGVTNLAGSPTAYRLLM-AAGAEVPARPK---GRLRRVSSAGEPLTPEVIRWFDAALGV 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 406 KCLRVFGQSEIGVTsFISVHALNIPYRA--TGVPSIYIRPSILSEEGEVLNSNEIGLVAFKLPMPPSFTITFYKNDEkfk 483
Cdd:cd05973 232 PIHDHYGQTELGMV-LANHHALEHPVHAgsAGRAMPGWRVAVLDDDGDELGPGEPGRLAIDIANSPLMWFRGYQLPD--- 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 484 qlfTRFP--GYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGIlsPDCHTAPI--GI 559
Cdd:cd05973 308 ---TPAIdgGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGV--PDPERTEVvkAF 382
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 66822213 560 LVLKEN--PSIDLNKlqnEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQILSN 615
Cdd:cd05973 383 VVLRGGheGTPALAD---ELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
243-615 |
1.66e-21 |
|
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: 98.69 E-value: 1.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 243 SPFYEYVPVESSHPLYILYTSGTTGNTKAVVRSNGPHMVGIK----YYTFRKESDIpqiVFSHTNIGWV--SFHGFFYGL 316
Cdd:cd05928 163 STEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKvngrYWLDLTASDI---MWNTSDTGWIksAWSSLFEPW 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 317 LSGGNTLVmyeggiiknKHME--DDLWI--AIVKHKVTHTFPSPSVFRYLIKTDpegtivRSKYDLSNLKEIWCGGEVIE 392
Cdd:cd05928 240 IQGACVFV---------HHLPrfDPLVIlkTLSSYPITTFCGAPTVYRMLVQQD------LSSYKFPSLQHCVTGGEPLN 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 393 ESIPEYIEQKLKIKCLRVFGQSEIGVTSFISvHALNIPYRATGVPSIYIRPSILSEEGEVLNSNEIGLVAFKL-PMPPSF 471
Cdd:cd05928 305 PEVLEKWKAQTGLDIYEGYGQTETGLICANF-KGMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRVkPIRPFG 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 472 TITFYKnDEKFKQLFTRFPGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGilSPD 551
Cdd:cd05928 384 LFSGYV-DNPEKTAATIRGDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVS--SPD 460
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66822213 552 chtaPIGILVLKE----NP---SIDLNKLQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQILSN 615
Cdd:cd05928 461 ----PIRGEVVKAfvvlAPqflSHDPEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRD 527
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
90-615 |
2.00e-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: 2.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 90 TIKLTYYQLYEKVCEFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGSSVKSLIDRIETITPKLII 169
Cdd:cd05926 12 TPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 170 TTNYGilNDEIITFTPNLKEAIELSTFKPSNVITLFRNEvldetklkkvqtipTIPNTLSWYDEIKKLKennqspfyeyv 249
Cdd:cd05926 92 TPKGE--LGPASRAASKLGLAILELALDVGVLIRAPSAE--------------SLSNLLADKKNAKSEG----------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 250 PVESSHPLYILYTSGTTGNTKAVVRSNGPHMVGIKYY--TFR-KESDIPQIV--FSHTnigwvsfHGFFYGLLSggnTLv 324
Cdd:cd05926 145 VPLPDDLALILHTSGTTGRPKGVPLTHRNLAASATNItnTYKlTPDDRTLVVmpLFHV-------HGLVASLLS---TL- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 325 mYEGG--IIKNKHMEDDLWIAIVKHKVTHTFPSPSVFRYLIKT-DPEGTIVRSKydlsnLKEIWCGGEVIEESIPEYIEQ 401
Cdd:cd05926 214 -AAGGsvVLPPRFSASTFWPDVRDYNATWYTAVPTIHQILLNRpEPNPESPPPK-----LRFIRSCSASLPPAVLEALEA 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 402 KLKIKCLRVFGQSEigVTSFISVHALNIPYRATG-VPsiyiRPS-----ILSEEGEVLNSNEIGLVAFKlpmPPSFTITF 475
Cdd:cd05926 288 TFGAPVLEAYGMTE--AAHQMTSNPLPPGPRKPGsVG----KPVgvevrILDEDGEILPPGVVGEICLR---GPNVTRGY 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 476 YKNDEKFKQLFTRFpGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGIlsPDCH-- 553
Cdd:cd05926 359 LNNPEANAEAAFKD-GWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGV--PDEKyg 435
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66822213 554 ---TAPIgilVLKENPSIDlnklQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQILSN 615
Cdd:cd05926 436 eevAAAV---VLREGASVT----EEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
91-608 |
5.17e-20 |
|
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: 93.55 E-value: 5.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 91 IKLTYYQLYEKVCEFSRVLLNLNVSkNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGSSVKSLIDRIETITPKLIIT 170
Cdd:cd05909 6 TSLTYRKLLTGAIALARKLAKMTKE-GENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 171 TNygilndeiiTFTPNLKEAIELSTFKPSNVITL--FRNEVldeTKLKKVQTIPTIPNTLSWYDEIKKLkennqspfyey 248
Cdd:cd05909 85 SK---------QFIEKLKLHHLFDVEYDARIVYLedLRAKI---SKADKCKAFLAGKFPPKWLLRIFGV----------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 249 VPVESSHPLYILYTSGTTGNTKAVVRSNGPHMVGIKYYTFRKESDIPQIVFSHTNIgwvsFHGF------FYGLLSGGNt 322
Cdd:cd05909 142 APVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPF----FHSFgltgclWLPLLSGIK- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 323 LVMY----EGGIIKNkhmeddlwiAIVKHKVTHTFPSPSVFRYLIKTdpegtivRSKYDLSNLKEIWCGGEVIEESIPEY 398
Cdd:cd05909 217 VVFHpnplDYKKIPE---------LIYDKKATILLGTPTFLRGYARA-------AHPEDFSSLRLVVAGAEKLKDTLRQE 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 399 IEQKLKIKCLRVFGQSEigVTSFISVHALNIPYRATGV----PSIYIRpsILSEEG-EVLNSNEIGLVAFKlpmPPSFTI 473
Cdd:cd05909 281 FQEKFGIRILEGYGTTE--CSPVISVNTPQSPNKEGTVgrplPGMEVK--IVSVEThEEVPIGEGGLLLVR---GPNVML 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 474 TFYKNDEKFKQLFTRfpGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKH-PSVLECCSIGIlsPDC 552
Cdd:cd05909 354 GYLNEPELTSFAFGD--GWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSV--PDG 429
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 66822213 553 HTAPIGILVLKEnPSIDLNKLQNEINNIitqDIESLAVLKKIIVINQLPKTKVGKI 608
Cdd:cd05909 430 RKGEKIVLLTTT-TDTDPSSLNDILKNA---GISNLAKPSYIHQVEEIPLLGTGKP 481
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
93-613 |
2.67e-19 |
|
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: 91.00 E-value: 2.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 93 LTYYQLYEKVCEFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATqctlfdgssvkslidrietitpkliittn 172
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAV----------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 173 ygilndeIITFTPNLKEAiELSTF-KPSNVITLFRNEVLDETKLkkvqtiptipntlswydeikklkennqspfyeyvpv 251
Cdd:cd05935 53 -------VVPINPMLKER-ELEYIlNDSGAKVAVVGSELDDLAL------------------------------------ 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 252 esshplyILYTSGTTGNTKAVVRSNG---PHMVGIKYYTFRKESDIpqIVFSHTNIGWVSFHGFFYGLLSGGNTLVMYeg 328
Cdd:cd05935 89 -------IPYTSGTTGLPKGCMHTHFsaaANALQSAVWTGLTPSDV--ILACLPLFHVTGFVGSLNTAVYVGGTYVLM-- 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 329 giikNKHMEDDLWIAIVKHKVTHTFPSPSVFRYLIKTdPEgtivRSKYDLSNLKEIWCGGEVIEESIPEYIEQKLKIKCL 408
Cdd:cd05935 158 ----ARWDRETALELIEKYKVTFWTNIPTMLVDLLAT-PE----FKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFV 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 409 RVFGQSEIgvtsfISVHALNIPYR----ATGVPSIYIRPSILS-EEGEVLNSNEIGLVAFKlpmPPSFTITFYKNDEKFK 483
Cdd:cd05935 229 EGYGLTET-----MSQTHTNPPLRpklqCLGIP*FGVDARVIDiETGRELPPNEVGEIVVR---GPQIFKGYWNRPEETE 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 484 QLFTRFPG--YYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGILSPDCHTAPIGILV 561
Cdd:cd05935 301 ESFIEIKGrrFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIV 380
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 66822213 562 LKenPSIDLNKLQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:cd05935 381 LR--PEYRGKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
256-550 |
5.10e-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. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 90.04 E-value: 5.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 256 PLYILYTSGTTGNTKAVVRSNGpHMVGIKYYTFR----KESDIPQIV--FSHTNIGWVSfhgfFYGLLSGGNTLVMYEgg 329
Cdd:cd05934 83 PASILYTSGTTGPPKGVVITHA-NLTFAGYYSARrfglGEDDVYLTVlpLFHINAQAVS----VLAALSVGATLVLLP-- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 330 iiknKHMEDDLWIAIVKHKVTHTFPSPSVFRYLIKTDPegtivrSKYDLSNLKEIWCGGEVIEESIPEYIEqKLKIKCLR 409
Cdd:cd05934 156 ----RFSASRFWSDVRRYGATVTNYLGAMLSYLLAQPP------SPDDRAHRLRAAYGAPNPPELHEEFEE-RFGVRLLE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 410 VFGQSEIGVTsFISVHALNIPYRATGVPSIYIRPSILSEEGEVLNSNEIGLVAFKLPMPPSFTITFYKNDEKFKQLFTRf 489
Cdd:cd05934 225 GYGMTETIVG-VIGPRDEPRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIRGLRGWGFFKGYYNMPEATAEAMRN- 302
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66822213 490 pGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGILSP 550
Cdd:cd05934 303 -GWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDE 362
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
261-613 |
2.06e-18 |
|
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: 88.30 E-value: 2.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 261 YTSGTTGNTKAVV----------RSNGPHMVGIKyytfrkESD----IPQIVFShtnigwvsfhgffYGLlsGGNTLVMY 326
Cdd:cd05958 104 FTSGTTGAPKATMhfhrdplasaDRYAVNVLRLR------EDDrfvgSPPLAFT-------------FGL--GGVLLFPF 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 327 EGG---IIKNKHMEDDLWIAIVKHKVTHTFPSPSVFRYLIKTDPEGtivrsKYDLSNLKEIWCGGEVIEESIPEYIEQKL 403
Cdd:cd05958 163 GVGasgVLLEEATPDLLLSAIARYKPTVLFTAPTAYRAMLAHPDAA-----GPDLSSLRKCVSAGEALPAALHRAWKEAT 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 404 KIKCLRVFGQSEIgVTSFISVHALNIPYRATGVPSIYIRPSILSEEGEVLNSNEIGLVAFKLPmppsfTITFYKNDEKFK 483
Cdd:cd05958 238 GIPIIDGIGSTEM-FHIFISARPGDARPGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRGP-----TGCRYLADKRQR 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 484 QLFTRfpGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGILSPDCHTAPIGILVLK 563
Cdd:cd05958 312 TYVQG--GWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLR 389
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 66822213 564 ENPSIDlNKLQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:cd05958 390 PGVIPG-PVLARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFAL 438
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
242-608 |
2.22e-18 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 88.60 E-value: 2.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 242 QSPFYEYVPVESshPLYILYTSGTTGNTKAVVRSNGP--------HMVGIKYytfrkeSDIPQIV--------FSHTNIg 305
Cdd:PRK12406 142 QQEPYDGPPVPQ--PQSMIYTSGTTGHPKGVRRAAPTpeqaaaaeQMRALIY------GLKPGIRalltgplyHSAPNA- 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 306 wvsfhgffYGLLSG--GNTLVMyeggiiKNKHMEDDLWIAIVKHKVTHTFPSPSVFRYLIKTDPEgtiVRSKYDLSNLKE 383
Cdd:PRK12406 213 --------YGLRAGrlGGVLVL------QPRFDPEELLQLIERHRITHMHMVPTMFIRLLKLPEE---VRAKYDVSSLRH 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 384 IW-----CGGEVIEESI----PEYIEqklkikclrVFGQSEIGVTSF-ISVHALNIPyRATGVPSIYIRPSILSEEGEVL 453
Cdd:PRK12406 276 VIhaaapCPADVKRAMIewwgPVIYE---------YYGSTESGAVTFaTSEDALSHP-GTVGKAAPGAELRFVDEDGRPL 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 454 NSNEIGLVAFKLPMPPSFTitfYKN-DEKFKQLftRFPGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTS 532
Cdd:PRK12406 346 PQGEIGEIYSRIAGNPDFT---YHNkPEKRAEI--DRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAV 420
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66822213 533 ILKHPSVLECCSIGIlsPDCHTAPIGILVLKENPSIDLnklqnEINNIITQDIESLA---VLKKIIVINQLPKTKVGKI 608
Cdd:PRK12406 421 LHAVPGVHDCAVFGI--PDAEFGEALMAVVEPQPGATL-----DEADIRAQLKARLAgykVPKHIEIMAELPREDSGKI 492
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
249-610 |
7.48e-18 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 86.73 E-value: 7.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 249 VPVESSHPLYILYTSGTTGNTKAVVRSNGPHMVG----IKYYTFRKESDIPQIVfshtnigwvSFHgFFYGL------LS 318
Cdd:cd05922 112 HEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANarsiAEYLGITADDRALTVL---------PLS-YDYGLsvlnthLL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 319 GGNTLVMYEGGIiknkhMEDDLWIAIVKHKVTHTFPSPSVFRYL--IKTDPEGtivrskydLSNLKEIW-CGGEVIEESI 395
Cdd:cd05922 182 RGATLVLTNDGV-----LDDAFWEDLREHGATGLAGVPSTYAMLtrLGFDPAK--------LPSLRYLTqAGGRLPQETI 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 396 PEYIEQKLKIKCLRVFGQSE-IGVTSFISVHALNIPYRATGVPSIYIRPSILSEEGEVLNSNEIGLVAFKLPmppsFTIT 474
Cdd:cd05922 249 ARLRELLPGAQVYVMYGQTEaTRRMTYLPPERILEKPGSIGLAIPGGEFEILDDDGTPTPPGEPGEIVHRGP----NVMK 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 475 FYKNDEKFKQLFTRFPGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGIlsPDCHT 554
Cdd:cd05922 325 GYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGL--PDPLG 402
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 66822213 555 APIGILVLKEnPSIDLnklqNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPR 610
Cdd:cd05922 403 EKLALFVTAP-DKIDP----KDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDY 453
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
93-619 |
1.05e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 86.37 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 93 LTYYQLYEKVCEfSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGSSVKSLIDRIETITPKLIITTN 172
Cdd:PRK07638 27 LTYKDWFESVCK-VANWLNEKESKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNADMIVTER 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 173 YgilndeiitftpnlkeaielstfkpsnvitlFRNEVLDEtklkKVQTIptipntlSWyDEIKKLKENNQSpfyEYVPVE 252
Cdd:PRK07638 106 Y-------------------------------KLNDLPDE----EGRVI-------EI-DEWKRMIEKYLP---TYAPIE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 253 SSH--PLYILYTSGTTGNTKAVVRSNGP--HMVGIKYYTFRKESD----IP-QIVFSHtnigwvsfhgFFYGLLSggnTL 323
Cdd:PRK07638 140 NVQnaPFYMGFTSGSTGKPKAFLRAQQSwlHSFDCNVHDFHMKREdsvlIAgTLVHSL----------FLYGAIS---TL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 324 VMYEGGIIKNKHMEDDL--WIAIVKHKVTHTFPSPSVFRYLIKTDPEgtivrskydlSNLKEIWCGGEVIEESIPEYIEQ 401
Cdd:PRK07638 207 YVGQTVHLMRKFIPNQVldKLETENISVMYTVPTMLESLYKENRVIE----------NKMKIISSGAKWEAEAKEKIKNI 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 402 KLKIKCLRVFGQSEIGVTSFISVHALNIPYRATGVPSIYIRPSILSEEGEVLNSNEIGLVAFKLPMppSFTitFYKNDEK 481
Cdd:PRK07638 277 FPYAKLYEFYGASELSFVTALVDEESERRPNSVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQ--FFM--GYIIGGV 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 482 FKQLFTRfPGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGIlsPDCHTAPIGILV 561
Cdd:PRK07638 353 LARELNA-DGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGV--PDSYWGEKPVAI 429
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 66822213 562 LKENPsidlNKLQneINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQILSNLLND 619
Cdd:PRK07638 430 IKGSA----TKQQ--LKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSWIEN 481
|
|
| ACAS_N |
pfam16177 |
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many ... |
16-63 |
2.07e-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: 76.36 E-value: 2.07e-17
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 66822213 16 YSKSNPEAFWDEVAKKnVFWDKMYDKVYSGDE-IYPDWFKGGELNTCYN 63
Cdd:pfam16177 7 RSIEDPEGFWGEVAKE-LDWFKPFDKVLDGSNgPFAKWFVGGKLNVCYN 54
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
93-613 |
2.11e-17 |
|
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: 85.36 E-value: 2.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 93 LTYYQLYEKVCEFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGSSVKSLIDRIETITPKLIITTN 172
Cdd:cd05904 33 LTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 173 ygilndeiiTFTPNLKEAielstfkpsnvitlfrnevldetkLKKVQTIPTIPNTLSWYDEIKKLKENNQSPFyeyVPVE 252
Cdd:cd05904 113 ---------ELAEKLASL------------------------ALPVVLLDSAEFDSLSFSDLLFEADEAEPPV---VVIK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 253 SSHPLYILYTSGTTGNTKAVVRSngpH-----MVGIkYYTFRKESDIPQIV------FSHTnigwVSFHGFFYGLLSGGN 321
Cdd:cd05904 157 QDDVAALLYSSGTTGRSKGVMLT---HrnliaMVAQ-FVAGEGSNSDSEDVflcvlpMFHI----YGLSSFALGLLRLGA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 322 TLV---MYEGGIIKNkhmeddlwiAIVKHKVTHTFPSPSVFRYLIKtDPEGtivrSKYDLSNLKEIWCGG-----EVIEE 393
Cdd:cd05904 229 TVVvmpRFDLEELLA---------AIERYKVTHLPVVPPIVLALVK-SPIV----DKYDLSSLRQIMSGAaplgkELIEA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 394 sipeyieqklkikCLRVFGQSEIG-----------VTSFISVHALNIPYRATG--VPSIYIRpsILS-EEGEVLNSNEIG 459
Cdd:cd05904 295 -------------FRAKFPNVDLGqgygmtestgvVAMCFAPEKDRAKYGSVGrlVPNVEAK--IVDpETGESLPPNQTG 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 460 LVAFKLPMppsfTITFYKNDEKFKQLFTRFPGYYDSGDLGYKDQRGFYTIVSRSDDQIKigFNKIQ-----LNTIdtsIL 534
Cdd:cd05904 360 ELWIRGPS----IMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIK--YKGFQvapaeLEAL---LL 430
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66822213 535 KHPSVLECCSIGILSPDCHTAPIGILVLKENPSIDlnklQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:cd05904 431 SHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLT----EDEIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
70-608 |
2.40e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 85.37 E-value: 2.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 70 KNPAKRdqdALIYEcpflkkTIKLTYYQLYEKVCEFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGAtqctlfd 149
Cdd:PRK08316 23 RYPDKT---ALVFG------DRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGA------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 150 gssvkslidrietitpkLIITTNYGILNDEI----------ITFT-PNLKEAIElstfkpsnvitlfrnEVLDETKLKKV 218
Cdd:PRK08316 87 -----------------VHVPVNFMLTGEELayildhsgarAFLVdPALAPTAE---------------AALALLPVDTL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 219 QTIPTIPNTL---SWYDEIKKLKenNQSPFYEYVPVESSHPLYILYTSGTTGNTKAVVRSNGPHM-------VGIKYytf 288
Cdd:PRK08316 135 ILSLVLGGREapgGWLDFADWAE--AGSVAEPDVELADDDLAQILYTSGTESLPKGAMLTHRALIaeyvsciVAGDM--- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 289 rKESDIPQIVFS--HTnigwVSFHGFFYGLLSGGNTLVMYEGGIIknkhmeDDLWIAIVKHKVTHTFPSPSVFRYLIktd 366
Cdd:PRK08316 210 -SADDIPLHALPlyHC----AQLDVFLGPYLYVGATNVILDAPDP------ELILRTIEAERITSFFAPPTVWISLL--- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 367 pegtivRS----KYDLSNLKEIWCG-----GEVIEEsipeyIEQKL-KIKCLRVFGQSEIGvtsfisvhalniPYrAT-- 434
Cdd:PRK08316 276 ------RHpdfdTRDLSSLRKGYYGasimpVEVLKE-----LRERLpGLRFYNCYGQTEIA------------PL-ATvl 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 435 ------------GVPSIYIRPSILSEEGEVLNSNEIGLVAFKlpmPPSFTITFYKNDEKFKQLFTrfPGYYDSGDLGYKD 502
Cdd:PRK08316 332 gpeehlrrpgsaGRPVLNVETRVVDDDGNDVAPGEVGEIVHR---SPQLMLGYWDDPEKTAEAFR--GGWFHSGDLGVMD 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 503 QRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGILSPDCHTAPIGILVLKENPSIDLNKLqneinniIT 582
Cdd:PRK08316 407 EEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTEDEL-------IA 479
|
570 580
....*....|....*....|....*....
