|
Name |
Accession |
Description |
Interval |
E-value |
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
36-482 |
0e+00 |
|
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model represents one of several closely related clades of the dihydrolipoamide acetyltransferase subunit of the pyruvate dehydrogenase complex. It includes sequences from mitochondria and from alpha and beta branches of the proteobacteria, as well as from some other bacteria. Sequences from Gram-positive bacteria are not included. The non-enzymatic homolog protein X, which serves as an E3 component binding protein, falls within the clade phylogenetically but is rejected by its low score. [Energy metabolism, Pyruvate dehydrogenase]
Pssm-ID: 273567 [Multi-domain] Cd Length: 436 Bit Score: 636.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 36 IIGMPALSPTMTQGNLAAWTKKEGDQLSPGEVIAEIETDKAQMDFEFQEDGYLAKILVPEGTKDIPVNKPIAVYVEDKAD 115
Cdd:TIGR01349 1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 116 VP-AFKDFKLEDSGS-DSKTSTKAQPAEPQAEKKQEAPAEETKTSAPEAKKSDVAAPQgRIFASPLAKTIALEKGISLKD 193
Cdd:TIGR01349 81 VAdAFKNYKLESSASpAPKPSEIAPTAPPSAPKPSPAPQKQSPEPSSPAPLSDKESGD-RIFASPLAKKLAKEKGIDLSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 194 VHGTGPRGRITKADIESYLEksskqssqtSGAAAATPAAATSSTTAGSAPSPSSTASYEDVPISTMRSIIGERLLQSTQG 273
Cdd:TIGR01349 160 VAGSGPNGRIVKKDIESFVP---------QSPASANQQAAATTPATYPAAAPVSTGSYEDVPLSNIRKIIAKRLLESKQT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 274 IPSYIVSSKISISKLLKLRQSLNATANDKYKLSINDLLVKAITVAAKRVPDANAYWlpNENVIRKFKNVDVSVAVATPTG 353
Cdd:TIGR01349 231 IPHYYVSIECNVDKLLALRKELNAMASEVYKLSVNDFIIKASALALREVPEANSSW--TDNFIRRYKNVDISVAVATPDG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 354 LLTPIVKNCEAKGLSQISNEIKELVKRARINKLAPEEFQGGTICISNMGMnNAVNMFTSIINPPQSTILAIATVERVAVE 433
Cdd:TIGR01349 309 LITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGM-FGIKDFTAIINPPQACILAVGAVEDVAVV 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 398365063 434 DAAAENGFSFDNQVTITGTFDHRTIDGAKGAEFMKELKTVIENPLEMLL 482
Cdd:TIGR01349 388 DNDEEKGFAVASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
26-482 |
2.67e-140 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 413.87 E-value: 2.67e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 26 RCYAS---YPEHTIIGMPALSPTMTQGNLAAWTKKEGDQLSPGEVIAEIETDKAQMDFEFQEDGYLAKILVPEGTKDIPV 102
Cdd:PLN02744 101 RGFSSssdLPPHQEIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKEIKV 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 103 NKPIAVYVEDKADVPAFKDFKLEDSGSDSKTSTKAQPAEPQAEKKQE-APAEETKTSAPEAKksdvAAPQGRIFASPLAK 181
Cdd:PLN02744 181 GEVIAITVEEEEDIGKFKDYKPSSSAAPAAPKAKPSPPPPKEEEVEKpASSPEPKASKPSAP----PSSGDRIFASPLAR 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 182 TIALEKGISLKDVHGTGPRGRITKADIESYLeksskqssqtsgaaaatPAAATSSTTAGSAPSPSSTASYEDVPISTMRS 261
Cdd:PLN02744 257 KLAEDNNVPLSSIKGTGPDGRIVKADIEDYL-----------------ASGGKGATAPPSTDSKAPALDYTDIPNTQIRK 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 262 IIGERLLQSTQGIPSYIVSSKISISKLLKLRQSLNAT--ANDKYKLSINDLLVKAITVAAKRVPDANAYWLpnENVIRKF 339
Cdd:PLN02744 320 VTASRLLQSKQTIPHYYLTVDTRVDKLMALRSQLNSLqeASGGKKISVNDLVIKAAALALRKVPQCNSSWT--DDYIRQY 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 340 KNVDVSVAVATPTGLLTPIVKNCEAKGLSQISNEIKELVKRARINKLAPEEFQGGTICISNMGMNNAVNMFTSIINPPQS 419
Cdd:PLN02744 398 HNVNINVAVQTENGLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLGGPFGIKQFCAIINPPQS 477
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398365063 420 TILAIATVERVAVEdAAAENGFSFDNQVTITGTFDHRTIDGAKGAEFMKELKTVIENPLEMLL 482
Cdd:PLN02744 478 AILAVGSAEKRVIP-GSGPDQYNFASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
267-481 |
1.02e-85 |
|
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to three copies of a lipoyl binding domain followed by the catalytic domain.