gi 66822213 583 QDIESLA---VLKKIIVINQLPKTKVGKI 608
Cdd:PRK08316 480 HCRARLAgfkVPKRVIFVDELPRNPSGKI 508
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
248-613 |
2.43e-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: 85.03 E-value: 2.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 248 YVPVESSHPLY-------------------ILYTSGTTGNTKAVV--RSNGPHMVG--IKYYTFRKESDIPQIV-FSHTn 303
Cdd:cd05941 64 AVPLNPSYPLAeleyvitdsepslvldpalILYTSGTTGRPKGVVltHANLAANVRalVDAWRWTEDDVLLHVLpLHHV- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 304 igwvsfHGFFYGL---LSGGNTLVMyeggiiknkHMEDDLWI-AIVKHK--VTHTFPSPSVFRYLIKT---DPEGTIVRS 374
Cdd:cd05941 143 ------HGLVNALlcpLFAGASVEF---------LPKFDPKEvAISRLMpsITVFMGVPTIYTRLLQYyeaHFTDPQFAR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 375 KYDLSNLKEIWCGGEVIEESIPEYIEQKLKIKCLRVFGQSEIGVtsfisvhALNIPY----RATGV----PSIYIRpsIL 446
Cdd:cd05941 208 AAAAERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTEIGM-------ALSNPLdgerRPGTVgmplPGVQAR--IV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 447 SEE-GEVLNSNEIGLVAFKlpmPPSFTITFYKNDEKFKQLFTRfPGYYDSGDLGYKDQRGFYTIVSR-SDDQIKIGFNKI 524
Cdd:cd05941 279 DEEtGEPLPRGEVGEIQVR---GPSVFKEYWNKPEATKEEFTD-DGWFKTGDLGVVDEDGYYWILGRsSVDIIKSGGYKV 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 525 QLNTIDTSILKHPSVLECCSIGILSPDCHTAPIGILVLKEN-PSIDLNKLQNEINniitqdiESLAVLK---KIIVINQL 600
Cdd:cd05941 355 SALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGaAALSLEELKEWAK-------QRLAPYKrprRLILVDEL 427
|
410
....*....|...
gi 66822213 601 PKTKVGKIPRQIL 613
Cdd:cd05941 428 PRNAMGKVNKKEL 440
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
92-616 |
3.66e-17 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 85.07 E-value: 3.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 92 KLTYYQLYEKVCEFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQC---TLFDGSSVKSLIDRIEtitPKLI 168
Cdd:PLN03102 39 RFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNpinTRLDATSIAAILRHAK---PKIL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 169 ITTNygilndeiiTFTPNLKEAIELSTFKPS--NVITLFRNEVlDETKLKKVQTIPtipntlswYDEIKKLKENNQSPFY 246
Cdd:PLN03102 116 FVDR---------SFEPLAREVLHLLSSEDSnlNLPVIFIHEI-DFPKRPSSEELD--------YECLIQRGEPTPSLVA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 247 EYVPVESSH-PLYILYTSGTTGNTKAVVRSN-GPHMVGIKYYTFRKESDIPQIVFS----HTNiGWVsfhgFFYGLLSGG 320
Cdd:PLN03102 178 RMFRIQDEHdPISLNYTSGTTADPKGVVISHrGAYLSTLSAIIGWEMGTCPVYLWTlpmfHCN-GWT----FTWGTAARG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 321 NTLVMYeggiiknKHME-DDLWIAIVKHKVTHTFPSPSVFRYLIKTD-------------------PEGTIVRSKYDLS- 379
Cdd:PLN03102 253 GTSVCM-------RHVTaPEIYKNIEMHNVTHMCCVPTVFNILLKGNsldlsprsgpvhvltggspPPAALVKKVQRLGf 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 380 ------NLKE-----IWCGGEVIEESIPEYIEQKLKIK-CLRVFGQSEIGVTSFISVHAlnIPYRATGVPSIYIRPSILS 447
Cdd:PLN03102 326 qvmhayGLTEatgpvLFCEWQDEWNRLPENQQMELKARqGVSILGLADVDVKNKETQES--VPRDGKTMGEIVIKGSSIM 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 448 EeGEVLNsneiglvafklpmpPSFTItfykndEKFKQlftrfpGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLN 527
Cdd:PLN03102 404 K-GYLKN--------------PKATS------EAFKH------GWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSV 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 528 TIDTSILKHPSVLECCSIGILSPDCHTAPIGILVLK---ENPSIDLNKLQNEINNIIT---QDIESLAVLKKIIVINQLP 601
Cdd:PLN03102 457 EVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEkgeTTKEDRVDKLVTRERDLIEycrENLPHFMCPRKVVFLQELP 536
|
570
....*....|....*
gi 66822213 602 KTKVGKIPRQILSNL 616
Cdd:PLN03102 537 KNGNGKILKPKLRDI 551
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
316-608 |
4.00e-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: 4.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 316 LLSGGNTLVMYEGGIiKNKHMEDDLWIAIVKHKVTHTFPSPSVFRYLIKTdPEGTivrskyDLSNLKEIWCGGEVIEESI 395
Cdd:cd05944 66 LASGAHVVLAGPAGY-RNPGLFDNFWKLVERYRITSLSTVPTVYAALLQV-PVNA------DISSLRFAMSGAAPLPVEL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 396 PEYIEQKLKIKCLRVFGQSEigVTSFISVHALNIPYR--ATGVPSIYIRPSILSEEGEV-----LNSNEIGLVAFKLPMp 468
Cdd:cd05944 138 RARFEDATGLPVVEGYGLTE--ATCLVAVNPPDGPKRpgSVGLRLPYARVRIKVLDGVGrllrdCAPDEVGEICVAGPG- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 469 psfTITFYKNDEKFKQLFTRfPGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGil 548
Cdd:cd05944 215 ---VFGGYLYTEGNKNAFVA-DGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVG-- 288
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66822213 549 SPDCHTA--PIGILVLKENPSIDLNKLQNEINNIITqdiESLAVLKKIIVINQLPKTKVGKI 608
Cdd:cd05944 289 QPDAHAGelPVAYVQLKPGAVVEEEELLAWARDHVP---ERAAVPKHIEVLEELPVTAVGKV 347
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
250-618 |
5.09e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 84.17 E-value: 5.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 250 PVESSHPLYILYTSGTTGNTKAVVRSNGphmvgikyytfrkesdipqivfshtNIGWVSF-HGFFYGLLSGGNTLV---- 324
Cdd:PRK06145 145 AVAPTDLVRLMYTSGTTDRPKGVMHSYG-------------------------NLHWKSIdHVIALGLTASERLLVvgpl 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 325 -------------MYEGGIIKnKHMEDD---LWIAIVKHKVTHTFPSPsVFRYLIKTDPEgtivRSKYDLSNLKeiWC-- 386
Cdd:PRK06145 200 yhvgafdlpgiavLWVGGTLR-IHREFDpeaVLAAIERHRLTCAWMAP-VMLSRVLTVPD----RDRFDLDSLA--WCig 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 387 GGEVIEES-IPEYIEQKLKIKCLRVFGQSE-IGVTSFISVHALNIPYRATGVPSIYIRPSILSEEGEVLNSNEIGLVAFK 464
Cdd:PRK06145 272 GGEKTPESrIRDFTRVFTRARYIDAYGLTEtCSGDTLMEAGREIEKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMR 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 465 lpmPPSFTITFYKNDEKFKQLFtrFPGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCS 544
Cdd:PRK06145 352 ---GPKVTKGYWKDPEKTAEAF--YGDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAV 426
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66822213 545 IGILSPDCHTAPIGILVLKENPSIDLNKLQNEINniitQDIESLAVLKKIIVINQLPKTKVGKIPRQILSNLLN 618
Cdd:PRK06145 427 IGVHDDRWGERITAVVVLNPGATLTLEALDRHCR----QRLASFKVPRQLKVRDELPRNPSGKVLKRVLRDELN 496
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
253-610 |
6.60e-17 |
|
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: 83.39 E-value: 6.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 253 SSHPLYILYTSGTTGNTKAVVRSNGPHMVG---IKYYTFRKESDIpqivfsHTNI---GWVSfHGF--FYGLLSGGNTLV 324
Cdd:cd05974 84 ADDPMLLYFTSGTTSKPKLVEHTHRSYPVGhlsTMYWIGLKPGDV------HWNIsspGWAK-HAWscFFAPWNAGATVF 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 325 MYEGGIIKNKHMEDdlwiAIVKHKVTHTFPSPSVFRYLIKTDPEGTIVRskydlsnLKEIWCGGEVIEesiPEYIEQKLK 404
Cdd:cd05974 157 LFNYARFDAKRVLA----ALVRYGVTTLCAPPTVWRMLIQQDLASFDVK-------LREVVGAGEPLN---PEVIEQVRR 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 405 IKCLRV---FGQSEIgvtsfiSVHALNIPYR-----ATGVPSIYIRPSILSEEGEVLNSNEIGLVAFKlpMPPSFTITFY 476
Cdd:cd05974 223 AWGLTIrdgYGQTET------TALVGNSPGQpvkagSMGRPLPGYRVALLDPDGAPATEGEVALDLGD--TRPVGLMKGY 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 477 KNDEKfKQLFTRFPGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGILSPDCHTAP 556
Cdd:cd05974 295 AGDPD-KTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVP 373
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 66822213 557 IGILVLKE--NPSIDLNKlqneinNIITQDIESLAVLKKI--IVINQLPKTKVGKIPR 610
Cdd:cd05974 374 KAFIVLRAgyEPSPETAL------EIFRFSRERLAPYKRIrrLEFAELPKTISGKIRR 425
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
259-613 |
7.43e-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: 83.16 E-value: 7.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 259 ILYTSGTTGNTKAVVRSNGPHmvgikYYTfrkesdipqIVFSHTNIG------WVS----FHgffyglLSGGNTL---VM 325
Cdd:cd05912 82 IMYTSGTTGKPKGVQQTFGNH-----WWS---------AIGSALNLGlteddnWLCalplFH------ISGLSILmrsVI 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 326 YegGI---IKNKHMEDDLWIAIVKHKVTHTFPSPSVFRYLIKTDPEGtivrskYDlSNLKEIWCGGEVIEESIPEYIEQK 402
Cdd:cd05912 142 Y--GMtvyLVDKFDAEQVLHLINSGKVTIISVVPTMLQRLLEILGEG------YP-NNLRCILLGGGPAPKPLLEQCKEK 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 403 lKIKCLRVFGQSEigvtSFISVHALNIPYRAT-----GVPSIYIRPSILSEEGevlNSNEIGLVAFKLPMppsFTITFYK 477
Cdd:cd05912 213 -GIPVYQSYGMTE----TCSQIVTLSPEDALNkigsaGKPLFPVELKIEDDGQ---PPYEVGEILLKGPN---VTKGYLN 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 478 NDEKFKQLFTRfpGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGILSPDCHTAPI 557
Cdd:cd05912 282 RPDATEESFEN--GWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPV 359
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 66822213 558 GILVLKENPSidlnklQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:cd05912 360 AFVVSERPIS------EEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
338-608 |
1.21e-16 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 83.47 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 338 DDLWIAIVKHKVTHTFPSPSVFRYLIKTDPEGtivrskYDLSNLKEIWCGGEVIEESIPEYIEQKLKIKCLRVFGqseig 417
Cdd:PRK07529 298 ANFWKIVERYRINFLSGVPTVYAALLQVPVDG------HDISSLRYALCGAAPLPVEVFRRFEAATGVRIVEGYG----- 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 418 VTSFISVHALNIPYRATGVPSIYIR-P------SILSEEGEVLNS---NEIGLVAFKLPmppsfTItF--YKNDEKFKQL 485
Cdd:PRK07529 367 LTEATCVSSVNPPDGERRIGSVGLRlPyqrvrvVILDDAGRYLRDcavDEVGVLCIAGP-----NV-FsgYLEAAHNKGL 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 486 FTrFPGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGilSPDCHTA--PIGILVLK 563
Cdd:PRK07529 441 WL-EDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVG--RPDAHAGelPVAYVQLK 517
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 66822213 564 ENPSIDLNKLQNEINNIITqdiESLAVLKKIIVINQLPKTKVGKI 608
Cdd:PRK07529 518 PGASATEAELLAFARDHIA---ERAAVPKHVRILDALPKTAVGKI 559
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
86-613 |
1.75e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 82.77 E-value: 1.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 86 FLKKTIklTYYQLYEKVCEFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGSSVKSLIDRIETITP 165
Cdd:PRK06710 45 FLGKDI--TFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 166 KLIITTNYGILNDEIITFTPNLKEAI--ELSTFKP--SNVITLFRNEVLDETKLKKVQTiptipNTLSWYDEIKKLKENN 241
Cdd:PRK06710 123 KVILCLDLVFPRVTNVQSATKIEHVIvtRIADFLPfpKNLLYPFVQKKQSNLVVKVSES-----ETIHLWNSVEKEVNTG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 242 QSpfyeyVPVESSHPLYIL-YTSGTTGNTKAVVRSN----GPHMVGIKYYTFRKESDipQIVfshtnIGWVSFHgFFYGL 316
Cdd:PRK06710 198 VE-----VPCDPENDLALLqYTGGTTGFPKGVMLTHknlvSNTLMGVQWLYNCKEGE--EVV-----LGVLPFF-HVYGM 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 317 LSGGNTLVM--YEGGIIKNKHMEDdLWIAIVKHKVThTFP-SPSVFRYLIKTDpegtiVRSKYDLSNLKEIWCGGEVIEE 393
Cdd:PRK06710 265 TAVMNLSIMqgYKMVLIPKFDMKM-VFEAIKKHKVT-LFPgAPTIYIALLNSP-----LLKEYDISSIRACISGSAPLPV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 394 SIPEYIEQKLKIKCLRVFGQSEIG-VTSFISVHALNIPyRATGVPSIYIRPSILS-EEGEVLNSNEIGLVAFKlpmPPSF 471
Cdd:PRK06710 338 EVQEKFETVTGGKLVEGYGLTESSpVTHSNFLWEKRVP-GSIGVPWPDTEAMIMSlETGEALPPGEIGEIVVK---GPQI 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 472 TITFYKNDEKFKQLFTrfPGYYDSGDLGYKDQRGFYTIVSRSDDQI-KIGFNkIQLNTIDTSILKHPSVLECCSIGILSP 550
Cdd:PRK06710 414 MKGYWNKPEETAAVLQ--DGWLHTGDVGYMDEDGFFYVKDRKKDMIvASGFN-VYPREVEEVLYEHEKVQEVVTIGVPDP 490
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66822213 551 DCHTAPIGILVLKENPSIDlnklQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:PRK06710 491 YRGETVKAFVVLKEGTECS----EEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
68-551 |
2.64e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 82.51 E-value: 2.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 68 HIKNPAKR--DQDALIYecpfLKKTIKLTYYQLYEKVCEFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQC 145
Cdd:PRK12583 23 AFDATVARfpDREALVV----RHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 146 TLFDGSSVKSLIDRIETITPKLII------TTNYGILNDEIItftPNLKEAIElstfkpsnviTLFRNEVLDEtkLKKVQ 219
Cdd:PRK12583 99 NINPAYRASELEYALGQSGVRWVIcadafkTSDYHAMLQELL---PGLAEGQP----------GALACERLPE--LRGVV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 220 TI-PTIPNTLSWYDEIKKLKE--NNQSPFYEYVPVESSHPLYILYTSGTTGNTKAVVRS-----NGPHMVGIKYYTfrKE 291
Cdd:PRK12583 164 SLaPAPPPGFLAWHELQARGEtvSREALAERQASLDRDDPINIQYTSGTTGFPKGATLShhnilNNGYFVAESLGL--TE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 292 SD---IPqivfshtnigwVSFHGFFYGLLSggNTLVMYEGG--IIKNKHMEDDLWI-AIVKHKVTHTFPSPSVFRYLIkT 365
Cdd:PRK12583 242 HDrlcVP-----------VPLYHCFGMVLA--NLGCMTVGAclVYPNEAFDPLATLqAVEEERCTALYGVPTMFIAEL-D 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 366 DPEgtivRSKYDLSNLKE-IWCGGEVIEESIPEYIEQKLKIKCLRVFGQSEIGVTSFISVHALNIPYRATGVPSI--YIR 442
Cdd:PRK12583 308 HPQ----RGNFDLSSLRTgIMAGAPCPIEVMRRVMDEMHMAEVQIAYGMTETSPVSLQTTAADDLERRVETVGRTqpHLE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 443 PSILSEEGEVLNSNEIGLVAFKlpmPPSFTITFYKNDEKFKQLFTRfPGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFN 522
Cdd:PRK12583 384 VKVVDPDGATVPRGEIGELCTR---GYSVMKGYWNNPEATAESIDE-DGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGE 459
|
490 500
....*....|....*....|....*....
gi 66822213 523 KIQLNTIDTSILKHPSVLECCSIGIlsPD 551
Cdd:PRK12583 460 NIYPREIEEFLFTHPAVADVQVFGV--PD 486
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
254-610 |
3.70e-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: 80.38 E-value: 3.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 254 SHPLYILYTSGTTGNTKAVVRSNGphmvgikyyTFRKESDIPQIVFSHTNIGWVSF---HGFFYGLLSGGNTLVMYEGGI 330
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANK---------TFFAVPDILQKEGLNWVVGDVTYlplPATHIGGLWWILTCLIHGGLC 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 331 I--KNKHMEDDLWIAIVKHKVTHTFPSPSVFRYLIkTDPEGTIVRSKydlsNLKEIWCGGEVIEESIPEYIEQKLKIKCL 408
Cdd:cd17635 72 VtgGENTTYKSLFKILTTNAVTTTCLVPTLLSKLV-SELKSANATVP----SLRLIGYGGSRAIAADVRFIEATGLTNTA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 409 RVFGQSEIGVTSFISVHALNIPYRATGVPSIYIRPSILSEEGEVLNSNEIGLVAFKlpmPPSFTITFYKNDEKFKQLFTR 488
Cdd:cd17635 147 QVYGLSETGTALCLPTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIK---SPANMLGYWNNPERTAEVLID 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 489 fpGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGIlsPDCHTAPIGILVLKENPSI 568
Cdd:cd17635 224 --GWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEI--SDEEFGELVGLAVVASAEL 299
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 66822213 569 DLNKLQNEINNIITQdIESLAVLKKIIVINQLPKTKVGKIPR 610
Cdd:cd17635 300 DENAIRALKHTIRRE-LEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
90-624 |
9.57e-16 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 80.44 E-value: 9.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 90 TIKLTYYQLYEKVCEFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATqCTLFDGSSVKSLIDRIETITpklii 169
Cdd:PRK05857 39 TSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAI-AVMADGNLPIAAIERFCQIT----- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 170 ttnygilndeiitftpnlkeaielstfKPSNVITLFRNEVLDETKLKKVQTIPTIPntlswYDEIKKLKENNQSPFYEYV 249
Cdd:PRK05857 113 ---------------------------DPAAALVAPGSKMASSAVPEALHSIPVIA-----VDIAAVTRESEHSLDAASL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 250 PVE----SSHPLYILYTSGTTGNTKAVVRSNgphmvgikyytfRKESDIPQIVfSHTNIGWVSF-------------H-G 311
Cdd:PRK05857 161 AGNadqgSEDPLAMIFTSGTTGEPKAVLLAN------------RTFFAVPDIL-QKEGLNWVTWvvgettysplpatHiG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 312 FFYGLLSGgntlVMYEGGIIKNKHMEDDLWIAIVKHKVTHTFPSPSVFRYLIKTDPEGTIvrskyDLSNLKEIWCGGEVI 391
Cdd:PRK05857 228 GLWWILTC----LMHGGLCVTGGENTTSLLEILTTNAVATTCLVPTLLSKLVSELKSANA-----TVPSLRLVGYGGSRA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 392 EESIPEYIEQKlKIKCLRVFGQSEIGVTSF-----------ISVHALNIPYraTGVpSIYIRPsilsEEG------EVLN 454
Cdd:PRK05857 299 IAADVRFIEAT-GVRTAQVYGLSETGCTALclptddgsivkIEAGAVGRPY--PGV-DVYLAA----TDGigptapGAGP 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 455 SNEIGLVAFKlpmPPSFTITFYKNDEKFKQLFTRfpGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSIL 534
Cdd:PRK05857 371 SASFGTLWIK---SPANMLGYWNNPERTAEVLID--GWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAE 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 535 KHPSVLECCSIGIlsPDCH-TAPIGILVLkenPSIDLN-----KLQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKI 608
Cdd:PRK05857 446 GVSGVREAACYEI--PDEEfGALVGLAVV---ASAELDesaarALKHTIAARFRRESEPMARPSTIVIVTDIPRTQSGKV 520
|
570
....*....|....*.
gi 66822213 609 PRQILSNLLNDPNYQL 624
Cdd:PRK05857 521 MRASLAAAATADKARV 536
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
91-613 |
1.06e-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: 80.25 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 91 IKLTYYQLYEKVCEFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGAtqctlfdgssVKSLIDrietitPKL-II 169
Cdd:cd05923 27 LRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGA----------VPALIN------PRLkAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 170 TTNYGILNDEIIT-FTPNLKEAIELSTFKPSNVITLfrnEVLDETKlkkvqtIPTipntlswydeikklkenNQSPFYEY 248
Cdd:cd05923 91 ELAELIERGEMTAaVIAVDAQVMDAIFQSGVRVLAL---SDLVGLG------EPE-----------------SAGPLIED 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 249 VPVESSHPLYILYTSGTTGNTKAVV---RSNGP------HMVGIKYYtfRKESDIPQIVFSHTnigwVSFHGFFYGLLSG 319
Cdd:cd05923 145 PPREPEQPAFVFYTSGTTGLPKGAVipqRAAESrvlfmsTQAGLRHG--RHNVVLGLMPLYHV----IGFFAVLVAALAL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 320 GNTLVMYEggiiknkhmEDDLWIA---IVKHKVTHTFPSPSVFRYLIktdpeGTIVRSKYDLSNLKEIWCGGEVIEESIP 396
Cdd:cd05923 219 DGTYVVVE---------EFDPADAlklIEQERVTSLFATPTHLDALA-----AAAEFAGLKLSSLRHVTFAGATMPDAVL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 397 EYIEQKLKIKCLRVFGQSEIgvtsFISVHALNIPYRATGVPSIYIR---PSILSEEGEVLNSNEIGLVAFKLPMPPSFTI 473
Cdd:cd05923 285 ERVNQHLPGEKVNIYGTTEA----MNSLYMRDARTGTEMRPGFFSEvriVRIGGSPDEALANGEEGELIVAAAADAAFTG 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 474 TFYKNDEKFKQLftRFpGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGIlsPDCH 553
Cdd:cd05923 361 YLNQPEATAKKL--QD-GWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGV--ADER 435
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66822213 554 TAPIGILVLKENPSidlNKLQNEINNI-ITQDIESLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:cd05923 436 WGQSVTACVVPREG---TLSADELDQFcRASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
256-608 |
1.11e-15 |
|
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: 79.73 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 256 PLYILYTSGTTGNTKAVVRSNGPHMVGIKYYTFRKESDIPQIVFSHTNIGwvSFHGFFYGLlsggnTLVMYEGGIIknkh 335
Cdd:cd05903 95 VALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFLVASPMA--HQTGFVYGF-----TLPLLLGAPV---- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 336 MEDDLW-----IAIVK-HKVTHTFPSPSVFRYLIKTdPEgtivRSKYDLSNLKEIWCGGEVIEESIPEYIEQKLKIKCLR 409
Cdd:cd05903 164 VLQDIWdpdkaLALMReHGVTFMMGATPFLTDLLNA-VE----EAGEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCS 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 410 VFGQSEIG--VTSFISVHALNIpYRATGVPSIYIRPSILSEEGEVLNSNEIGLVAFKlpmPPSFTITFYKNDEKFKQLFT 487
Cdd:cd05903 239 AYGSTECPgaVTSITPAPEDRR-LYTDGRPLPGVEIKVVDDTGATLAPGVEGELLSR---GPSVFLGYLDRPDLTADAAP 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 488 RfpGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGIlsPDCHTAP--IGILVLKEN 565
Cdd:cd05903 315 E--GWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVAL--PDERLGEraCAVVVTKSG 390
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 66822213 566 PSIDLNKLQNEINNiitQDIESLAVLKKIIVINQLPKTKVGKI 608
Cdd:cd05903 391 ALLTFDELVAYLDR---QGVAKQYWPERLVHVDDLPRTPSGKV 430
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
248-610 |
2.11e-15 |
|
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: 78.83 E-value: 2.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 248 YVPVESSHPL-----------------------YILYTSGTTGNTKAVVRSNG------PHMVGikYYTFrkesdIPQIV 298
Cdd:cd05945 68 YVPLDASSPAerireildaakpalliadgddnaYIIFTSGSTGRPKGVQISHDnlvsftNWMLS--DFPL-----GPGDV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 299 FSHTNIgwVSF----HGFFYGLLSGGnTLVmyeggiIKNKHMEDD---LWIAIVKHKVTHTFPSPSVFRYLIKT---DPE 368
Cdd:cd05945 141 FLNQAP--FSFdlsvMDLYPALASGA-TLV------PVPRDATADpkqLFRFLAEHGITVWVSTPSFAAMCLLSptfTPE 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 369 GtivrskydLSNLKEIWCGGEVIEESIPEYIEQKL-KIKCLRVFGQSE--IGVTSF-ISVHALNipyRATGVPSIYIRP- 443
Cdd:cd05945 212 S--------LPSLRHFLFCGEVLPHKTARALQQRFpDARIYNTYGPTEatVAVTYIeVTPEVLD---GYDRLPIGYAKPg 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 444 ---SILSEEGEVLNSNEIG--LVAfklpmPPSFTITFYKNDEKFKQLFTRFPGY--YDSGDLGYKDQRGFYTIVSRSDDQ 516
Cdd:cd05945 281 aklVILDEDGRPVPPGEKGelVIS-----GPSVSKGYLNNPEKTAAAFFPDEGQraYRTGDLVRLEADGLLFYRGRLDFQ 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 517 IKIGFNKIQLNTIDTSILKHPSVLECCSIGILSPDCHTAPIGILVLKENpsiDLNKLQNEINNIITQDIESLAVLKKIIV 596
Cdd:cd05945 356 VKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPG---AEAGLTKAIKAELAERLPPYMIPRRFVY 432
|
410
....*....|....
gi 66822213 597 INQLPKTKVGKIPR 610
Cdd:cd05945 433 LDELPLNANGKIDR 446
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
249-543 |
3.98e-15 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 77.69 E-value: 3.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 249 VPVESSHPLYILYTSGTTGNTKAVV---RSNGPHMVGIKYYTFRKESDipqIVFSHTNIGW-VSFHGFFYGLLSGGNTLV 324
Cdd:TIGR01733 115 APSGPDDLAYVIYTSGSTGRPKGVVvthRSLVNLLAWLARRYGLDPDD---RVLQFASLSFdASVEEIFGALLAGATLVV 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 325 MYEGGIiknKHMEDDLWIAIVKHKVTHTFPSPSVFRYLIKTDPEgtivrskyDLSNLKEIWCGGEVIE-ESIPEYIEQKL 403
Cdd:TIGR01733 192 PPEDEE---RDDAALLAALIAEHPVTVLNLTPSLLALLAAALPP--------ALASLRLVILGGEALTpALVDRWRARGP 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 404 KIKCLRVFGQSE--IGVTSFISVHALNIPYRAT--GVP----SIYI-----RPSILSEEGEVLnsneIG--LVAFKlpmp 468
Cdd:TIGR01733 261 GARLINLYGPTEttVWSTATLVDPDDAPRESPVpiGRPlantRLYVldddlRPVPVGVVGELY----IGgpGVARG---- 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 469 psftitfYKND-EKFKQLFTRFPGY-------YDSGDLGYKDQRGFYTIVSRSDDQIKI-GFnKIQLNTIDTSILKHPSV 539
Cdd:TIGR01733 333 -------YLNRpELTAERFVPDPFAggdgarlYRTGDLVRYLPDGNLEFLGRIDDQVKIrGY-RIELGEIEAALLRHPGV 404
|
....
gi 66822213 540 LECC 543
Cdd:TIGR01733 405 REAV 408
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
256-613 |
1.22e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 76.95 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 256 PLYILYTSGTTGNTKAVVRSN--GPHMVGIKYYTFrkesDIP-QIVF------SHtnigwVSFHGFFYGLLSGGnTLVMY 326
Cdd:PRK06188 170 IAGLAYTGGTTGKPKGVMGTHrsIATMAQIQLAEW----EWPaDPRFlmctplSH-----AGGAFFLPTLLRGG-TVIVL 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 327 EGgiiknkhMEDDLWIAIVK-HKVTHTFPSPSVFRYLIKTDPEgtivrSKYDLSNLKEIWCGGEVIEES-IPEYIEQKLK 404
Cdd:PRK06188 240 AK-------FDPAEVLRAIEeQRITATFLVPTMIYALLDHPDL-----RTRDLSSLETVYYGASPMSPVrLAEAIERFGP 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 405 IkCLRVFGQSEIGvtSFISV-----HALNIPYRAT--GVPSIYIRPSILSEEGEVLNSNEIG-------LVA---FKLPM 467
Cdd:PRK06188 308 I-FAQYYGQTEAP--MVITYlrkrdHDPDDPKRLTscGRPTPGLRVALLDEDGREVAQGEVGeicvrgpLVMdgyWNRPE 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 468 ppsftitfyKNDEKFKQlftrfpGYYDSGDLGYKDQRGFYTIVSRSDDQIkI--GFNkIQLNTIDTSILKHPSVLECCSI 545
Cdd:PRK06188 385 ---------ETAEAFRD------GWLHTGDVAREDEDGFYYIVDRKKDMI-VtgGFN-VFPREVEDVLAEHPAVAQVAVI 447
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66822213 546 GILSPDCHTAPIGILVLKENPSIDLNKLQneinNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:PRK06188 448 GVPDEKWGEAVTAVVVLRPGAAVDAAELQ----AHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKAL 511
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
251-617 |
2.52e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 75.85 E-value: 2.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 251 VESSHPLYILYTSGTTGNTKAVVRSNGphmvgikyytfrkesdipQIVFSHTN-----------------IGWVSfHGff 313
Cdd:PRK07470 160 VDHDDPCWFFFTSGTTGRPKAAVLTHG------------------QMAFVITNhladlmpgtteqdaslvVAPLS-HG-- 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 314 ygllSGGNTLVMYEGG----IIKNKHME-DDLWIAIVKHKVTHTFPSPSVFRYLIKtDPEgtivRSKYDLSNLKEiwcgg 388
Cdd:PRK07470 219 ----AGIHQLCQVARGaatvLLPSERFDpAEVWALVERHRVTNLFTVPTILKMLVE-HPA----VDRYDHSSLRY----- 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 389 eVIEESIPEYIE-QKLKIKCL-----RVFGQSEigVTSFISV-----HAL----NIPYRATGVPSIYIRPSILSEEGEVL 453
Cdd:PRK07470 285 -VIYAGAPMYRAdQKRALAKLgkvlvQYFGLGE--VTGNITVlppalHDAedgpDARIGTCGFERTGMEVQIQDDEGREL 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 454 NSNEIGLVAFKlpMPPSFTiTFYKNDEKFKQLFTRfpGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSI 533
Cdd:PRK07470 362 PPGETGEICVI--GPAVFA-GYYNNPEANAKAFRD--GWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKL 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 534 LKHPSVLECCSIGIlsPDCHTAPIGI--LVLKENPSIDlnklQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQ 611
Cdd:PRK07470 437 LTHPAVSEVAVLGV--PDPVWGEVGVavCVARDGAPVD----EAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKK 510
|
....*.
gi 66822213 612 ILSNLL 617
Cdd:PRK07470 511 MVREEL 516
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
253-617 |
2.63e-14 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 75.66 E-value: 2.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 253 SSHPLYILYTSGTTGNTKAVVRSNGPHMVGIKYYT----FRKESDIPQivF-SHTnigW-VSFHGFFYGLLSGGNTLVMY 326
Cdd:cd05918 105 PSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGralgLTSESRVLQ--FaSYT---FdVSILEIFTTLAAGGCLCIPS 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 327 EGGIIknkhmeDDLWIAIVKHKVTHTFPSPSVFRYLiktDPEgtivrskyDLSNLKEIWCGGEVIEESIpeyIEQ-KLKI 405
Cdd:cd05918 180 EEDRL------NDLAGFINRLRVTWAFLTPSVARLL---DPE--------DVPSLRTLVLGGEALTQSD---VDTwADRV 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 406 KCLRVFGQSE--IGVTSFISV---HALNI--PYRATGV---PSIYIRPSILSEEGEVLNS---------NEIGLVAFKLP 466
Cdd:cd05918 240 RLINAYGPAEctIAATVSPVVpstDPRNIgrPLGATCWvvdPDNHDRLVPIGAVGELLIEgpilargylNDPEKTAAAFI 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 467 MPPSFTITFYKNDekfkqlFTRFpgyYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIG 546
Cdd:cd05918 320 EDPAWLKQEGSGR------GRRL---YRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVE 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 547 ILSPDCHTAP---IGILVLKE-----NPSIDLNKLQNEINNIITQDIESLA--------VLKKIIVINQLPKTKVGKIPR 610
Cdd:cd05918 391 VVKPKDGSSSpqlVAFVVLDGsssgsGDGDSLFLEPSDEFRALVAELRSKLrqrlpsymVPSVFLPLSHLPLTASGKIDR 470
|
....*..
gi 66822213 611 QILSNLL 617
Cdd:cd05918 471 RALRELA 477
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
92-618 |
4.16e-14 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 75.00 E-value: 4.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 92 KLTYYQLYEKVCEFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATqcTLFdgssvksLIDRIetiTPKLIitt 171
Cdd:PRK03640 27 KVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAV--AVL-------LNTRL---SREEL--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 172 NYGILNdeiitftpnlkeaielstfkpSNVITLFRNEVLdETKLKKVQTIPtipntlswYDEIKKLKENNQSPfYEYVPV 251
Cdd:PRK03640 92 LWQLDD---------------------AEVKCLITDDDF-EAKLIPGISVK--------FAELMNGPKEEAEI-QEEFDL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 252 ESShpLYILYTSGTTGNTKAVVRSNGPHmvgikYYTfrkesdipqIVFSHTNIG------WVS----FHgffyglLSGGN 321
Cdd:PRK03640 141 DEV--ATIMYTSGTTGKPKGVIQTYGNH-----WWS---------AVGSALNLGlteddcWLAavpiFH------ISGLS 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 322 TL---VMYegGI---IKNKHMEDDLWIAIVKHKVTHTFPSPSVFRYLIKTDPEGTivrskYDlSNLKEIWCGGEvieeSI 395
Cdd:PRK03640 199 ILmrsVIY--GMrvvLVEKFDAEKINKLLQTGGVTIISVVSTMLQRLLERLGEGT-----YP-SSFRCMLLGGG----PA 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 396 PEYIEQKLKIKCLRVFgQSeIGVTSFIS-VHALNIPYRATGVPS---------IYIRpsilsEEGEVLNSNEIGLVAFKl 465
Cdd:PRK03640 267 PKPLLEQCKEKGIPVY-QS-YGMTETASqIVTLSPEDALTKLGSagkplfpceLKIE-----KDGVVVPPFEEGEIVVK- 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 466 pmPPSFTITFYKNDEKFKQLFTRfpGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSI 545
Cdd:PRK03640 339 --GPNVTKGYLNREDATRETFQD--GWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVV 414
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66822213 546 GILSPDCHTAPIGILVLKENPSidlnklQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQILSNLLN 618
Cdd:PRK03640 415 GVPDDKWGQVPVAFVVKSGEVT------EEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQLVE 481
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
261-627 |
4.24e-14 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 75.17 E-value: 4.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 261 YTSGTTGNTKAVV---RSN--------GPHMVGIKyytfRKESDIPQIVFSHTNiGWvsfhGFFYGLLSGGNTLVM---- 325
Cdd:PRK06018 184 YTSGTTGDPKGVLyshRSNvlhalmanNGDALGTS----AADTMLPVVPLFHAN-SW----GIAFSAPSMGTKLVMpgak 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 326 YEGGIIknkhmeddlWIAIVKHKVTHTFPSPSVFRYLIKTdpegtIVRSKYDLSNLKEIWCGGEVIEESIPEYIEqKLKI 405
Cdd:PRK06018 255 LDGASV---------YELLDTEKVTFTAGVPTVWLMLLQY-----MEKEGLKLPHLKMVVCGGSAMPRSMIKAFE-DMGV 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 406 KCLRVFGQSE---IGVTSFISVHALNIPYRA-------TGVPSIYIRPSILSEEGEVLNSNeiGLVAFKLPMP-PSFTIT 474
Cdd:PRK06018 320 EVRHAWGMTEmspLGTLAALKPPFSKLPGDArldvlqkQGYPPFGVEMKITDDAGKELPWD--GKTFGRLKVRgPAVAAA 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 475 FYKNDEKfkQLFTRfpGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGILSPDCHT 554
Cdd:PRK06018 398 YYRVDGE--ILDDD--GFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDE 473
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66822213 555 APIGILVLKEnpsiDLNKLQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQILSNLLNDpnYQLPDD 627
Cdd:PRK06018 474 RPLLIVQLKP----GETATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALREQFKD--YKLPTA 540
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
259-617 |
1.12e-13 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 74.11 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 259 ILYTSGTTGNTKAVVRSNGPHMVGIKYYTfRKESDipQIVFSHTNIGWVS----FHG-----FFYGLLSGGNTLVmyegg 329
Cdd:PLN02574 203 IMYSSGTTGASKGVVLTHRNLIAMVELFV-RFEAS--QYEYPGSDNVYLAalpmFHIyglslFVVGLLSLGSTIV----- 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 330 iIKNKHMEDDLWIAIVKHKVTHtFPS-PSVFRYLIK-TDPEGTIVrskydLSNLKEIWCGGE-VIEESIPEYIEQKLKIK 406
Cdd:PLN02574 275 -VMRRFDASDMVKVIDRFKVTH-FPVvPPILMALTKkAKGVCGEV-----LKSLKQVSCGAApLSGKFIQDFVQTLPHVD 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 407 CLRVFGQSE---IGVTSFISVHALNipYRATGVPSIYIRPSILS-EEGEVLNSNEIGLVAFKLPMppsfTITFYKNDEKF 482
Cdd:PLN02574 348 FIQGYGMTEstaVGTRGFNTEKLSK--YSSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGPG----VMKGYLNNPKA 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 483 KQLFTRFPGYYDSGDLGYKDQRGFYTIVSRSDDQIKI-GFnKIQLNTIDTSILKHPSVLECCSIGILSPDCHTAPIGILV 561
Cdd:PLN02574 422 TQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYkGF-QIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVV 500
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 66822213 562 LKENPSIDlnklQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQILSNLL 617
Cdd:PLN02574 501 RRQGSTLS----QEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRSL 552
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
250-617 |
2.35e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 72.92 E-value: 2.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 250 PVESSHPLYILYTSGTTGNTKAVVRSngphmvgikyytfrkESDIPQIVFSHTNIGWVSFHGFFY---------GLLSGG 320
Cdd:PRK09088 131 SIPPERVSLILFTSGTSGQPKGVMLS---------------ERNLQQTAHNFGVLGRVDAHSSFLcdapmfhiiGLITSV 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 321 NTLVMYEGGIIKNKHMEDDL---WIAIVKHKVTHTFPSPSVFRyLIKTDPEGTIVRskydLSNLKEIWCGGEV-IEESIP 396
Cdd:PRK09088 196 RPVLAVGGSILVSNGFEPKRtlgRLGDPALGITHYFCVPQMAQ-AFRAQPGFDAAA----LRHLTALFTGGAPhAAEDIL 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 397 EYIEQKLKIKClrVFGQSEIGVTSFISVHALNIPYRA--TGVPSIYIRPSILSEEGEVLNSNEIGLVAFKlpmPPSFTIT 474
Cdd:PRK09088 271 GWLDDGIPMVD--GFGMSEAGTVFGMSVDCDVIRAKAgaAGIPTPTVQTRVVDDQGNDCPAGVPGELLLR---GPNLSPG 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 475 FYKNDEKFKQLFTRfPGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGIlsPDCHT 554
Cdd:PRK09088 346 YWRRPQATARAFTG-DGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGM--ADAQW 422
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66822213 555 APIGILVLKENPSIDLnklqnEINNIITQDIESLA---VLKKIIVINQLPKTKVGKIPRQILSNLL 617
Cdd:PRK09088 423 GEVGYLAIVPADGAPL-----DLERIRSHLSTRLAkykVPKHLRLVDALPRTASGKLQKARLRDAL 483
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
254-551 |
2.54e-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: 2.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 254 SHPLYILYTSGTTGNTKaVVRSNGPHmvgikyytfRKESDIPQIVFShTNIGWVS----------FHG----FFYGLLSG 319
Cdd:cd05929 125 AAGWKMLYSGGTTGRPK-GIKRGLPG---------GPPDNDTLMAAA-LGFGPGAdsvylspaplYHAapfrWSMTALFM 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 320 GNTLVMYE----GGIIKnkhmeddlwiAIVKHKVTHTFPSPSVFRYLIKTdPEgtIVRSKYDLSNL-------------- 381
Cdd:cd05929 194 GGTLVLMEkfdpEEFLR----------LIERYRVTFAQFVPTMFVRLLKL-PE--AVRNAYDLSSLkrvihaaapcppwv 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 382 KEIWC--GGEVIEEsipeyieqklkikclrVFGQSE-IGVTSFISVHALNIPyRATGVPsIYIRPSILSEEGEVLNSNEI 458
Cdd:cd05929 261 KEQWIdwGGPIIWE----------------YYGGTEgQGLTIINGEEWLTHP-GSVGRA-VLGKVHILDEDGNEVPPGEI 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 459 GLVAFKlpMPPSFTITFYKNDEKFKqlftRFPGYYDS-GDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHP 537
Cdd:cd05929 323 GEVYFA--NGPGFEYTNDPEKTAAA----RNEGGWSTlGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHP 396
|
330
....*....|....
gi 66822213 538 SVLECCSIGILSPD 551
Cdd:cd05929 397 KVLDAAVVGVPDEE 410
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
251-613 |
4.10e-13 |
|
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: 71.98 E-value: 4.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 251 VESSHP--LYILYTSGTTGNTKAVVRSNGPHmvgikYYTFRKESDIPQIVfSHTNIGWVSFHGFFYGLLSGGNTLVMYEG 328
Cdd:cd05920 134 LAESIPevALFLLSGGTTGTPKLIPRTHNDY-----AYNVRASAEVCGLD-QDTVYLAVLPAAHNFPLACPGVLGTLLAG 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 329 G--IIKNKHMEDDLWIAIVKHKVTHTFPSPSVFRYLIktdpeGTIVRSKYDLSNLKEIWCGGEVIEESIPEYIEQKLKIK 406
Cdd:cd05920 208 GrvVLAPDPSPDAAFPLIEREGVTVTALVPALVSLWL-----DAAASRRADLSSLRLLQVGGARLSPALARRVPPVLGCT 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 407 CLRVFGQSE--IGVTSF-----ISVHALNIPYRatgvPSIYIRpsILSEEGEVLNSNEIGLVAFKLPmppsFTIT-FYKN 478
Cdd:cd05920 283 LQQVFGMAEglLNYTRLddpdeVIIHTQGRPMS----PDDEIR--VVDEEGNPVPPGEEGELLTRGP----YTIRgYYRA 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 479 DEKFKQLFTRfPGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGILSPDCHTAPIG 558
Cdd:cd05920 353 PEHNARAFTP-DGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCA 431
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 66822213 559 ILVLKeNPSIDLNKLQNEINNiitQDIESLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:cd05920 432 FVVLR-DPPPSAAQLRRFLRE---RGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
249-543 |
4.29e-13 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 72.97 E-value: 4.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 249 VPVESSHPLYILYTSGTTGNTKAVVRSNGP---HMVGI-KYYTFRKESDIPQivfsHTNIGW-VSFHGFFYGLLSGGnTL 323
Cdd:COG1020 612 VPVTPDDLAYVIYTSGSTGRPKGVMVEHRAlvnLLAWMqRRYGLGPGDRVLQ----FASLSFdASVWEIFGALLSGA-TL 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 324 VMYEGGIIKNkhmEDDLWIAIVKHKVTHTFPSPSVFRYLIKTDPEgtivrskyDLSNLKEIWCGGEVIEESIPEYIEQKL 403
Cdd:COG1020 687 VLAPPEARRD---PAALAELLARHRVTVLNLTPSLLRALLDAAPE--------ALPSLRLVLVGGEALPPELVRRWRARL 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 404 kiKCLRVF---GQSEIGVTSfiSVHALNIPYRATGVPSI---------YirpsILSEEGEvlnsneiglvafklPMP--- 468
Cdd:COG1020 756 --PGARLVnlyGPTETTVDS--TYYEVTPPDADGGSVPIgrpiantrvY----VLDAHLQ--------------PVPvgv 813
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 469 ------------------PSFTitfyknDEKFKQLFTRFPG--YYDSGDLGYKDQRGfyTI--VSRSDDQIKI-GFnKIQ 525
Cdd:COG1020 814 pgelyiggaglargylnrPELT------AERFVADPFGFPGarLYRTGDLARWLPDG--NLefLGRADDQVKIrGF-RIE 884
|
330
....*....|....*...
gi 66822213 526 LNTIDTSILKHPSVLECC 543
Cdd:COG1020 885 LGEIEAALLQHPGVREAV 902
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
93-613 |
4.81e-13 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 71.83 E-value: 4.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 93 LTYYQLYEKVCEFSRVLLN-LNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCT---LFDGSSVK-SLIDRIETItpkL 167
Cdd:PRK08751 51 ITYREADQLVEQFAAYLLGeLQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNvnpLYTPRELKhQLIDSGASV---L 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 168 IITTNYGILNDEIITFTPnLKEAI-----ELSTFKPSNVITLFRNEVldetklKKVQTIPTIPNTLSWYDEIKKLKENNQ 242
Cdd:PRK08751 128 VVIDNFGTTVQQVIADTP-VKQVIttglgDMLGFPKAALVNFVVKYV------KKLVPEYRINGAIRFREALALGRKHSM 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 243 SPfyeyVPVESSHPLYILYTSGTTGNTKAVVRSN----------GPHMVGIKYYTFRKESDIPQIVFSHtnIGWVSFHGF 312
Cdd:PRK08751 201 PT----LQIEPDDIAFLQYTGGTTGVAKGAMLTHrnlvanmqqaHQWLAGTGKLEEGCEVVITALPLYH--IFALTANGL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 313 FYGLLSGGNTLvmyeggiIKNKHMEDDLWIAIVKHKVTHTFPSPSVFRYLIKTDPEGTIvrskyDLSNLKEIWCGGEVIE 392
Cdd:PRK08751 275 VFMKIGGCNHL-------ISNPRDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQI-----DFSSLKMTLGGGMAVQ 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 393 ESIPEYIEQKLKIKCLRVFGQSEIGVTSFISVHALNIPYRATGVPSIYIRPSILSEEGEVLNSNEIGLVAFKlpmPPSFT 472
Cdd:PRK08751 343 RSVAERWKQVTGLTLVEAYGLTETSPAACINPLTLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIK---GPQVM 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 473 ITFYKNDEKFKQLFTRfPGYYDSGDLGYKDQRGFYTIVSRSDDQIKI-GFNkIQLNTIDTSILKHPSVLECCSIGIlsPD 551
Cdd:PRK08751 420 KGYWKRPEETAKVMDA-DGWLHTGDIARMDEQGFVYIVDRKKDMILVsGFN-VYPNEIEDVIAMMPGVLEVAAVGV--PD 495
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66822213 552 CHTAPI-GILVLKENPSIDLNKLQNEINNIITQdieslavLKKIIVIN---QLPKTKVGKIPRQIL 613
Cdd:PRK08751 496 EKSGEIvKVVIVKKDPALTAEDVKAHARANLTG-------YKQPRIIEfrkELPKTNVGKILRREL 554
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
259-608 |
5.42e-13 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 71.62 E-value: 5.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 259 ILYTSGTTGNTKAVVRSNGPHMVGIKYYTFRKESDIPQIVFSHTNIGwvsfH--GFFYGL---LSGGNTLVMyeggiikn 333
Cdd:PRK13295 202 LIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMA----HqtGFMYGLmmpVMLGATAVL-------- 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 334 khmeDDLW-----IAIVK-HKVTHTFPSPSVFrylikTDPEGTIVRSKYDLSNLKEIWCGGEVIEESIPEYIEQKLKIKC 407
Cdd:PRK13295 270 ----QDIWdparaAELIRtEGVTFTMASTPFL-----TDLTRAVKESGRPVSSLRTFLCAGAPIPGALVERARAALGAKI 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 408 LRVFGQSEIG-VTSFISVHALNIPYRATGVPSIYIRPSILSEEGEVLNSNEIGLVAFKlpmPPSFTITFYKNDEKFKqlf 486
Cdd:PRK13295 341 VSAWGMTENGaVTLTKLDDPDERASTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVR---GCSNFGGYLKRPQLNG--- 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 487 TRFPGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGIlsPD-------ChtapiGI 559
Cdd:PRK13295 415 TDADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAY--PDerlgeraC-----AF 487
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 66822213 560 LVLKENPSIDLNKLQNEINniiTQDIESLAVLKKIIVINQLPKTKVGKI 608
Cdd:PRK13295 488 VVPRPGQSLDFEEMVEFLK---AQKVAKQYIPERLVVRDALPRTPSGKI 533
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
529-607 |
7.03e-13 |
|
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: 64.10 E-value: 7.03e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66822213 529 IDTSILKHPSVLECCSIGILSPDCHTAPIGILVLKENPSIdlnkLQNEINNIITQDIESLAVLKKIIVINQLPKTKVGK 607
Cdd:pfam13193 2 VESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVEL----LEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
436-613 |
8.45e-13 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 71.20 E-value: 8.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 436 VPSIYIrpSILSEEGEVLNSNEIGLVAFKLP--MPPsftitfYKN--DEKFKQLFTrfPGYYDSGDLGYKDQRGFYTIVS 511
Cdd:PRK07059 386 LPSTEV--SIRDDDGNDLPLGEPGEICIRGPqvMAG------YWNrpDETAKVMTA--DGFFRTGDVGVMDERGYTKIVD 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 512 RSDDQIKI-GFNkIQLNTIDTSILKHPSVLECCSIGIlsPDCHTAP-IGILVLKENPSIDlnklQNEINNIITQDIESLA 589
Cdd:PRK07059 456 RKKDMILVsGFN-VYPNEIEEVVASHPGVLEVAAVGV--PDEHSGEaVKLFVVKKDPALT----EEDVKAFCKERLTNYK 528
|
170 180
....*....|....*....|....
gi 66822213 590 VLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:PRK07059 529 RPKFVEFRTELPKTNVGKILRREL 552
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
2-613 |
8.89e-13 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 71.65 E-value: 8.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 2 YKlsDPFDYLND-NSYSKSNPEAFWDEVakknvfWDKMYDK--------VYSGDEIYP--DWFKGGELNTCYNLLdihIK 70
Cdd:PLN03052 115 YK--DPISSFSEfQRFSVENPEVYWSIV------LDELSLVfsvpprciLDTSDESNPggQWLPGAVLNVAECCL---TP 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 71 NPAKRDQD-ALIY------ECPFLKKTIKltyyQLYEKVCEFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGAT 143
Cdd:PLN03052 184 KPSKTDDSiAIIWrdegsdDLPVNRMTLS----ELRSQVSRVANALDALGFEKGDAIAIDMPMNVHAVIIYLAIILAGCV 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 144 QCTLFDGSSVKSLIDRIETITPKLIITTNYGILNDEIITFTPNLKEAielstfKPSNVITLFRNEVLDETKLKKvqtipt 223
Cdd:PLN03052 260 VVSIADSFAPSEIATRLKISKAKAIFTQDVIVRGGKSIPLYSRVVEA------KAPKAIVLPADGKSVRVKLRE------ 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 224 ipNTLSWYDEIKKlkENNQSPFYEYVPVESSHPLY--ILYTSGTTGNTKAV-------VRSNG---PHMvgikyytfrke 291
Cdd:PLN03052 328 --GDMSWDDFLAR--ANGLRRPDEYKAVEQPVEAFtnILFSSGTTGEPKAIpwtqltpLRAAAdawAHL----------- 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 292 sDIPQ--IVFSHTNIGWVSFHGFFYGLLSGGNTLVMYEGGIIKN---KHMEDdlwiaivkHKVTHTFPSPSVFRYLIKTD 366
Cdd:PLN03052 393 -DIRKgdIVCWPTNLGWMMGPWLVYASLLNGATLALYNGSPLGRgfaKFVQD--------AKVTMLGTVPSIVKTWKNTN 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 367 pegtiVRSKYDLSNLKEIWCGGEVieESIPEYI------EQKLKIKCLrvfGQSEIGvTSFISVHALNiP--YRATGVPS 438
Cdd:PLN03052 464 -----CMAGLDWSSIRCFGSTGEA--SSVDDYLwlmsraGYKPIIEYC---GGTELG-GGFVTGSLLQ-PqaFAAFSTPA 531
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 439 IYIRPSILSEEGEVLNSN-----EIGLvaFKLPMPPSFTITfykNDEKFKQLFTRFPGYYDS-----GDLGYKDQRGFYT 508
Cdd:PLN03052 532 MGCKLFILDDSGNPYPDDapctgELAL--FPLMFGASSTLL---NADHYKVYFKGMPVFNGKilrrhGDIFERTSGGYYR 606
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 509 IVSRSDDQIKIGFNKIQLNTIDTSILK-HPSVLECCSIGIlspdchtAPIG--------ILVLKENPS--IDLNKLQNEI 577
Cdd:PLN03052 607 AHGRADDTMNLGGIKVSSVEIERVCNAaDESVLETAAIGV-------PPPGggpeqlviAAVLKDPPGsnPDLNELKKIF 679
|
650 660 670
....*....|....*....|....*....|....*.
gi 66822213 578 NNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:PLN03052 680 NSAIQKKLNPLFKVSAVVIVPSFPRTASNKVMRRVL 715
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
375-615 |
2.26e-12 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 69.70 E-value: 2.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 375 KYDLSNLKEIWCGGEVIEESIPEYIEQKLKIKCLRVFGQSEigVTSFISVHalniPYRATG--------VPSIYIRpsIL 446
Cdd:PRK08974 321 ELDFSSLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTE--CSPLVSVN----PYDLDYysgsiglpVPSTEIK--LV 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 447 SEEGEVLNSNEIGLVAFKLP--MP-----PSFTitfyknDEKFKQlftrfpGYYDSGDLGYKDQRGFYTIVSRSDDQIKI 519
Cdd:PRK08974 393 DDDGNEVPPGEPGELWVKGPqvMLgywqrPEAT------DEVIKD------GWLATGDIAVMDEEGFLRIVDRKKDMILV 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 520 -GFNkIQLNTIDTSILKHPSVLECCSIGILSPDCHTApIGILVLKENPSIDLNKLQNEINNIITqdieSLAVLKKIIVIN 598
Cdd:PRK08974 461 sGFN-VYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEA-VKIFVVKKDPSLTEEELITHCRRHLT----GYKVPKLVEFRD 534
|
250
....*....|....*..
gi 66822213 599 QLPKTKVGKIPRQILSN 615
Cdd:PRK08974 535 ELPKSNVGKILRRELRD 551
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
94-615 |
2.40e-12 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 69.78 E-value: 2.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 94 TYYQLYEKVCEFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTL---FDGSSVKSLIDRIET---ITPKL 167
Cdd:PRK06087 51 TYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLlpsWREAELVWVLNKCQAkmfFAPTL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 168 IITTNYGILNDEIITFTPNLKEAIELSTFKPSNvitlfrnevldetklkkvqtiptipNTLSwydeIKKLKENNQsPFYE 247
Cdd:PRK06087 131 FKQTRPVDLILPLQNQLPQLQQIVGVDKLAPAT-------------------------SSLS----LSQIIADYE-PLTT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 248 YVPVESSHPLYILYTSGTTGNTKAVVRSNGPHMVGIKYYTFRKESDIPQIVFSHTNIGWVSfhGFFYGLlsggnTLVMYE 327
Cdd:PRK06087 181 AITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHAT--GFLHGV-----TAPFLI 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 328 GG-IIKNKHMEDDLWIAIV-KHKVTHTF-PSPSVFRYLiktdpeGTIVRSKYDLSNLKEIWCGGEVIEESIPEYIEQKlK 404
Cdd:PRK06087 254 GArSVLLDIFTPDACLALLeQQRCTCMLgATPFIYDLL------NLLEKQPADLSALRFFLCGGTTIPKKVARECQQR-G 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 405 IKCLRVFGQSEIGVTSFISVH---ALNIPYRATGVPSIYIRpsILSEEGEVLNSNEIGLVAFKLPM-------PPSFTIT 474
Cdd:PRK06087 327 IKLLSVYGSTESSPHAVVNLDdplSRFMHTDGYAAAGVEIK--VVDEARKTLPPGCEGEEASRGPNvfmgyldEPELTAR 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 475 FYKNDekfkqlftrfpGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGIlsPD--- 551
Cdd:PRK06087 405 ALDEE-----------GWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAM--PDerl 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66822213 552 ----CHTApigilVLKENPSIDlnKLQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQILSN 615
Cdd:PRK06087 472 gersCAYV-----VLKAPHHSL--TLEEVVAFFSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
259-613 |
5.25e-12 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 68.63 E-value: 5.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 259 ILYTSGTTGNTKAVVRSNGPHMVGIKYYTFRkesdIPQIVFSHTNIGWVSFH--GF----FYGLLSggNTLVMyeggiiK 332
Cdd:PRK13382 201 ILLTSGTTGTPKGARRSGPGGIGTLKAILDR----TPWRAEEPTVIVAPMFHawGFsqlvLAASLA--CTIVT------R 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 333 NKHMEDDLWIAIVKHKVTHTFPSPSVFRYLIKTDPEgtiVRSKYDLSNLKEIWCGGEVIEESIPEYIEQKLKIKCLRVFG 412
Cdd:PRK13382 269 RRFDPEATLDLIDRHRATGLAVVPVMFDRIMDLPAE---VRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYN 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 413 QSEIGVTSFISVHALNIPYRATGVPSIYIRPSILSEEGEVLNSNEIGLVafklpmppsftitFYKNDEKFKQlFTR---- 488
Cdd:PRK13382 346 ATEAGMIATATPADLRAAPDTAGRPAEGTEIRILDQDFREVPTGEVGTI-------------FVRNDTQFDG-YTSgstk 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 489 --FPGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGILSPDCHTAPIGILVLKEnp 566
Cdd:PRK13382 412 dfHDGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKP-- 489
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 66822213 567 siDLNKLQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:PRK13382 490 --GASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRREL 534
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
256-610 |
7.21e-12 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 67.30 E-value: 7.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 256 PLYILYTSGTTGNTKAV------VRSNGpHMVGIKYYTFRKESDIPQIVFshtnigwvsFHGFfyGLLSG-------GNT 322
Cdd:cd05917 4 VINIQFTSGTTGSPKGAtlthhnIVNNG-YFIGERLGLTEQDRLCIPVPL---------FHCF--GSVLGvlaclthGAT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 323 LVMYEGGIiknkHMEDDLwIAIVKHKVTHTFPSPSVFRYLIkTDPEgtivRSKYDLSNLKEIWCGGEVIEESIPEYIEQK 402
Cdd:cd05917 72 MVFPSPSF----DPLAVL-EAIEKEKCTALHGVPTMFIAEL-EHPD----FDKFDLSSLRTGIMAGAPCPPELMKRVIEV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 403 LKIKCLRV-FGQSEIGVTSFISVHALNIPYRATGVPSI--YIRPSILSEEG-EVLNSNEIGLVAFKlpmppSFTIT--FY 476
Cdd:cd05917 142 MNMKDVTIaYGMTETSPVSTQTRTDDSIEKRVNTVGRImpHTEAKIVDPEGgIVPPVGVPGELCIR-----GYSVMkgYW 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 477 KNDEKFKQLFTRfPGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGILSPDCHTAP 556
Cdd:cd05917 217 NDPEKTAEAIDG-DGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEV 295
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 66822213 557 IGILVLKENPSIDlnklQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPR 610
Cdd:cd05917 296 CAWIRLKEGAELT----EEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
92-497 |
7.23e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 68.37 E-value: 7.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 92 KLTYYQLYEKVCEFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCT------------LFDGSSVKSLI-- 157
Cdd:PRK07798 28 RLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNvnyryvedelryLLDDSDAVALVye 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 158 ----DRIETITPKLiittnygilndeiitftPNLKEAIElstfkpsnvitlfrneVLDETklkkvqTIPTIPNTLSWYDE 233
Cdd:PRK07798 108 refaPRVAEVLPRL-----------------PKLRTLVV----------------VEDGS------GNDLLPGAVDYEDA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 234 IKklkenNQSPfyEYVPVE-SSHPLYILYTSGTTGNTKAVV-------RSNgphMVGIKYYT---FRKESDI-------- 294
Cdd:PRK07798 149 LA-----AGSP--ERDFGErSPDDLYLLYTGGTTGMPKGVMwrqedifRVL---LGGRDFATgepIEDEEELakraaagp 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 295 PQIVFS-----HTNIGWVSFHGFFygllsGGNTLVMYEggiiKNKHMEDDLWIAIVKHKVThtfpspSVF-------RYL 362
Cdd:PRK07798 219 GMRRFPapplmHGAGQWAAFAALF-----SGQTVVLLP----DVRFDADEVWRTIEREKVN------VITivgdamaRPL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 363 IKT-DPEGTivrskYDLSNLKEIWCGGEVIEESIPE-YIEQKLKIKCLRVFGQSEIGVTSFISVHALNIPyraTGVPSIY 440
Cdd:PRK07798 284 LDAlEARGP-----YDLSSLFAIASGGALFSPSVKEaLLELLPNVVLTDSIGSSETGFGGSGTVAKGAVH---TGGPRFT 355
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66822213 441 IRPS--ILSEEGEVL--NSNEIGLVAFKLPMPpsftITFYKNDEKFKQLFTRFPG--YYDSGD 497
Cdd:PRK07798 356 IGPRtvVLDEDGNPVepGSGEIGWIARRGHIP----LGYYKDPEKTAETFPTIDGvrYAIPGD 414
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
260-551 |
8.38e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 68.01 E-value: 8.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 260 LYTSGTTGNTKAVVRS---NGPH-----MVGIKYYTFRKESDipQIVFS-----HTNIGwvsfhGFFYGLLSGGNTLVMy 326
Cdd:PRK08276 146 LYSSGTTGRPKGIKRPlpgLDPDeapgmMLALLGFGMYGGPD--SVYLSpaplyHTAPL-----RFGMSALALGGTVVV- 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 327 eggiiknkhME----DDLWIAIVKHKVTHTFPSPSVFRYLIKTDPEgtiVRSKYDLSNLKEIWCGG-----EV----IE- 392
Cdd:PRK08276 218 ---------MEkfdaEEALALIERYRVTHSQLVPTMFVRMLKLPEE---VRARYDVSSLRVAIHAAapcpvEVkramIDw 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 393 --ESIPEYieqklkikclrvFGQSE-IGVTSFISVHALNIPY---RA-TGVpsiyIRpsILSEEGEVLNSNEIGLVAFKL 465
Cdd:PRK08276 286 wgPIIHEY------------YASSEgGGVTVITSEDWLAHPGsvgKAvLGE----VR--ILDEDGNELPPGEIGTVYFEM 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 466 PMPPsFTitfYKND-EKFKQLFTRfPGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCS 544
Cdd:PRK08276 348 DGYP-FE---YHNDpEKTAAARNP-HGWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAV 422
|
....*..
gi 66822213 545 IGIlsPD 551
Cdd:PRK08276 423 FGV--PD 427
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
256-613 |
1.05e-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: 67.49 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 256 PLYILYTSGTTGNTKAVV--RSNGPHMvgikYYTFRKESDIPQIVFSHTNIGWVSFHGFF----YGLLSGGnTLVMYEGG 329
Cdd:cd17650 95 LAYVIYTSGTTGKPKGVMveHRNVAHA----AHAWRREYELDSFPVRLLQMASFSFDVFAgdfaRSLLNGG-TLVICPDE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 330 IIKNKHMeddLWIAIVKHKVTHTFPSPSVFRYLIKtdpegTIVRSKYDLSNLKEIWCGGEVIEESIP----EYIEQKLKI 405
Cdd:cd17650 170 VKLDPAA---LYDLILKSRITLMESTPALIRPVMA-----YVYRNGLDLSAMRLLIVGSDGCKAQDFktlaARFGQGMRI 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 406 kcLRVFGQSEIGV-TSFISVHALNIPYRAT---GVPSIYIRPSILSEEgevLNSNEIGlVAFKLPMPPSFTITFYKNDEK 481
Cdd:cd17650 242 --INSYGVTEATIdSTYYEEGRDPLGDSANvpiGRPLPNTAMYVLDER---LQPQPVG-VAGELYIGGAGVARGYLNRPE 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 482 F-KQLFTRFP-----GYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGILSPDCHTA 555
Cdd:cd17650 316 LtAERFVENPfapgeRMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEAR 395
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 66822213 556 PIGILVLKENPSIdlnklqNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:cd17650 396 LCAYVVAAATLNT------AELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
249-543 |
1.43e-11 |
|
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: 67.23 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 249 VPVESSHPLYILYTSGTTGNTK-------AVVR--SNGPHMvgikyytfrkeSDIPQIVFSHTniGWVSFHGF---FYG- 315
Cdd:cd12117 131 VPVSPDDLAYVMYTSGSTGRPKgvavthrGVVRlvKNTNYV-----------TLGPDDRVLQT--SPLAFDAStfeIWGa 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 316 LLSGGnTLVMYEGGIIKNKhmeDDLWIAIVKHKVTHTFPSPSVFRYLIKTDPEGtivrskydLSNLKEIWCGGEVIEesi 395
Cdd:cd12117 198 LLNGA-RLVLAPKGTLLDP---DALGALIAEEGVTVLWLTAALFNQLADEDPEC--------FAGLRELLTGGEVVS--- 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 396 PEYIEQKLK----IKCLRVFGQSEigVTSFISVHALNIPYRATG-VP--------SIYI-----RPSILSEEGEVLNSNE 457
Cdd:cd12117 263 PPHVRRVLAacpgLRLVNGYGPTE--NTTFTTSHVVTELDEVAGsIPigrpiantRVYVldedgRPVPPGVPGELYVGGD 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 458 iGLVAfklpmppsftitFYKND-----EKFKQLfTRFPG--YYDSGDLGYKDQRGFYTIVSRSDDQIKI-GFnKIQLNTI 529
Cdd:cd12117 341 -GLAL------------GYLNRpaltaERFVAD-PFGPGerLYRTGDLARWLPDGRLEFLGRIDDQVKIrGF-RIELGEI 405
|
330
....*....|....
gi 66822213 530 DTSILKHPSVLECC 543
Cdd:cd12117 406 EAALRAHPGVREAV 419
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
448-613 |
1.62e-11 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 66.82 E-value: 1.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 448 EEGEVLNSNEIGLVAFKLP--------MPpsftitfykndEKFKQLFTRfPGYYDSGDLGYKDQRGFYTIVSRSDDQIkI 519
Cdd:PRK07514 338 ETGAELPPGEIGMIEVKGPnvfkgywrMP-----------EKTAEEFRA-DGFFITGDLGKIDERGYVHIVGRGKDLI-I 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 520 --GFNkIQLNTIDTSILKHPSVLECCSIGILSPDCHTAPIGILVLKENPSIDLNKLQNEINniitqdiESLA---VLKKI 594
Cdd:PRK07514 405 sgGYN-VYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALDEAAILAALK-------GRLArfkQPKRV 476
|
170
....*....|....*....
gi 66822213 595 IVINQLPKTKVGKIPRQIL 613
Cdd:PRK07514 477 FFVDELPRNTMGKVQKNLL 495
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
242-613 |
2.40e-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: 66.55 E-value: 2.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 242 QSPFYEYVPVESSH-PLYILYTSGTTGNTKAVVRSngpH-------MVGIKYYTFRKESdipqiVFSHT------NiGWv 307
Cdd:cd12118 120 GDPDFEWIPPADEWdPIALNYTSGTTGRPKGVVYH---HrgaylnaLANILEWEMKQHP-----VYLWTlpmfhcN-GW- 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 308 sfhGFFYGLLSGGNTLVMYeggiiknKHMEDDL-WIAIVKHKVTHTFPSPSVFRYLIKTDPEgtivrSKYDLSNLKEIWC 386
Cdd:cd12118 190 ---CFPWTVAAVGGTNVCL-------RKVDAKAiYDLIEKHKVTHFCGAPTVLNMLANAPPS-----DARPLPHRVHVMT 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 387 GGEVIEESIPEYIEQkLKIKCLRVFGQSEigVTSFISV-------HALNIPYRA-----TGVPSIyirpsiLSEEGEVLN 454
Cdd:cd12118 255 AGAPPPAAVLAKMEE-LGFDVTHVYGLTE--TYGPATVcawkpewDELPTEERArlkarQGVRYV------GLEEVDVLD 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 455 SN----------EIGLVAFK--LPMppsftITFYKNDEKFKQLFTRfpGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFN 522
Cdd:cd12118 326 PEtmkpvprdgkTIGEIVFRgnIVM-----KGYLKNPEATAEAFRG--GWFHSGDLAVIHPDGYIEIKDRSKDIIISGGE 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 523 KIQLNTIDTSILKHPSVLECCSIGilSPDCH--TAPIGILVLKEnpsiDLNKLQNEinnIITQDIESLAVLK--KIIVIN 598
Cdd:cd12118 399 NISSVEVEGVLYKHPAVLEAAVVA--RPDEKwgEVPCAFVELKE----GAKVTEEE---IIAFCREHLAGFMvpKTVVFG 469
|
410
....*....|....*
gi 66822213 599 QLPKTKVGKIPRQIL 613
Cdd:cd12118 470 ELPKTSTGKIQKFVL 484
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
249-613 |
3.31e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 67.11 E-value: 3.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 249 VPVESSHPLYILYTSGTTGNTKAVVRSNGP--HMVGIKYYTFRKESDipQIVFSHTNIGWVSFHGFFYGLLSGGNTLVMY 326
Cdd:PRK12467 651 VALDPDNLAYVIYTSGSTGQPKGVAISHGAlaNYVCVIAERLQLAAD--DSMLMVSTFAFDLGVTELFGALASGATLHLL 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 327 EGGIIKNKhmeDDLWIAIVKHKVTHTFPSPSVFRYLIKtDPEGTIVRSkydlsnLKEIWCGGEVIEESIPEYIEQK-LKI 405
Cdd:PRK12467 729 PPDCARDA---EAFAALMADQGVTVLKIVPSHLQALLQ-ASRVALPRP------QRALVCGGEALQVDLLARVRALgPGA 798
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 406 KCLRVFGQSE--IGVTSF-ISVHALNIPYRATGVP----SIYI-----RPSILSEEGEVLNSNEiGLvAFKLPMPPSFTI 473
Cdd:PRK12467 799 RLINHYGPTEttVGVSTYeLSDEERDFGNVPIGQPlanlGLYIldhylNPVPVGVVGELYIGGA-GL-ARGYHRRPALTA 876
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 474 TFYKNDeKFKQLFTRFpgyYDSGDLGYKDQRGFYTIVSRSDDQIKI-GFnKIQLNTIDTSILKHPSVLECCSIGIlSPDC 552
Cdd:PRK12467 877 ERFVPD-PFGADGGRL---YRTGDLARYRADGVIEYLGRMDHQVKIrGF-RIELGEIEARLLAQPGVREAVVLAQ-PGDA 950
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66822213 553 HTAPIGILVLKENPSIDLNKLQN-EINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:PRK12467 951 GLQLVAYLVPAAVADGAEHQATRdELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKAL 1012
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
261-608 |
3.97e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 65.75 E-value: 3.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 261 YTSGTTGNTKAVVRSNGPHMvgikyytfrkesdipqivfsHTNIG---WVS-------------FH--GFFYGLLS---G 319
Cdd:PRK08314 197 YTSGTTGVPKGCMHTHRTVM--------------------ANAVGsvlWSNstpesvvlavlplFHvtGMVHSMNApiyA 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 320 GNTLVMYEggiIKNKHMEDDLwiaIVKHKVTH-TFPSPSVFRYLIKTDPEgtivrsKYDLSNLKEIWCGGEvieeSIPEY 398
Cdd:PRK08314 257 GATVVLMP---RWDREAAARL---IERYRVTHwTNIPTMVVDFLASPGLA------ERDLSSLRYIGGGGA----AMPEA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 399 IEQKLKikclRVFGQSEI---GVTSFISVHALNIPYRAT----GVPSIYIRPSILS-EEGEVLNSNEIGLVAFKlpmPPS 470
Cdd:PRK08314 321 VAERLK----ELTGLDYVegyGLTETMAQTHSNPPDRPKlqclGIPTFGVDARVIDpETLEELPPGEVGEIVVH---GPQ 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 471 FTITFYKNDEKFKQLFTRFPG--YYDSGDLGYKDQRGFYTIVSRSDDQIKI-GFnKIQLNTIDTSILKHPSVLECCSIGi 547
Cdd:PRK08314 394 VFKGYWNRPEATAEAFIEIDGkrFFRTGDLGRMDEEGYFFITDRLKRMINAsGF-KVWPAEVENLLYKHPAIQEACVIA- 471
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66822213 548 lSPDCHTAPI--GILVLKENpsidlNKLQNEINNIITQDIESLAVLK---KIIVINQLPKTKVGKI 608
Cdd:PRK08314 472 -TPDPRRGETvkAVVVLRPE-----ARGKTTEEEIIAWAREHMAAYKyprIVEFVDSLPKSGSGKI 531
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
76-614 |
5.65e-11 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 65.47 E-value: 5.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 76 DQDALIYEcPFLKKTIKLTYYQLYEKVCEFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQC---TLFDGSS 152
Cdd:PRK08008 22 HKTALIFE-SSGGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVpinARLLREE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 153 VKSLIDRIETitpKLIITTNygilndeiiTFTPnLKEAIELSTFKPSNVITLFRnevldetklkkvQTIPTIPNTLSWYD 232
Cdd:PRK08008 101 SAWILQNSQA---SLLVTSA---------QFYP-MYRQIQQEDATPLRHICLTR------------VALPADDGVSSFTQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 233 eikkLKENNQSPFYEYVPVESSHPLYILYTSGTTGNTKAVV------RSNGphmvgikYYT-----FRkESDIPQIVFSh 301
Cdd:PRK08008 156 ----LKAQQPATLCYAPPLSTDDTAEILFTSGTTSRPKGVVithynlRFAG-------YYSawqcaLR-DDDVYLTVMP- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 302 tnigwvSFHGFF-----YGLLSGGNTLVMYEggiiknKHMEDDLWIAIVKHKVTHTFPSPSVFRYLIKTDPegtivrSKY 376
Cdd:PRK08008 223 ------AFHIDCqctaaMAAFSAGATFVLLE------KYSARAFWGQVCKYRATITECIPMMIRTLMVQPP------SAN 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 377 DLSNlkeiwCGGEV-----IEESIPEYIEQKLKIKCLRVFGQSE-----IGVTSFISVHalnipYRATGVPSIYIRPSIL 446
Cdd:PRK08008 285 DRQH-----CLREVmfylnLSDQEKDAFEERFGVRLLTSYGMTEtivgiIGDRPGDKRR-----WPSIGRPGFCYEAEIR 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 447 SEEGEVLNSNEIGLVAFKlpMPPSFTI--TFYKNDEKFKQLFTRfPGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKI 524
Cdd:PRK08008 355 DDHNRPLPAGEIGEICIK--GVPGKTIfkEYYLDPKATAKVLEA-DGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENV 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 525 QLNTIDTSILKHPSVLECCSIGILSPDCHTAPIGILVLKENPSIDlnklQNEINNIITQDIESLAVLKKIIVINQLPKTK 604
Cdd:PRK08008 432 SCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLS----EEEFFAFCEQNMAKFKVPSYLEIRKDLPRNC 507
|
570
....*....|
gi 66822213 605 VGKIPRQILS 614
Cdd:PRK08008 508 SGKIIKKNLK 517
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
259-617 |
9.76e-11 |
|
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: 63.50 E-value: 9.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 259 ILYTSGTTGNTKAVVRSNGPHMVGIKYytfrkesdipqivfSHTNIG------WV----SFH--GF---FYGLLSGGNtL 323
Cdd:cd17630 5 VILTSGSTGTPKAVVHTAANLLASAAG--------------LHSRLGfgggdsWLlslpLYHvgGLailVRSLLAGAE-L 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 324 VMYEGgiiknkhmEDDLWIAIVKHKVTHTFPSPSVFRYLIkTDPEGTivrskYDLSNLKEIWCGGEVIEESIPEYIEQkL 403
Cdd:cd17630 70 VLLER--------NQALAEDLAPPGVTHVSLVPTQLQRLL-DSGQGP-----AALKSLRAVLLGGAPIPPELLERAAD-R 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 404 KIKCLRVFGQSEIGvtSFISVHALNIPYRAT-GVPSIYIRPSILSEEgevlnsnEIGLVAFKLPMPpsftitfYKNDEKF 482
Cdd:cd17630 135 GIPLYTTYGMTETA--SQVATKRPDGFGRGGvGVLLPGRELRIVEDG-------EIWVGGASLAMG-------YLRGQLV 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 483 KQLFTrfPGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGILSPDCHTAPIGILVL 562
Cdd:cd17630 199 PEFNE--DGWFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVG 276
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 66822213 563 KENPSIDlnklqnEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQILSNLL 617
Cdd:cd17630 277 RGPADPA------ELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
344-619 |
1.72e-10 |
|
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: 63.63 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 344 IVKHKVTHTFPSPSVFRYLIKTDPegtivRSKYDLSNLKEIWCGGEVIEESIPEYIEQKLKIKCLRVFGQSEiGVTSF-- 421
Cdd:COG1021 270 IERERVTVTALVPPLALLWLDAAE-----RSRYDLSSLRVLQVGGAKLSPELARRVRPALGCTLQQVFGMAE-GLVNYtr 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 422 ------ISVHalnipyraT-GVP-SIY--IRpsILSEEGEVLNSNEIGLVAFKLPmppsFTIT-FYKNDEKFKQLFTRfP 490
Cdd:COG1021 344 lddpeeVILT--------TqGRPiSPDdeVR--IVDEDGNPVPPGEVGELLTRGP----YTIRgYYRAPEHNARAFTP-D 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 491 GYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGIlsPD-------ChtapiGILVLK 563
Cdd:COG1021 409 GFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAM--PDeylgersC-----AFVVPR 481
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66822213 564 eNPSIDLNKLQN---EINniitqdiesLAVLK---KIIVINQLPKTKVGKIPRQILSNLLND 619
Cdd:COG1021 482 -GEPLTLAELRRflrERG---------LAAFKlpdRLEFVDALPLTAVGKIDKKALRAALAA 533
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
68-615 |
3.18e-10 |
|
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: 62.71 E-value: 3.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 68 HIKNPAKRDQDALIYEcpflKKTIKLTYYQLYEKVCEFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTL 147
Cdd:cd17653 2 AFERIAAAHPDAVAVE----SLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 148 fDGssvKSLIDRIETItpkliittnygilndeiitftpnlkeaieLSTFKPSNVITlfrnevldetklkkvqtiPTIPNT 227
Cdd:cd17653 78 -DA---KLPSARIQAI-----------------------------LRTSGATLLLT------------------TDSPDD 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 228 LSwydeikklkennqspfyeyvpvesshplYILYTSGTTGNTKAV---------VRSNGPHMVGIkyytfRKESDIPQiV 298
Cdd:cd17653 107 LA----------------------------YIIFTSGSTGIPKGVmvphrgvlnYVSQPPARLDV-----GPGSRVAQ-V 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 299 FShtnIGWVSFHGFFYGLLSGGNTLVMyeggiiknKHMEDDLwiAIVKHKVTHTFPSPSVfryLIKTDPEgtivrskyDL 378
Cdd:cd17653 153 LS---IAFDACIGEIFSTLCNGGTLVL--------ADPSDPF--AHVARTVDALMSTPSI---LSTLSPQ--------DF 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 379 SNLKEIWCGGEVIEESIpeyIEQKLKIKCL-RVFGQSEigvTSFISVHALNIPYRAT--GVP----SIYI-----RPSIL 446
Cdd:cd17653 209 PNLKTIFLGGEAVPPSL---LDRWSPGRRLyNAYGPTE---CTISSTMTELLPGQPVtiGKPipnsTCYIldadlQPVPE 282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 447 SEEGEVLNSNeIGLvafklpmppsfTITFYKNDE----KFKqLFTRFPG--YYDSGDLGYKDQRGFYTIVSRSDDQIKI- 519
Cdd:cd17653 283 GVVGEICISG-VQV-----------ARGYLGNPAltasKFV-PDPFWPGsrMYRTGDYGRWTEDGGLEFLGREDNQVKVr 349
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 520 GFnKIQLNTIDTSILKHPSVLECCSIgILSPDCHTApigiLVLKEnpSIDLNKLQNEinniITQDIESLAVLKKIIVINQ 599
Cdd:cd17653 350 GF-RINLEEIEEVVLQSQPEVTQAAA-IVVNGRLVA----FVTPE--TVDVDGLRSE----LAKHLPSYAVPDRIIALDS 417
|
570
....*....|....*.
gi 66822213 600 LPKTKVGKIPRQILSN 615
Cdd:cd17653 418 FPLTANGKVDRKALRE 433
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
222-541 |
6.74e-10 |
|
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: 61.98 E-value: 6.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 222 PTIPNTLSWYDEIKKLKENNQSPFyeyVPVESSHPLYILYTSGTTGNTKAVVRSNGPHMVGIKYYTFRKESDIPQIVFSH 301
Cdd:cd17651 107 AVELVAVTLLDQPGAAAGADAEPD---PALDADDLAYVIYTSGSTGRPKGVVMPHRSLANLVAWQARASSLGPGARTLQF 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 302 TNIGW-VSFHGFFYGLLSGGnTLVmyeggiIKNKHMEDD---LWIAIVKHKVTHTFPSPSVFRYLIK-TDPEGTIvrsky 376
Cdd:cd17651 184 AGLGFdVSVQEIFSTLCAGA-TLV------LPPEEVRTDppaLAAWLDEQRISRVFLPTVALRALAEhGRPLGVR----- 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 377 dLSNLKEIWCGGE--VIEESIPEYIEqklKIKCLRVF---GQSEigvTSFISVHAL-NIPYRATGVPSI---------YI 441
Cdd:cd17651 252 -LAALRYLLTGGEqlVLTEDLREFCA---GLPGLRLHnhyGPTE---THVVTALSLpGDPAAWPAPPPIgrpidntrvYV 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 442 -----RPSILSEEGEvLNSNEIGLVAFKLPMPPsftitfyKNDEKFKQL-FTRFPGYYDSGDLGYKDQRGFYTIVSRSDD 515
Cdd:cd17651 325 ldaalRPVPPGVPGE-LYIGGAGLARGYLNRPE-------LTAERFVPDpFVPGARMYRTGDLARWLPDGELEFLGRADD 396
|
330 340
....*....|....*....|....*..
gi 66822213 516 QIKI-GFnKIQLNTIDTSILKHPSVLE 541
Cdd:cd17651 397 QVKIrGF-RIELGEIEAALARHPGVRE 422
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
344-610 |
8.22e-10 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 61.53 E-value: 8.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 344 IVKHKVTHTFpSPSVFRYLIKTDPEgTIVRSKYDLSNLKEIWCGGE-VIEESIPEYIEQ----KLKIKCLR-VFGQSEI- 416
Cdd:cd05906 256 IDRYRVTITW-APNFAFALLNDLLE-EIEDGTWDLSSLRYLVNAGEaVVAKTIRRLLRLlepyGLPPDAIRpAFGMTETc 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 417 -GVT--------------SFISVHAlniPYratgvPSIYIRpsILSEEGEVLNSNEIGLVAFKlpmPPSFTITFYKNDEK 481
Cdd:cd05906 334 sGVIysrsfptydhsqalEFVSLGR---PI-----PGVSMR--IVDDEGQLLPEGEVGRLQVR---GPVVTKGYYNNPEA 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 482 FKQLFTRfPGYYDSGDLGYKDQrGFYTIVSRSDDQIKIGFNKIQLNTIDTSILK----HPSVLECCSIgilspdcHTAPI 557
Cdd:cd05906 401 NAEAFTE-DGWFRTGDLGFLDN-GNLTITGRTKDTIIVNGVNYYSHEIEAAVEEvpgvEPSFTAAFAV-------RDPGA 471
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 66822213 558 GI--LVLKENPSIDLNKLQNEINNIITQDIESLAVLKKIIVI----NQLPKTKVGKIPR 610
Cdd:cd05906 472 ETeeLAIFFVPEYDLQDALSETLRAIRSVVSREVGVSPAYLIplpkEEIPKTSLGKIQR 530
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
491-613 |
8.81e-10 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 61.76 E-value: 8.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 491 GYYDSGDLGYKDQRGFYTIVSRSDDQIKI-GFNkIQLNTIDTSILKHPSVLECCSIGIlsPDCHTA-PIGILVLKENPSI 568
Cdd:PRK12492 441 GWFKTGDIAVIDPDGFVRIVDRKKDLIIVsGFN-VYPNEIEDVVMAHPKVANCAAIGV--PDERSGeAVKLFVVARDPGL 517
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 66822213 569 DLnklqNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:PRK12492 518 SV----EELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
259-613 |
9.86e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 61.18 E-value: 9.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 259 ILYTSGTTGNTKAV--------VRSNGPHMVGIKYYTFR-KESDI---PQIVFSHTNIGWVSF-HGFfygllsgGNTLVM 325
Cdd:PRK13390 153 MLYSSGTTGFPKGIqpdlpgrdVDAPGDPIVAIARAFYDiSESDIyysSAPIYHAAPLRWCSMvHAL-------GGTVVL 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 326 yeggiIKNKHMEDDLWiAIVKHKVTHTFPSPSVFRYLIKTDPEgtiVRSKYDLSNLKEiwcggeVIEESIPEYIEQK--- 402
Cdd:PRK13390 226 -----AKRFDAQATLG-HVERYRITVTQMVPTMFVRLLKLDAD---VRTRYDVSSLRA------VIHAAAPCPVDVKham 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 403 ---LKIKCLRVFGQSEIGVTSFISVHALnIPYRATGVPSIYIRPSILSEEGEVLNSNEIGLVAFKLPMPPsftITFYKND 479
Cdd:PRK13390 291 idwLGPIVYEYYSSTEAHGMTFIDSPDW-LAHPGSVGRSVLGDLHICDDDGNELPAGRIGTVYFERDRLP---FRYLNDP 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 480 EKFKQL-FTRFPGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGILSPDCHTAPIG 558
Cdd:PRK13390 367 EKTAAAqHPAHPFWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKA 446
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 66822213 559 ILVLKE--NPSidlNKLQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:PRK13390 447 VIQLVEgiRGS---DELARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLL 500
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
259-614 |
1.14e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 61.17 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 259 ILYTSGTTGNTKAVVRSngPHM---VGIkYYTFRKESDIPqiVFSHTNIGWVSFHGFFYGLLsggnTLVMYEGG-IIKNK 334
Cdd:PRK13383 179 VLLTSGTTGKPKGVPRA--PQLrsaVGV-WVTILDRTRLR--TGSRISVAMPMFHGLGLGML----MLTIALGGtVLTHR 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 335 HMEDDLWIAIVK-HKVTHTFPSPSVFRYLIKTDPEgtiVRSKYDLSNLKEIWCGGEVIEESIPEYIEQKLKIKCLRVFGQ 413
Cdd:PRK13383 250 HFDAEAALAQASlHRADAFTAVPVVLARILELPPR---VRARNPLPQLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGS 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 414 SEIGVTsfisvhALNIPYRATGVPSIYIRPsILSEEGEVLNSNeiglvafKLPMPPSFTITFYKNDEKFKQLFTR----- 488
Cdd:PRK13383 327 TEVGIG------ALATPADLRDAPETVGKP-VAGCPVRILDRN-------NRPVGPRVTGRIFVGGELAGTRYTDgggka 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 489 -FPGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGILSPDCHTAPIGILVLKENPS 567
Cdd:PRK13383 393 vVDGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSG 472
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 66822213 568 IDLNKLQNEINNIITQdiesLAVLKKIIVINQLPKTKVGKIPRQILS 614
Cdd:PRK13383 473 VDAAQLRDYLKDRVSR----FEQPRDINIVSSIPRNPTGKVLRKELP 515
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
344-619 |
1.27e-09 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 61.16 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 344 IVKHKVTHTFPSPSVFRYLIKTDPEGTivrSKYDLSNLKEIWCGGEVIEESIPEYIEQKLKIKCLRVFGQSEiGVTSFIs 423
Cdd:PRK10946 268 IEKHQVNVTALVPPAVSLWLQAIAEGG---SRAQLASLKLLQVGGARLSETLARRIPAELGCQLQQVFGMAE-GLVNYT- 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 424 vhALNIP----YRATGVPsiyIRPS----ILSEEGEVLNSNEIGLVAFKLPmppsFTIT-FYKNDEKFKQLFTRfPGYYD 494
Cdd:PRK10946 343 --RLDDSderiFTTQGRP---MSPDdevwVADADGNPLPQGEVGRLMTRGP----YTFRgYYKSPQHNASAFDA-NGFYC 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 495 SGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGIlsPDCHtapIG-----ILVLKEnP--S 567
Cdd:PRK10946 413 SGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSM--EDEL---MGekscaFLVVKE-PlkA 486
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 66822213 568 IDLNKLQNEinniitQDIESLAVLKKIIVINQLPKTKVGKIPRQILSNLLND 619
Cdd:PRK10946 487 VQLRRFLRE------QGIAEFKLPDRVECVDSLPLTAVGKVDKKQLRQWLAS 532
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
257-574 |
1.27e-09 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 60.47 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 257 LYILYTSGTTGNTKAVV-RSNGPHMVGIKYYTFRKESDIPQIVFSH---TNIGWVSF------HG----FFYGLLSGGNT 322
Cdd:cd05924 6 LYILYTGGTTGMPKGVMwRQEDIFRMLMGGADFGTGEFTPSEDAHKaaaAAAGTVMFpapplmHGtgswTAFGGLLGGQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 323 LVmyeggIIKNKHMEDDLWIAIVKHKVTHTFPSPSVF-RYLIKT-DPEGTivrskYDLSNLKEIWCGGEVIEESIPE-YI 399
Cdd:cd05924 86 VV-----LPDDRFDPEEVWRTIEKHKVTSMTIVGDAMaRPLIDAlRDAGP-----YDLSSLFAISSGGALLSPEVKQgLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 400 EQKLKIKCLRVFGQSEIGVTSFiSVHALNIPYRAtgvPSIYIRPS--ILSEEGEVL--NSNEIGLVAFKLPMPpsftITF 475
Cdd:cd05924 156 ELVPNITLVDAFGSSETGFTGS-GHSAGSGPETG---PFTRANPDtvVLDDDGRVVppGSGGVGWIARRGHIP----LGY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 476 YKNDEKFKQLFTRFPG--YYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGILSPDCH 553
Cdd:cd05924 228 YGDEAKTAETFPEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWG 307
|
330 340
....*....|....*....|.
gi 66822213 554 TAPIGILVLKENPSIDLNKLQ 574
Cdd:cd05924 308 QEVVAVVQLREGAGVDLEELR 328
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
255-541 |
1.41e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 61.51 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 255 HPLYILYTSGTTGNTKAVVRSNGPHMVGIKYYTFRKESDIPQIVFSHTNIGW-VSFHGFFYGLLSGGNTLVMYEGgiikn 333
Cdd:PRK12316 656 NLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFdVSVWEFFWPLMSGARLVVAAPG----- 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 334 KHME-DDLWIAIVKHKVTHTFPSPSVFRYLIktdPEGTIVrskyDLSNLKEIWCGGEVIEESIPEYIEQKLKIKCL-RVF 411
Cdd:PRK12316 731 DHRDpAKLVELINREGVDTLHFVPSMLQAFL---QDEDVA----SCTSLRRIVCSGEALPADAQEQVFAKLPQAGLyNLY 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 412 GQSE--IGVTSFISVHAL--NIPyraTGVPSIYIRPSILSEEGEvlnsneiglvafklPMPPSFTITFYKNDEKFKQLFT 487
Cdd:PRK12316 804 GPTEaaIDVTHWTCVEEGgdSVP---IGRPIANLACYILDANLE--------------PVPVGVLGELYLAGRGLARGYH 866
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 488 RFPGY----------------YDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLE 541
Cdd:PRK12316 867 GRPGLtaerfvpspfvagermYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVRE 936
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
257-613 |
1.63e-09 |
|
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: 60.53 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 257 LYILYTSGTTGNTKAVV---RSNGPHMVGIKYYTFRKESDipqIVFSHTNIGW-VSFHGFFYGLLSGGnTLVMYEGGIIK 332
Cdd:cd17644 109 AYVIYTSGSTGKPKGVMiehQSLVNLSHGLIKEYGITSSD---RVLQFASIAFdVAAEEIYVTLLSGA-TLVLRPEEMRS 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 333 NKHmedDLWIAIVKHKVTHTFPSPSVFRYLIKtdpegTIVRSKYDL-SNLKEIWCGGEVIEESIPEYIEQKL--KIKCLR 409
Cdd:cd17644 185 SLE---DFVQYIQQWQLTVLSLPPAYWHLLVL-----ELLLSTIDLpSSLRLVIVGGEAVQPELVRQWQKNVgnFIQLIN 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 410 VFGQSEIGVTSfiSVHALNIPYRATgVPSIYIRPSILSEEGEVLNSNeiglvafKLPMPPSFTITF----------YKN- 478
Cdd:cd17644 257 VYGPTEATIAA--TVCRLTQLTERN-ITSVPIGRPIANTQVYILDEN-------LQPVPVGVPGELhiggvglargYLNr 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 479 ----DEKFKQ-LFTRFPG--YYDSGDLGYKDQRGFYTIVSRSDDQIKI-GFnKIQLNTIDTSILKHPSVLECCSIGILSP 550
Cdd:cd17644 327 peltAEKFIShPFNSSESerLYKTGDLARYLPDGNIEYLGRIDNQVKIrGF-RIELGEIEAVLSQHNDVKTAVVIVREDQ 405
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66822213 551 DCHTAPIGILVLKENPSIDLNKLQneinNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:cd17644 406 PGNKRLVAYIVPHYEESPSTVELR----QFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
249-613 |
2.81e-09 |
|
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: 59.65 E-value: 2.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 249 VPVESSHPLYILYTSGTTGNTKAVVR-----SNGPHMVGIKYYTFRKeSDIPQ---IVF--SHTNIgwvsfhgfFYGLLS 318
Cdd:cd17655 132 PVSKSDDLAYVIYTSGSTGKPKGVMIehrgvVNLVEWANKVIYQGEH-LRVALfasISFdaSVTEI--------FASLLS 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 319 gGNTLVMYEGgiiKNKHMEDDLWIAIVKHKVTHTFPSPSVFRYLIKTDpegtivrsKYDLSNLKEIWCGGEVIEESIPEY 398
Cdd:cd17655 203 -GNTLYIVRK---ETVLDGQALTQYIRQNRITIIDLTPAHLKLLDAAD--------DSEGLSLKHLIVGGEALSTELAKK 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 399 IEQKLKIKC--LRVFGQSE--IGVTSF-ISVHALNIPYRATGVP----SIYI-----RPSILSEEGEVLNSNEiGLVAFK 464
Cdd:cd17655 271 IIELFGTNPtiTNAYGPTEttVDASIYqYEPETDQQVSVPIGKPlgntRIYIldqygRPQPVGVAGELYIGGE-GVARGY 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 465 LPMPpsfTITfyknDEKFKQlfTRF-PG--YYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLE 541
Cdd:cd17655 350 LNRP---ELT----AEKFVD--DPFvPGerMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKE 420
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66822213 542 ccSIGILSPDCHTAPIGILVLKENPSIDLNKLQNEinniITQDIESLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:cd17655 421 --AVVIARKDEQGQNYLCAYIVSEKELPVAQLREF----LARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
258-613 |
3.55e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 60.36 E-value: 3.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 258 YILYTSGTTGNTKAVVRSNGPHMVGIKYYTFRKESDIPQIVFSHTNIGWVSFHGFFYGLLSGGNTLVMYEGGIiknkHME 337
Cdd:PRK12316 4698 YVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSL----WDP 4773
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 338 DDLWIAIVKHKVTHTFPSPSVFRYLIKTDPEgtivrsKYDLSNLKEIWCGGEVIEESIPEYIEQKLKIKCL-RVFGQSEI 416
Cdd:PRK12316 4774 ERLYAEIHEHRVTVLVFPPVYLQQLAEHAER------DGEPPSLRVYCFGGEAVAQASYDLAWRALKPVYLfNGYGPTET 4847
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 417 GVTSFISVHALNIPYRATGVP--------SIYI-----RPSILSEEGEVLNSNEigLVAFKLPMPPSFTITFYKNDeKFK 483
Cdd:PRK12316 4848 TVTVLLWKARDGDACGAAYMPigtplgnrSGYVldgqlNPLPVGVAGELYLGGE--GVARGYLERPALTAERFVPD-PFG 4924
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 484 QLFTRFpgyYDSGDLGYKDQRGFYTIVSRSDDQIKI-GFnKIQLNTIDTSILKHPSVLEccSIGILSPDCHTAP-IGILV 561
Cdd:PRK12316 4925 APGGRL---YRTGDLARYRADGVIDYLGRVDHQVKIrGF-RIELGEIEARLREHPAVRE--AVVIAQEGAVGKQlVGYVV 4998
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 66822213 562 LKENPSIDLNKLQ----NEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:PRK12316 4999 PQDPALADADEAQaelrDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKAL 5054
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
92-541 |
5.50e-09 |
|
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: 59.02 E-value: 5.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 92 KLTYYQLYEKVCEFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGatqctlfdGSSVKslidrietITPKLIITT 171
Cdd:cd17656 13 KLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAG--------GAFVP--------IDPEYPEER 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 172 NYGILNDEIITFtpnlkeaielstfkpsnvitlfrneVLDETKLKKVQTIPTIPNTLSWYDEIKKLKENNQSPfyeyvpV 251
Cdd:cd17656 77 RIYIMLDSGVRV-------------------------VLTQRHLKSKLSFNKSTILLEDPSISQEDTSNIDYI------N 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 252 ESSHPLYILYTSGTTGNTKAVVRsngPH--MVGIKYYTFRK-ESDIPQIVFSHTNIGW-VSFHGFFYGLLSGGnTLVmye 327
Cdd:cd17656 126 NSDDLLYIIYTSGTTGKPKGVQL---EHknMVNLLHFEREKtNINFSDKVLQFATCSFdVCYQEIFSTLLSGG-TLY--- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 328 ggIIKNKHMED-DLWIAIVKHKVTHTFPSPSVFRYLIKTDPEgtivrSKYDL-SNLKEIWCGGE--VIEESIPEYIEQKl 403
Cdd:cd17656 199 --IIREETKRDvEQLFDLVKRHNIEVVFLPVAFLKFIFSERE-----FINRFpTCVKHIITAGEqlVITNEFKEMLHEH- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 404 KIKCLRVFGQSEIGVTSFISV-HALNIP-YRATGVPSIYIRPSILSEEGEVlnsNEIGLVAFKLPMPPSFTITFYKNDEK 481
Cdd:cd17656 271 NVHLHNHYGPSETHVVTTYTInPEAEIPeLPPIGKPISNTWIYILDQEQQL---QPQGIVGELYISGASVARGYLNRQEL 347
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66822213 482 FKQLFTRFP-----GYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLE 541
Cdd:cd17656 348 TAEKFFPDPfdpneRMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSE 412
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
91-613 |
5.59e-09 |
|
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: 58.98 E-value: 5.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 91 IKLTYYQLYEKVCEFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGSSVKSLIDRIETITPKLIIt 170
Cdd:cd05915 23 HRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLL- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 171 tnygiLNDEIITFTpnlkeaielstfkpsnvitlfrnevldETKLKKVQTIPTIPNTLSWYDEIKKLKENNQSPFYEYVP 250
Cdd:cd05915 102 -----FDPNLLPLV---------------------------EAIRGELKTVQHFVVMDEKAPEGYLAYEEALGEEADPVR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 251 VESSHPLYILYTSGTTGNTKAVVRSN-GPHMVGIKYYTFRKESDIPQIVFSHTnIGWVSFHGFFYGLlsggnTLVMYEGG 329
Cdd:cd05915 150 VPERAACGMAYTTGTTGLPKGVVYSHrALVLHSLAASLVDGTALSEKDVVLPV-VPMFHVNAWCLPY-----AATLVGAK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 330 IIKNKHMEDD--LWIAIVKHKVTHTFPSPSVFRYLIKTDPEgtiVRSKYDLSnlKEIWCGGevieeSIPEYIEQKLK--- 404
Cdd:cd05915 224 QVLPGPRLDPasLVELFDGEGVTFTAGVPTVWLALADYLES---TGHRLKTL--RRLVVGG-----SAAPRSLIARFerm 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 405 -IKCLRVFGQSEI---GVTSFISVHALNIPYRATGVPSIYIRPSILSEEGEVLNSNEI-----GLVAFKLPMPPSFTITF 475
Cdd:cd05915 294 gVEVRQGYGLTETspvVVQNFVKSHLESLSEEEKLTLKAKTGLPIPLVRLRVADEEGRpvpkdGKALGEVQLKGPWITGG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 476 YKNDEKFKQLFTRFPGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGILSPDCHTA 555
Cdd:cd05915 374 YYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQER 453
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 66822213 556 PIGILVLKENPSidlnkLQNEINNIITQDIESLAVLKKIIVINQ-LPKTKVGKIPRQIL 613
Cdd:cd05915 454 PLAVVVPRGEKP-----TPEELNEHLLKAGFAKWQLPDAYVFAEeIPRTSAGKFLKRAL 507
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
93-547 |
5.95e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 58.79 E-value: 5.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 93 LTYYQLYEKVCEFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGSSVKSLIDRIETITPKLIIttn 172
Cdd:PRK07788 75 LTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVAAREGVKALV--- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 173 ygiLNDEiitFTPNLKEAielstfkPSNVI---TLFRNEVLDETKLKKVQTIptipntlswyDEIkkLKENNQSPFyeyv 249
Cdd:PRK07788 152 ---YDDE---FTDLLSAL-------PPDLGrlrAWGGNPDDDEPSGSTDETL----------DDL--IAGSSTAPL---- 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 250 PVESSHPLYILYTSGTTGNTKAVVRS--NGPHMVG--IKYYTFRKESDIpQIV--------FSHTNIGWvsfhgffyGLl 317
Cdd:PRK07788 203 PKPPKPGGIVILTSGTTGTPKGAPRPepSPLAPLAglLSRVPFRAGETT-LLPapmfhatgWAHLTLAM--------AL- 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 318 sgGNTLVMYEggIIKNKHMEDDlwiaIVKHKVTHTFPSPSVFRYLIKTDPEgtiVRSKYDLSNLKEIWCGGEVIEesiPE 397
Cdd:PRK07788 273 --GSTVVLRR--RFDPEATLED----IAKHKATALVVVPVMLSRILDLGPE---VLAKYDTSSLKIIFVSGSALS---PE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 398 YIEQKLK----IKClRVFGQSEIGVTSFISVHALNIPYRATGVPSIYIRPSILSEEGEVLNSNEIGLVafklpmppsfti 473
Cdd:PRK07788 339 LATRALEafgpVLY-NLYGSTEVAFATIATPEDLAEAPGTVGRPPKGVTVKILDENGNEVPRGVVGRI------------ 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 474 tFYKNDEKFKQlFT------RFPGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGI 547
Cdd:PRK07788 406 -FVGNGFPFEG-YTdgrdkqIIDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGV 483
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
248-542 |
1.14e-08 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 57.80 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 248 YVPVESSHP-----------------------LYILYTSGTTGNTKAVVRSNGP----HMVGIKYYTFRKESDIPQIVFS 300
Cdd:cd17648 65 YVPIDPSYPderiqfiledtgarvvitnstdlAYAIYTSGTTGKPKGVLVEHGSvvnlRTSLSERYFGRDNGDEAVLFFS 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 301 HtnigWVsFHGFFYGL---LSGGNTLVMYEGGIIKNKhmeDDLWIAIVKHKVTHTFPSPSVFryliktdpegtivrSKYD 377
Cdd:cd17648 145 N----YV-FDFFVEQMtlaLLNGQKLVVPPDEMRFDP---DRFYAYINREKVTYLSGTPSVL--------------QQYD 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 378 LS---NLKEIWCGGEVIEESIPEYIEQKLKIKCLRVFGQSEIGVTSFISVHALNIPY-RATGVPSIYIRPSILSEEGEVL 453
Cdd:cd17648 203 LArlpHLKRVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTETTVTNHKRFFPGDQRFdKSLGRPVRNTKCYVLNDAMKRV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 454 NSNEIG------------------LVAFKLPMPPsftitFYKNDEKfkqLFTRFPGYYDSGDLGYKDQRGFYTIVSRSDD 515
Cdd:cd17648 283 PVGAVGelylggdgvargylnrpeLTAERFLPNP-----FQTEQER---ARGRNARLYKTGDLVRWLPSGELEYLGRNDF 354
|
330 340
....*....|....*....|....*..
gi 66822213 516 QIKIGFNKIQLNTIDTSILKHPSVLEC 542
Cdd:cd17648 355 QVKIRGQRIEPGEVEAALASYPGVREC 381
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
251-613 |
1.18e-08 |
|
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: 57.70 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 251 VESSHPLYILYTSGTTGNTKAVVRSNGpHMVGIKYYTfrkESDIPqivFSHTNIgWVSFHGF--------FYGLLSGGNT 322
Cdd:cd17643 90 TDPDDLAYVIYTSGSTGRPKGVVVSHA-NVLALFAAT---QRWFG---FNEDDV-WTLFHSYafdfsvweIWGALLHGGR 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 323 LVMYEGGIIKNkhmEDDLWIAIVKHKVTHTFPSPSVFRYLIKTDPEGTIvrskyDLSNLKEIWCGGEVIEESIPEYIEQK 402
Cdd:cd17643 162 LVVVPYEVARS---PEDFARLLRDEGVTVLNQTPSAFYQLVEAADRDGR-----DPLALRYVIFGGEALEAAMLRPWAGR 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 403 LKIKCLRV---FGQSEIGV-TSFISVHALNIPYRAT---GVP----SIYI-----RPSILSEEGEVLNS---------NE 457
Cdd:cd17643 234 FGLDRPQLvnmYGITETTVhVTFRPLDAADLPAAAAspiGRPlpglRVYVldadgRPVPPGVVGELYVSgagvargylGR 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 458 IGLVAFKLPMPPsftitfykndekfkqlFTRfPG--YYDSGDLGYKDQRGFYTIVSRSDDQIKI-GFnKIQLNTIDTSIL 534
Cdd:cd17643 314 PELTAERFVANP----------------FGG-PGsrMYRTGDLARRLPDGELEYLGRADEQVKIrGF-RIELGEIEAALA 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 535 KHPSVLECCSIGILSPDCHTAPIGILVLKENPSIDLNKLQNEINniitqdiESLA---VLKKIIVINQLPKTKVGKIPRQ 611
Cdd:cd17643 376 THPSVRDAAVIVREDEPGDTRLVAYVVADDGAAADIAELRALLK-------ELLPdymVPARYVPLDALPLTVNGKLDRA 448
|
..
gi 66822213 612 IL 613
Cdd:cd17643 449 AL 450
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
375-613 |
1.30e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 57.85 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 375 KYDLSNLKEIWCGGEVIEESIPEYIEQKLKIKCLRVFGQSEIG-VTSFISVHALNIPYRATGVPSIYIRpsILSEEGEVL 453
Cdd:PRK05677 322 KLDFSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSpVVSVNPSQAIQVGTIGIPVPSTLCK--VIDDDGNEL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 454 NSNEIGLVAFKlpmPPSFTITFYKNDEKFKQLFTRfPGYYDSGDLGYKDQRGFYTIVSRSDDQIKI-GFNkIQLNTIDTS 532
Cdd:PRK05677 400 PLGEVGELCVK---GPQVMKGYWQRPEATDEILDS-DGWLKTGDIALIQEDGYMRIVDRKKDMILVsGFN-VYPNELEDV 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 533 ILKHPSVLECCSIGIlsPDCHTAP-IGI-LVLKENPSIDLNKLQNEINNIITqdieSLAVLKKIIVINQLPKTKVGKIPR 610
Cdd:PRK05677 475 LAALPGVLQCAAIGV--PDEKSGEaIKVfVVVKPGETLTKEQVMEHMRANLT----GYKVPKAVEFRDELPTTNVGKILR 548
|
...
gi 66822213 611 QIL 613
Cdd:PRK05677 549 REL 551
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
259-608 |
1.36e-08 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 58.40 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 259 ILYTSGTTGNTKAVVRSNGPHMvgikyytfrkeSDIPQI--VF---SHTNIgwVS----FHGF------FYGLLSGgnTL 323
Cdd:PRK08633 787 IIFSSGSEGEPKGVMLSHHNIL-----------SNIEQIsdVFnlrNDDVI--LSslpfFHSFgltvtlWLPLLEG--IK 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 324 VMY-----EG-GIIKnkhmeddlwiAIVKHKVTHTFPSPSVFR-YL--IKTDPEgtivrskyDLSNLKEIWCGGEVIEES 394
Cdd:PRK08633 852 VVYhpdptDAlGIAK----------LVAKHRATILLGTPTFLRlYLrnKKLHPL--------MFASLRLVVAGAEKLKPE 913
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 395 IPEYIEQKLKIKCLRVFGQSEigvTSfiSVHALNIP-------YRATG---------VPSIYIRpsILS-EEGEVLNSNE 457
Cdd:PRK08633 914 VADAFEEKFGIRILEGYGATE---TS--PVASVNLPdvlaadfKRQTGskegsvgmpLPGVAVR--IVDpETFEELPPGE 986
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 458 IGLVAFKLP--MppsftITFYKNDEKFKQLFT--RFPGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSI 533
Cdd:PRK08633 987 DGLILIGGPqvM-----KGYLGDPEKTAEVIKdiDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEEL 1061
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66822213 534 LK--HPSVLECCSIGIlsPDchtAPIG--ILVLKENPSIDLNKLQNEINNiitQDIESLAVLKKIIVINQLPKTKVGKI 608
Cdd:PRK08633 1062 AKalGGEEVVFAVTAV--PD---EKKGekLVVLHTCGAEDVEELKRAIKE---SGLPNLWKPSRYFKVEALPLLGSGKL 1132
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
93-542 |
1.79e-08 |
|
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: 57.30 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 93 LTYYQLYEKVCEFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGSSVksliDRIEtitpkliittn 172
Cdd:cd12116 13 LSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPA----DRLR----------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 173 yGILNDEiitftpnlkeaielstfKPSNVITlfrnevlDETKLKKVQTIPTIPNTLSWYDEIkklkennqSPFYEYVPVE 252
Cdd:cd12116 78 -YILEDA-----------------EPALVLT-------DDALPDRLPAGLPVLLLALAAAAA--------APAAPRTPVS 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 253 SSHPLYILYTSGTTGNTKAVVRSN----------------GP--HMVGIKYYTFrkesDIpqivfshtnigwvSFHGFFY 314
Cdd:cd12116 125 PDDLAYVIYTSGSTGRPKGVVVSHrnlvnflhsmrerlglGPgdRLLAVTTYAF----DI-------------SLLELLL 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 315 GLLSGGnTLVMYEGGIIKNKHmedDLWIAIVKHKVTHTFPSPSVFRYLIKTDPEGtivrskydLSNLKeIWCGGEVIEES 394
Cdd:cd12116 188 PLLAGA-RVVIAPRETQRDPE---ALARLIEAHSITVMQATPATWRMLLDAGWQG--------RAGLT-ALCGGEALPPD 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 395 IPEYIeqKLKIKCL-RVFGQSEIGVTSfiSVHALNIPYRAT--GVP----SIYI-----RPSILSEEGEVLnsneIGlva 462
Cdd:cd12116 255 LAARL--LSRVGSLwNLYGPTETTIWS--TAARVTAAAGPIpiGRPlantQVYVldaalRPVPPGVPGELY----IG--- 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 463 fklpmPPSFTITFYKNDEKFKQLFTRFPGY------YDSGDLGYKDQRGFYTIVSRSDDQIKI-GFnKIQLNTIDTSILK 535
Cdd:cd12116 324 -----GDGVAQGYLGRPALTAERFVPDPFAgpgsrlYRTGDLVRRRADGRLEYLGRADGQVKIrGH-RIELGEIEAALAA 397
|
....*..
gi 66822213 536 HPSVLEC 542
Cdd:cd12116 398 HPGVAQA 404
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
94-613 |
4.99e-08 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 56.14 E-value: 4.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 94 TYYQLYEKVCEFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGAtqctLFDGSSVKSLIDRI----ETITPKLII 169
Cdd:PLN02330 57 TYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGG----VFSGANPTALESEIkkqaEAAGAKLIV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 170 T--TNYGILndeiitftpnlkEAIELSTFkpsnvitlfrneVLDETKlkkvqtiptIPNTLSWYDEIKKLKENNQSPFYE 247
Cdd:PLN02330 133 TndTNYGKV------------KGLGLPVI------------VLGEEK---------IEGAVNWKELLEAADRAGDTSDNE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 248 yvPVESSHPLYILYTSGTTGNTKAVVRSNGPHMVGIKYYTFrkeSDIPQIVFSHTNIGWVSFHgFFYGLLSGGNTLVMYE 327
Cdd:PLN02330 180 --EILQTDLCALPFSSGTTGISKGVMLTHRNLVANLCSSLF---SVGPEMIGQVVTLGLIPFF-HIYGITGICCATLRNK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 328 GGIIKNKHMEDDLWI-AIVKHKVTHTFPSPSVFRYLIKtDPegtiVRSKYDLSNLK--EIWCGGEVIEESIPEYIEQKL- 403
Cdd:PLN02330 254 GKVVVMSRFELRTFLnALITQEVSFAPIVPPIILNLVK-NP----IVEEFDLSKLKlqAIMTAAAPLAPELLTAFEAKFp 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 404 KIKCLRVFGQSEigvTSFISVHALNiPYRATGVP---SI-YIRPS-----ILSEEGEVLNSNEIGLVAFKlpmPPSFTIT 474
Cdd:PLN02330 329 GVQVQEAYGLTE---HSCITLTHGD-PEKGHGIAkknSVgFILPNlevkfIDPDTGRSLPKNTPGELCVR---SQCVMQG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 475 FYKNDEKFKQLFTRfPGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGILSPDCHT 554
Cdd:PLN02330 402 YYNNKEETDRTIDE-DGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGE 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 66822213 555 APIGILVLkeNPSIdlNKLQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:PLN02330 481 IPAACVVI--NPKA--KESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLL 535
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
82-283 |
5.53e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 56.14 E-value: 5.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 82 YECPFLKKTIKLTYYQLYEKVCEFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCArigatqctlfdgssvkslidrie 161
Cdd:PTZ00216 111 MEVTHFNETRYITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIW----------------------- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 162 tiTPKLIITTNYGILNDEIITFTpnLKE----AIELSTFKPSNVITLFRNEVLDETKLKKVQTIPTIPNT-----LSWYD 232
Cdd:PTZ00216 168 --SQSMVAATVYANLGEDALAYA--LREteckAIVCNGKNVPNLLRLMKSGGMPNTTIIYLDSLPASVDTegcrlVAWTD 243
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66822213 233 EIKKLKEnnqspfyeyvpVESSHPL----------YILYTSGTTGNTKAVVRSNGPHMVGI 283
Cdd:PTZ00216 244 VVAKGHS-----------AGSHHPLnipennddlaLIMYTSGTTGDPKGVMHTHGSLTAGI 293
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
93-277 |
1.37e-07 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 54.74 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 93 LTYYQLYEKVCEFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGSSVKSLIDRI-ETitpklIITT 171
Cdd:PLN02387 107 ITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLnET-----EVTT 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 172 nygilndeIITFTPNLKEAIELStfkpSNVITLFRNEVLDETKLKKVQTIPTIPN-TLSWYDEIKKLKENNqspfyeyvP 250
Cdd:PLN02387 182 --------VICDSKQLKKLIDIS----SQLETVKRVIYMDDEGVDSDSSLSGSSNwTVSSFSEVEKLGKEN--------P 241
|
170 180 190
....*....|....*....|....*....|..
gi 66822213 251 VESSHPL-----YILYTSGTTGNTKAVVRSNG 277
Cdd:PLN02387 242 VDPDLPSpndiaVIMYTSGSTGLPKGVMMTHG 273
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
73-273 |
1.87e-07 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 54.34 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 73 AKRDQDALIYECPFLKKTIKLTYYQLYEKVCEFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFdgss 152
Cdd:COG1022 21 AARFPDRVALREKEDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPIY---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 153 vkslidriETITPKLIIttnYgILNDeiitftpnlkeaielstfkpSNVITLFrneVLDETKLKKVQTI----PTI---- 224
Cdd:COG1022 97 --------PTSSAEEVA---Y-ILND--------------------SGAKVLF---VEDQEQLDKLLEVrdelPSLrhiv 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66822213 225 ----------PNTLSWyDEIKKLKENNQSP-FYEYVP--VESSHPLYILYTSGTTGNTKAVV 273
Cdd:COG1022 142 vldprglrddPRLLSL-DELLALGREVADPaELEARRaaVKPDDLATIIYTSGTTGRPKGVM 202
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
490-613 |
2.81e-07 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 53.46 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 490 PGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGIlsPDCH--TAPIGILVLKeNPS 567
Cdd:PRK07445 323 QGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGL--PDPHwgEVVTAIYVPK-DPS 399
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 66822213 568 IDLNKLQNEinniITQDIESLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:PRK07445 400 ISLEELKTA----IKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQL 441
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
475-613 |
3.98e-07 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 52.92 E-value: 3.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 475 FYKNDEKFKQLFTRfpGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGILSPDCHT 554
Cdd:PLN02479 416 YLKNPKANEEAFAN--GWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGE 493
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 555 APIGILVLKEN-PSIDLNKLQNEINNIITQDIESLAVLKKiIVINQLPKTKVGKIPRQIL 613
Cdd:PLN02479 494 SPCAFVTLKPGvDKSDEAALAEDIMKFCRERLPAYWVPKS-VVFGPLPKTATGKIQKHVL 552
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
60-613 |
8.36e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 52.05 E-value: 8.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 60 TCYNLLDIHiknpAKRDQDALiyecPFLKKTIKLTYYQLYEKVCEFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCAR 139
Cdd:PRK06164 11 TLASLLDAH----ARARPDAV----ALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 140 IGATQC---TLFDGSSVKSLIDRIETitpkliittnygilndEIITFTPNLKE---AIELSTFKPSNVITLFRNEVLDET 213
Cdd:PRK06164 83 LGATVIavnTRYRSHEVAHILGRGRA----------------RWLVVWPGFKGidfAAILAAVPPDALPPLRAIAVVDDA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 214 KlkkvQTIPTiPNTLSWYDEIkklkennQSPFYEYVPVESSHP-----LYILYT-SGTTGNTKAVVRSNGphmvgikyyT 287
Cdd:PRK06164 147 A----DATPA-PAPGARVQLF-------ALPDPAPPAAAGERAadpdaGALLFTtSGTTSGPKLVLHRQA---------T 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 288 FRKESDIPQIVFS----HTNIGWVSFHGFF-----YGLLSGGNTLVM---YEGGIIKNkhmeddlwiAIVKHKVTHTFPS 355
Cdd:PRK06164 206 LLRHARAIARAYGydpgAVLLAALPFCGVFgfstlLGALAGGAPLVCepvFDAARTAR---------ALRRHRVTHTFGN 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 356 PSVFRYLIKTDPEgtivrsKYDLSNLKeiWCGGEVIEESIPEYIEQKLK--IKCLRVFGQSEigVTSFISVHALNIPYR- 432
Cdd:PRK06164 277 DEMLRRILDTAGE------RADFPSAR--LFGFASFAPALGELAALARArgVPLTGLYGSSE--VQALVALQPATDPVSv 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 433 ---ATGVPsiyIRPSIL-----SEEGEVLNSNEIGLVAFKlpmPPSFTITFYKNDEKFKQLFTRfPGYYDSGDLGYKDQR 504
Cdd:PRK06164 347 rieGGGRP---ASPEARvrardPQDGALLPDGESGEIEIR---APSLMRGYLDNPDATARALTD-DGYFRTGDLGYTRGD 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 505 GFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGILSpDCHTAPIGILVLKENPSIDLNKLqneinniITQD 584
Cdd:PRK06164 420 GQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATR-DGKTVPVAFVIPTDGASPDEAGL-------MAAC 491
|
570 580 590
....*....|....*....|....*....|....*
gi 66822213 585 IESLAVLK---KIIVINQLPKTKVG---KIPRQIL 613
Cdd:PRK06164 492 REALAGFKvpaRVQVVEAFPVTESAngaKIQKHRL 526
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
258-543 |
1.03e-06 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 51.70 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 258 YILYTSGTTGNTKAV---VRSNGPHMVGikyytFRKESDIPQ--IVFShTNIGW--VSFHGFFYGLLSGGnTLVMYEGGI 330
Cdd:cd17654 122 YVIHTSGTTGTPKIVavpHKCILPNIQH-----FRSLFNITSedILFL-TSPLTfdPSVVEIFLSLSSGA-TLLIVPTSV 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 331 IKNKHMEDDlwIAIVKHKVTHTFPSPSVFRYLIKTDPEGTiVRSKydLSNLKEIWCGGE-----VIEESipeYIEQKLKI 405
Cdd:cd17654 195 KVLPSKLAD--ILFKRHRITVLQATPTLFRRFGSQSIKST-VLSA--TSSLRVLALGGEpfpslVILSS---WRGKGNRT 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 406 KCLRVFGQSEigVTSFISVHalNIPYRATGVP--------SIYIRPSILSE-EGEVlnsnEIGLVAFKLPMPPSFTITFY 476
Cdd:cd17654 267 RIFNIYGITE--VSCWALAY--KVPEEDSPVQlgspllgtVIEVRDQNGSEgTGQV----FLGGLNRVCILDDEVTVPKG 338
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66822213 477 KNdekfkqlftrfpgyYDSGDLgYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECC 543
Cdd:cd17654 339 TM--------------RATGDF-VTVKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCA 390
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
343-569 |
2.99e-06 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 49.61 E-value: 2.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 343 AIVKHKVTHTFPSPSVFRYLIKTDPEGtivrsKYDLSNL-----KEIWCGGEVIEESIPEYieqklkikCLRVFGQSEig 417
Cdd:cd17636 83 LIEAERCTHAFLLPPTIDQIVELNADG-----LYDLSSLrsspaAPEWNDMATVDTSPWGR--------KPGGYGQTE-- 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 418 VTSFISVHALNIPYRAT-GVPSIYIRPSILSEEGEVLNSNEIGLVAFKLPMppsfTITFYKNDEKFKQLFTRFpGYYDSG 496
Cdd:cd17636 148 VMGLATFAALGGGAIGGaGRPSPLVQVRILDEDGREVPDGEVGEIVARGPT----VMAGYWNRPEVNARRTRG-GWHHTN 222
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66822213 497 DLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGILSPDCHTAPIGILVLKENPSID 569
Cdd:cd17636 223 DLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASVT 295
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
249-613 |
4.46e-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: 49.62 E-value: 4.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 249 VPVESSHPLYILYTSGTTGNTKAVVRSNGPHMVGIKYYTFRKESDIPQIVFSHTNIGW-VSFHGFFyGLLSGGNTLVMYE 327
Cdd:cd12115 100 VLTDPDDLAYVIYTSGSTGRPKGVAIEHRNAAAFLQWAAAAFSAEELAGVLASTSICFdLSVFELF-GPLATGGKVVLAD 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 328 GGIiknkhmedDLWIAIVKHKVTHTFPSPSVFRYLIKTDPEGTIVRSkydlSNLkeiwcGGEVIEESIPEYIEQKLKIKC 407
Cdd:cd12115 179 NVL--------ALPDLPAAAEVTLINTVPSAAAELLRHDALPASVRV----VNL-----AGEPLPRDLVQRLYARLQVER 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 408 LR-VFGQSEigVTSFISVHALniPYRATGVPSIYiRP------SILSEEGEVLNSNEIGL-------VAFKLPMPPSFTI 473
Cdd:cd12115 242 VVnLYGPSE--DTTYSTVAPV--PPGASGEVSIG-RPlantqaYVLDRALQPVPLGVPGElyiggagVARGYLGRPGLTA 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 474 tfykndEKFkqLFTRF-PG--YYDSGDLGYKDQRGFYTIVSRSDDQIKI-GFnKIQLNTIDTSILKHPSVLECCSIGILS 549
Cdd:cd12115 317 ------ERF--LPDPFgPGarLYRTGDLVRWRPDGLLEFLGRADNQVKVrGF-RIELGEIEAALRSIPGVREAVVVAIGD 387
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66822213 550 PDCHTAPIGILVLKENPSIDLnklqNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQIL 613
Cdd:cd12115 388 AAGERRLVAYIVAEPGAAGLV----EDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
93-277 |
9.01e-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: 48.75 E-value: 9.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 93 LTYYQLYEKVCEFSRVLLNLNV--SKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDgssvkslidrieTITPKLIIT 170
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPLYD------------TLGPEAIEY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 171 tnygILND---EIITFTPNLKeaielstfkpsnVITLfrNEVLDETKLKKVQTIPTIPNTLSwydeikklkennqspfye 247
Cdd:cd05927 74 ----ILNHaeiSIVFCDAGVK------------VYSL--EEFEKLGKKNKVPPPPPKPEDLA------------------ 117
|
170 180 190
....*....|....*....|....*....|
gi 66822213 248 yvpvesshplYILYTSGTTGNTKAVVRSNG 277
Cdd:cd05927 118 ----------TICYTSGTTGNPKGVMLTHG 137
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
493-608 |
1.02e-05 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 48.67 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 493 YDSGDLGYKDQRGFYTIVSRSDDQIKI-GFnKIQLNTIDTSILKHPSVLEccSIGILSPDCHTAP--IGILVLKENPSID 569
Cdd:cd17647 374 YRTGDLGRYLPNGDCECCGRADDQVKIrGF-RIELGEIDTHISQHPLVRE--NITLVRRDKDEEPtlVSYIVPRFDKPDD 450
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66822213 570 LN-----------------------KLQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKI 608
Cdd:cd17647 451 ESfaqedvpkevstdpivkgligyrKLIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKV 512
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
249-610 |
1.15e-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: 48.42 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 249 VPVESSHPLYILYTSGTTGNTKAVVRSNGPHMVGIkyytfrkeSDIPQ--IVFSHTNIGWVSFHGF------FYGLLSGG 320
Cdd:cd12114 121 VDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTI--------LDINRrfAVGPDDRVLALSSLSFdlsvydIFGALSAG 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 321 NTLVMYEGgiikNKHMEDDLWI-AIVKHKVTHTFPSPSVFRYLIKTDPEGTIvrskyDLSNLKEIWCGGEVIEESIPEYI 399
Cdd:cd12114 193 ATLVLPDE----ARRRDPAHWAeLIERHGVTLWNSVPALLEMLLDVLEAAQA-----LLPSLRLVLLSGDWIPLDLPARL 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 400 eQKLKIKClRVF---GQSEIGVTS-FISVHALN-----IPYratGVP----SIYIRPSILSE-----EGEVLnsneIGLV 461
Cdd:cd12114 264 -RALAPDA-RLIslgGATEASIWSiYHPIDEVPpdwrsIPY---GRPlanqRYRVLDPRGRDcpdwvPGELW----IGGR 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 462 AFKLPmppsftitfYKNDEKFKQlfTRFP------GYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILK 535
Cdd:cd12114 335 GVALG---------YLGDPELTA--ARFVthpdgeRLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQA 403
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66822213 536 HPSVLECCSIGILSPDcHTAPIGILVLKENPSIDlnkLQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPR 610
Cdd:cd12114 404 HPGVARAVVVVLGDPG-GKRLAAFVVPDNDGTPI---APDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDR 474
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
249-613 |
2.66e-05 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 47.64 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 249 VPVESSHPLYILYTSGTTGNTKAVVRSNGPHMVGIKYYTFRKESDIPQIVFSHTNIGWVSFHGFFYGLLSGGNTLVMYEG 328
Cdd:PRK12316 3191 IRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGP 3270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 329 GIiknkHMEDDLWIAIVKHKVTHTFPS-PSVFRYLIKTDpegtivrSKYDLSNLKEIWCGGEvieeSIPEYIEQKL--KI 405
Cdd:PRK12316 3271 ED----WRDPALLVELINSEGVDVLHAyPSMLQAFLEEE-------DAHRCTSLKRIVCGGE----ALPADLQQQVfaGL 3335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 406 KCLRVFGQSEIGVTSfiSVHALNIPY-------RATGVPSIYI-----RPSILSEEGEVLNSNEiGLVAFKLPMPPSFTI 473
Cdd:PRK12316 3336 PLYNLYGPTEATITV--THWQCVEEGkdavpigRPIANRACYIldgslEPVPVGALGELYLGGE-GLARGYHNRPGLTAE 3412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 474 TFYKNDekfkqlFTRFPGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGILSPDch 553
Cdd:PRK12316 3413 RFVPDP------FVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVDGRQ-- 3484
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 554 tapigiLVLKENPSIDLNKLQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQIL 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 |
2.84e-05 |
|
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: 46.86 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 254 SHPLYILYTSGTTGNTKAVV--RSNGPHMVG--IKYYTFRKESDIPQivFSHtnigwVSFHGFFY----GLLSGGnTLVM 325
Cdd:cd17652 93 DNLAYVIYTSGSTGRPKGVVvtHRGLANLAAaqIAAFDVGPGSRVLQ--FAS-----PSFDASVWellmALLAGA-TLVL 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 326 YEGGIIKNKhmeDDLWIAIVKHKVTHTFPSPSVFRYLiktdPEGtivrskyDLSNLKEIWCGGEVIEesiPEYIEQKLKI 405
Cdd:cd17652 165 APAEELLPG---EPLADLLREHRITHVTLPPAALAAL----PPD-------DLPDLRTLVVAGEACP---AELVDRWAPG 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 406 KC-LRVFGQSEIGVTSFISVhalniPYRATGVPSIYiRPsILSEEGEVLNSNeiglvafkL-PMPPSFTITFY------- 476
Cdd:cd17652 228 RRmINAYGPTETTVCATMAG-----PLPGGGVPPIG-RP-VPGTRVYVLDAR--------LrPVPPGVPGELYiagagla 292
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66822213 477 --------KNDEKFKQLFTRFPG--YYDSGDLGYKDQRGFYTIVSRSDDQIKI-GFnKIQLNTIDTSILKHPSVLE 541
Cdd:cd17652 293 rgylnrpgLTAERFVADPFGAPGsrMYRTGDLARWRADGQLEFLGRADDQVKIrGF-RIELGEVEAALTEHPGVAE 367
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
92-618 |
3.35e-05 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 46.81 E-value: 3.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 92 KLTYYQLYEKVCEFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLfDGSSVKSLIDRI-ETITPKLIIT 170
Cdd:PRK04813 27 KLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPV-DVSSPAERIEMIiEVAKPSLIIA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 171 TNygilnDEIITFTpnlkeaiELSTFKPSNVitlfrnevldetklkkvQTIPTIPNTlswYDEIKKLKENNQspfyeyvp 250
Cdd:PRK04813 106 TE-----ELPLEIL-------GIPVITLDEL-----------------KDIFATGNP---YDFDHAVKGDDN-------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 251 vesshpLYILYTSGTTGNTKAVvrsngphmvgikyytfrkesdipQIvfSHTNIgwVSF--------------------- 309
Cdd:PRK04813 146 ------YYIIFTSGTTGKPKGV-----------------------QI--SHDNL--VSFtnwmledfalpegpqflnqap 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 310 HGF-------FYGLLSGGnTLVMYEGGIIKN-KhmedDLWIAIVKHKVTHTFPSPSvFRYLIKTDPEgtivRSKYDLSNL 381
Cdd:PRK04813 193 YSFdlsvmdlYPTLASGG-TLVALPKDMTANfK----QLFETLPQLPINVWVSTPS-FADMCLLDPS----FNEEHLPNL 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 382 KE-IWCGgevieESIPEYIEQKLKikclrvfgqseigvTSFISVHALNI--PYRATG-VPSI----------------YI 441
Cdd:PRK04813 263 THfLFCG-----EELPHKTAKKLL--------------ERFPSATIYNTygPTEATVaVTSIeitdemldqykrlpigYA 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 442 RP----SILSEEGEVLNSNEIG--LVAfklpmPPSFTITFYKNDEKFKQLFTRFPGY--YDSGDLGYKDQrGFYTIVSRS 513
Cdd:PRK04813 324 KPdsplLIIDEEGTKLPDGEQGeiVIS-----GPSVSKGYLNNPEKTAEAFFTFDGQpaYHTGDAGYLED-GLLFYQGRI 397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 514 DDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGILSPDCHTAPIGILVLKENPSIDLNKLQNEINNIITQDIESLAVLKK 593
Cdd:PRK04813 398 DFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYVVPKEEDFEREFELTKAIKKELKERLMEYMIPRK 477
|
570 580
....*....|....*....|....*
gi 66822213 594 IIVINQLPKTKVGKIPRQILSNLLN 618
Cdd:PRK04813 478 FIYRDSLPLTPNGKIDRKALIEEVN 502
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
64-610 |
4.57e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 46.53 E-value: 4.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 64 LLDIHIKNPAKR-DQDALiyecPFLKKTIklTYYQLYEKVCEFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGA 142
Cdd:PRK05605 34 LVDLYDNAVARFgDRPAL----DFFGATT--TYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 143 T---------------QCTlfD-GSSVKSLIDRIETITPKLIITTNY-GILNDEIITFTPNLKE-AIELstfkPsnvitl 204
Cdd:PRK05605 108 VvvehnplytahelehPFE--DhGARVAIVWDKVAPTVERLRRTTPLeTIVSVNMIAAMPLLQRlALRL----P------ 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 205 frnevLDETKLKKVQTIPTIPNTLSWyDEIKKLKENNQSPFYEYVPVESSHPLYILYTSGTTGNTKAVV------RSN-- 276
Cdd:PRK05605 176 -----IPALRKARAALTGPAPGTVPW-ETLVDAAIGGDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQlthrnlFANaa 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 277 -GPHMV-GIKyytfrkesDIPQIVFSHTNIgwvsFHGffYGLLSGGnTLVMYEGG-IIKNKHMEDDLWIAIVKhKVTHTF 353
Cdd:PRK05605 250 qGKAWVpGLG--------DGPERVLAALPM----FHA--YGLTLCL-TLAVSIGGeLVLLPAPDIDLILDAMK-KHPPTW 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 354 -PS-PSVFRYLIKTDPEGTIvrskyDLSNLKEIWCGGEVIEESIPEYIEQKLKIKCLRVFGQSEigvTSFISV-HALNIP 430
Cdd:PRK05605 314 lPGvPPLYEKIAEAAEERGV-----DLSGVRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTE---TSPIIVgNPMSDD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 431 YRA--TGVP--SIYIR---PSILS------EEGEVLNSNeiglvafklpmPPSFTiTFYKNDEKFKQLFTrfPGYYDSGD 497
Cdd:PRK05605 386 RRPgyVGVPfpDTEVRivdPEDPDetmpdgEEGELLVRG-----------PQVFK-GYWNRPEETAKSFL--DGWFRTGD 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 498 LGYKDQRGFYTIVSRSDDQIkI--GFNkIQLNTIDTSILKHPSVLECCSIGILSPDCHTAPIGILVLKENPSIDLNKLQn 575
Cdd:PRK05605 452 VVVMEEDGFIRIVDRIKELI-ItgGFN-VYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPEGLR- 528
|
570 580 590
....*....|....*....|....*....|....*...
gi 66822213 576 einniiTQDIESLA---VLKKIIVINQLPKTKVGKIPR 610
Cdd:PRK05605 529 ------AYCREHLTrykVPRRFYHVDELPRDQLGKVRR 560
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
493-541 |
8.22e-05 |
|
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: 45.83 E-value: 8.22e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 66822213 493 YDSGDLGYKDQRGFYTIVSRSDDQIKI-GFnKIQLNTIDTSILKHPSVLE 541
Cdd:TIGR03443 680 YRTGDLGRYLPDGNVECCGRADDQVKIrGF-RIELGEIDTHLSQHPLVRE 728
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
490-617 |
8.25e-05 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 45.42 E-value: 8.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 490 PGYYDSGDLGYKDQrGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGILSPDCHTAPIGILVLKENPSID 569
Cdd:PRK07824 233 PGWFRTDDLGALDD-GVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDGGPAPT 311
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 66822213 570 LNKLQNEinniITQDIESLAVLKKIIVINQLPKTKVGKIPRQILSNLL 617
Cdd:PRK07824 312 LEALRAH----VARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRRF 355
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
248-541 |
9.25e-05 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 45.44 E-value: 9.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 248 YVPVESSHPL------------------------YILYTSGTTGNTKAVVRSNGP---HMVGI-KYYTFRKESDIPQivF 299
Cdd:cd17649 64 YVPLDPEYPAerlrymledsgaglllthhprqlaYVIYTSGSTGTPKGVAVSHGPlaaHCQATaERYGLTPGDRELQ--F 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 300 SHtnigwVSFHGF----FYGLLSGGnTLVMYEGGIIKNkhmEDDLWIAIVKHKVTH-TFPSPSVFRYLIKTDPEGTIVRS 374
Cdd:cd17649 142 AS-----FNFDGAheqlLPPLICGA-CVVLRPDELWAS---ADELAEMVRELGVTVlDLPPAYLQQLAEEADRTGDGRPP 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 375 KydlsnLKEIWCGGEVIEesiPEYIEQKLKIKCLRV--FGQSEIGVTSfiSVH---------ALNIPY-RATGVPSIYI- 441
Cdd:cd17649 213 S-----LRLYIFGGEALS---PELLRRWLKAPVRLFnaYGPTEATVTP--LVWkceagaaraGASMPIgRPLGGRSAYIl 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 442 ----RPSILSEEGEVLNSNEiGLVAFKLPMPPSFTITFYKNdeKFKQLFTRFpgyYDSGDLGYKDQRGFYTIVSRSDDQI 517
Cdd:cd17649 283 dadlNPVPVGVTGELYIGGE-GLARGYLGRPELTAERFVPD--PFGAPGSRL---YRTGDLARWRDDGVIEYLGRVDHQV 356
|
330 340
....*....|....*....|....
gi 66822213 518 KIGFNKIQLNTIDTSILKHPSVLE 541
Cdd:cd17649 357 KIRGFRIELGEIEAALLEHPGVRE 380
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
76-286 |
9.29e-05 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 45.64 E-value: 9.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 76 DQDALIYEcpflKKTIklTYYQLYEKVCEFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATqCTLFDGSSV-K 154
Cdd:PRK08279 52 DRPALLFE----DQSI--SYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAV-VALLNTQQRgA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 155 SLIDRIETITPKLIITtnygilndeiitfTPNLKEAIElstfkpsnvitlfrnEVLDETKLKKVQTIPTiPNTLSWYDEI 234
Cdd:PRK08279 125 VLAHSLNLVDAKHLIV-------------GEELVEAFE---------------EARADLARPPRLWVAG-GDTLDDPEGY 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 66822213 235 KKLKEnNQSPFYEYVPVESSHP------LYIlYTSGTTGNTKAVVRSngpHMVGIKYY 286
Cdd:PRK08279 176 EDLAA-AAAGAPTTNPASRSGVtakdtaFYI-YTSGTTGLPKAAVMS---HMRWLKAM 228
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
344-536 |
9.40e-05 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 45.58 E-value: 9.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 344 IVKHKVTHTFPSPSVFRYLIKTDPegtivRSKYDLSNLKEIWCGGEVIEESIPEYIEQKLKIKCLRV-FGQSEigVTSFI 422
Cdd:PRK06334 269 IDEAKVTFLGSTPVFFDYILKTAK-----KQESCLPSLRFVVIGGDAFKDSLYQEALKTFPHIQLRQgYGTTE--CSPVI 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 423 SVHALNIPY--RATGVPSIYIRPSILSEEGEV-LNSNEIGLVafkLPMPPSFTITFYKNDekFKQLFTRFPG--YYDSGD 497
Cdd:PRK06334 342 TINTVNSPKheSCVGMPIRGMDVLIVSEETKVpVSSGETGLV---LTRGTSLFSGYLGED--FGQGFVELGGetWYVTGD 416
|
170 180 190
....*....|....*....|....*....|....*....
gi 66822213 498 LGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKH 536
Cdd:PRK06334 417 LGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEG 455
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
262-418 |
1.67e-04 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 44.37 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 262 TSGTTGNTKAVVRS------------NGPHMVGikyytFRKEsDIPQIVFSHtniG-WVSFHGFFYGL---------LSG 319
Cdd:COG1541 91 SSGTTGKPTVVGYTrkdldrwaelfaRSLRAAG-----VRPG-DRVQNAFGY---GlFTGGLGLHYGAerlgatvipAGG 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 320 GNTlvmyeggiiknkhmeDDLWIAIVKHKVTHTFPSPSVFRYLIKTDPEGTIvrsKYDLSNLKEIWCGGEVIEESIPEYI 399
Cdd:COG1541 162 GNT---------------ERQLRLMQDFGPTVLVGTPSYLLYLAEVAEEEGI---DPRDLSLKKGIFGGEPWSEEMRKEI 223
|
170
....*....|....*....
gi 66822213 400 EQKLKIKCLRVFGQSEIGV 418
Cdd:COG1541 224 EERWGIKAYDIYGLTEVGP 242
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
344-610 |
2.18e-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: 43.80 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 344 IVKHKVTH--TFPsPSVFRYLIKTDpegtivRSKYDLSNLKEIwCGGEVieesiPEYIEQKLKI---KCLRVFGQSEigv 418
Cdd:cd17637 84 IEEEKVTLmgSFP-PILSNLLDAAE------KSGVDLSSLRHV-LGLDA-----PETIQRFEETtgaTFWSLYGQTE--- 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 419 TS-FISVHalniPYR----ATGVPSIYIRPSILSEEGEVLNSNEIGLVAFKLPMppsftiTF--YKNDEKFKQLFTRfPG 491
Cdd:cd17637 148 TSgLVTLS----PYRerpgSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPL------VFqgYWNLPELTAYTFR-NG 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 492 YYDSGDLGYKDQRGFYTIVSRS--DDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGILSPDCHTAPIGILVLKENPSID 569
Cdd:cd17637 217 WHHTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGATLT 296
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 66822213 570 lnklQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPR 610
Cdd:cd17637 297 ----ADELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
94-284 |
2.32e-04 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 44.42 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 94 TYYQLYEKVCEFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFD---GSSVKSLIDRIETITPKLIIT 170
Cdd:PLN02430 78 TYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHSLICVPLYDtlgPGAVDYIVDHAEIDFVFVQDK 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 171 TNYGILNdeiitftPNLKEAIELSTfkpsnvITLFRNeVLDETKLKKVQtIPTIPntLSWYDEIKKLKENNQSPFyeyvP 250
Cdd:PLN02430 158 KIKELLE-------PDCKSAKRLKA------IVSFTS-VTEEESDKASQ-IGVKT--YSWIDFLHMGKENPSETN----P 216
|
170 180 190
....*....|....*....|....*....|....
gi 66822213 251 VESSHPLYILYTSGTTGNTKAVVRSNGPHMVGIK 284
Cdd:PLN02430 217 PKPLDICTIMYTSGTSGDPKGVVLTHEAVATFVR 250
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
491-624 |
2.38e-04 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 44.00 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 491 GYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGILSPDCHTAPIGILVLKEN--PSI 568
Cdd:PRK05620 430 GWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGiePTR 509
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66822213 569 DL-----NKLQNEINNIITQdiESLAVLKKIivinqlPKTKVGKIPRQILSNLLNDPNYQL 624
Cdd:PRK05620 510 ETaerlrDQLRDRLPNWMLP--EYWTFVDEI------DKTSVGKFDKKDLRQHLADGDFEI 562
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
92-169 |
2.57e-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: 43.88 E-value: 2.57e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66822213 92 KLTYYQLYEKVCEFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATQCTLFDGSSVKSLIDRIETITPKLII 169
Cdd:cd05940 3 ALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV 80
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
248-554 |
2.69e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 43.86 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 248 YVPVESSHPLYILYTSGTTGNTKAVVRSNGphMVGIKYY--TFRkesdipqivFSHT--NIGWVS---FHGffygllsgg 320
Cdd:PRK13388 144 HREVDAMDPFMLIFTSGTTGAPKAVRCSHG--RLAFAGRalTER---------FGLTrdDVCYVSmplFHS--------- 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 321 NTLVMyeggiiknkhmeddLWIAIVKHKVTHTFP---SPSVF-------------------RYLIKTdPEgtivrSKYDL 378
Cdd:PRK13388 204 NAVMA--------------GWAPAVASGAAVALPakfSASGFlddvrrygatyfnyvgkplAYILAT-PE-----RPDDA 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 379 SNLKEIWCGGEVIEESIPEYiEQKLKIKCLRVFGQSEIGVtsfISVHALNIPYRATGVP----SIY-------IRPSILS 447
Cdd:PRK13388 264 DNPLRVAFGNEASPRDIAEF-SRRFGCQVEDGYGSSEGAV---IVVREPGTPPGSIGRGapgvAIYnpetlteCAVARFD 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 448 EEGEVLNSNE-IG-LVAfklPMPPSFTITFYKND----EKFKQlftrfpGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGF 521
Cdd:PRK13388 340 AHGALLNADEaIGeLVN---TAGAGFFEGYYNNPeataERMRH------GMYWSGDLAYRDADGWIYFAGRTADWMRVDG 410
|
330 340 350
....*....|....*....|....*....|...
gi 66822213 522 NKIQLNTIDTSILKHPSVLECCSIGIlsPDCHT 554
Cdd:PRK13388 411 ENLSAAPIERILLRHPAINRVAVYAV--PDERV 441
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
242-625 |
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 66822213 242 QSPFYEYVPVESSHPLYILYTSGTTGNTKAVVRSNG-----------PHMVGIKyytfRKESDIPQIVFSHTNiGWvsfh 310
Cdd:PRK07008 164 QDGDYDWPRFDENQASSLCYTSGTTGNPKGALYSHRstvlhaygaalPDAMGLS----ARDAVLPVVPMFHVN-AW---- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 311 GFFYGLLSGGNTLVMyeggiiKNKHME-DDLWIAIVKHKVTHTFPSPSVFRYLIktdpeGTIVRSKYDLSNLKEIWCGGE 389
Cdd:PRK07008 235 GLPYSAPLTGAKLVL------PGPDLDgKSLYELIEAERVTFSAGVPTVWLGLL-----NHMREAGLRFSTLRRTVIGGS 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 390 VIEESIPEYIEQKLKIKCLRVFGQSEI---GVTSFISVHALNIPYRAtgvpsiyiRPSILSEEGEVLNSNEIGLV---AF 463
Cdd:PRK07008 304 ACPPAMIRTFEDEYGVEVIHAWGMTEMsplGTLCKLKWKHSQLPLDE--------QRKLLEKQGRVIYGVDMKIVgddGR 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 464 KLPMP-----------PSFTITFYKNDEKfkqlftrfP---GYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTI 529
Cdd:PRK07008 376 ELPWDgkafgdlqvrgPWVIDRYFRGDAS--------PlvdGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDI 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 530 DTSILKHPSVLECCSIGILSPDCHTAPIGILVLKenPSIDLNKlqNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIP 609
Cdd:PRK07008 448 ENVAVAHPAVAEAACIACAHPKWDERPLLVVVKR--PGAEVTR--EELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQ 523
|
410
....*....|....*.
gi 66822213 610 RQILSNLLNDpnYQLP 625
Cdd:PRK07008 524 KLKLREQFRD--YVLP 537
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
491-614 |
3.22e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 43.90 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 491 GYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGIlsPDCHT--APIGILVLKENPSI 568
Cdd:PRK07867 381 GVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAV--PDPVVgdQVMAALVLAPGAKF 458
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 66822213 569 DLNKLQNEINNiiTQDIESLAVLKKIIVINQLPKTKVGKIPRQILS 614
Cdd:PRK07867 459 DPDAFAEFLAA--QPDLGPKQWPSYVRVCAELPRTATFKVLKRQLS 502
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
491-616 |
4.23e-04 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 43.25 E-value: 4.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 491 GYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGIlsPDCHTAPIGILV--LKENPSI 568
Cdd:PLN02860 414 GWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGV--PDSRLTEMVVACvrLRDGWIW 491
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66822213 569 DLNKLQNEINNIITQDIE--------SLAVLK--KIIVINQ--LPKTKVGKIPR-----QILSNL 616
Cdd:PLN02860 492 SDNEKENAKKNLTLSSETlrhhcrekNLSRFKipKLFVQWRkpFPLTTTGKIRRdevrrEVLSHL 556
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
493-633 |
6.11e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 43.23 E-value: 6.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 493 YDSGDLGYKDQRGFYTIVSRSDDQIKI-GFnKIQLNTIDTSILKHPSVLECCSIGILSPDcHTAPIGILVLK--ENPSID 569
Cdd:PRK05691 2570 YRTGDLVRLRADGLVEYVGRIDHQVKIrGF-RIELGEIESRLLEHPAVREAVVLALDTPS-GKQLAGYLVSAvaGQDDEA 2647
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66822213 570 LNKLQNEINNIITQDIESLAVLKKIIVINQLPKTKVGKIPRQILSN---LLNDPNYQLPDDVNDSEL 633
Cdd:PRK05691 2648 QAALREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPApdpELNRQAYQAPRSELEQQL 2714
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
491-617 |
1.28e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 41.95 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 491 GYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGILSPDCHTAPIGILVLKENPSIDL 570
Cdd:PRK06178 442 GWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTA 521
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 66822213 571 NKLQNEINniitqdiESLAVLK--KIIVINQLPKTKVGKIPRQILSNLL 617
Cdd:PRK06178 522 AALQAWCR-------ENMAVYKvpEIRIVDALPMTATGKVRKQDLQALA 563
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
475-613 |
2.70e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 40.70 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 475 FYKNDEKFKQLFTrfPGYYDSGDLGYKDQRGFYTIVSRSDDQIKIGFNKIQLNTIDTSILKHPSVLECCSIGILSPDCHT 554
Cdd:PRK08162 402 YLKNPKATEEAFA--GGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGE 479
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66822213 555 APIGILVLKENPSIDlnklQNEInniITQDIESLAVLK--KIIVINQLPKTKVGKIPRQIL 613
Cdd:PRK08162 480 VPCAFVELKDGASAT----EEEI---IAHCREHLAGFKvpKAVVFGELPKTSTGKIQKFVL 533
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
92-367 |
3.09e-03 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 40.49 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 92 KLTYYQLYEKVCEFSRVLLNLNVSKNDNVLIFMANTLEPLIAMLSCARIGATqcTLFDGSSVK--SLIDRIETITPKLII 169
Cdd:cd05939 3 HWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVE--TALINSNLRleSLLHCITVSKAKALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 170 TTnygiLNDEIITFTPnlkeaielstfkpsnvitlfrnevldetklkkvqtipTIPNTLswydeikklkennqspfyeyV 249
Cdd:cd05939 81 FN----LLDPLLTQSS-------------------------------------TEPPSQ--------------------D 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66822213 250 PVESSHPLYILYTSGTTGNTKAVVRSNGPH--MVGIKYYTFR-KESDIPQIVFS--HTNIGWVsfhGFFYGLLsGGNTLV 324
Cdd:cd05939 100 DVNFRDKLFYIYTSGTTGLPKAAVIVHSRYyrIAAGAYYAFGmRPEDVVYDCLPlyHSAGGIM---GVGQALL-HGSTVV 175
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 66822213 325 myeggiIKNKHMEDDLWIAIVKHKVTHTFPSPSVFRYLIKTDP 367
Cdd:cd05939 176 ------IRKKFSASNFWDDCVKYNCTIVQYIGEICRYLLAQPP 212
|
|
| |