Pssm-ID: 425518 [Multi-domain] Cd Length: 212 Bit Score: 262.09 E-value: 1.02e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 267 LLQSTQGIPSYIVSSKISISKLLKLRQSLNATANDKY-KLSINDLLVKAITVAAKRVPDANAYWLPNENVIRKFKNVDVS 345
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEEtKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 346 VAVATPTGLLTPIVKNCEAKGLSQISNEIKELVKRARINKLAPEEFQGGTICISNMGMNNaVNMFTSIINPPQSTILAIA 425
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFG-VTFFTPIINPPQVAILGVG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 398365063 426 TVERVAVedaAAENGFSFDNQVTITGTFDHRTIDGAKGAEFMKELKTVIENPLEML 481
Cdd:pfam00198 160 RIRKRPV---VVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
35-108 |
3.01e-25 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 98.63 E-value: 3.01e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398365063 35 TIIGMPALSPTMTQGNLAAWTKKEGDQLSPGEVIAEIETDKAQMDFEFQEDGYLAKILVPEGTKdIPVNKPIAV 108
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAV 73
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
35-108 |
2.10e-20 |
|
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440274 [Multi-domain] Cd Length: 77 Bit Score: 85.12 E-value: 2.10e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398365063 35 TIIGMPALSPTMTQGNLAAWTKKEGDQLSPGEVIAEIETDKAQMDFEFQEDGYLAKILVPEGTKdIPVNKPIAV 108
Cdd:COG0508 3 IEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDT-VPVGAVIAV 75
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
36-482 |
0e+00 |
|
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model represents one of several closely related clades of the dihydrolipoamide acetyltransferase subunit of the pyruvate dehydrogenase complex. It includes sequences from mitochondria and from alpha and beta branches of the proteobacteria, as well as from some other bacteria. Sequences from Gram-positive bacteria are not included. The non-enzymatic homolog protein X, which serves as an E3 component binding protein, falls within the clade phylogenetically but is rejected by its low score. [Energy metabolism, Pyruvate dehydrogenase]
Pssm-ID: 273567 [Multi-domain] Cd Length: 436 Bit Score: 636.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 36 IIGMPALSPTMTQGNLAAWTKKEGDQLSPGEVIAEIETDKAQMDFEFQEDGYLAKILVPEGTKDIPVNKPIAVYVEDKAD 115
Cdd:TIGR01349 1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 116 VP-AFKDFKLEDSGS-DSKTSTKAQPAEPQAEKKQEAPAEETKTSAPEAKKSDVAAPQgRIFASPLAKTIALEKGISLKD 193
Cdd:TIGR01349 81 VAdAFKNYKLESSASpAPKPSEIAPTAPPSAPKPSPAPQKQSPEPSSPAPLSDKESGD-RIFASPLAKKLAKEKGIDLSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 194 VHGTGPRGRITKADIESYLEksskqssqtSGAAAATPAAATSSTTAGSAPSPSSTASYEDVPISTMRSIIGERLLQSTQG 273
Cdd:TIGR01349 160 VAGSGPNGRIVKKDIESFVP---------QSPASANQQAAATTPATYPAAAPVSTGSYEDVPLSNIRKIIAKRLLESKQT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 274 IPSYIVSSKISISKLLKLRQSLNATANDKYKLSINDLLVKAITVAAKRVPDANAYWlpNENVIRKFKNVDVSVAVATPTG 353
Cdd:TIGR01349 231 IPHYYVSIECNVDKLLALRKELNAMASEVYKLSVNDFIIKASALALREVPEANSSW--TDNFIRRYKNVDISVAVATPDG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 354 LLTPIVKNCEAKGLSQISNEIKELVKRARINKLAPEEFQGGTICISNMGMnNAVNMFTSIINPPQSTILAIATVERVAVE 433
Cdd:TIGR01349 309 LITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGM-FGIKDFTAIINPPQACILAVGAVEDVAVV 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 398365063 434 DAAAENGFSFDNQVTITGTFDHRTIDGAKGAEFMKELKTVIENPLEMLL 482
Cdd:TIGR01349 388 DNDEEKGFAVASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
26-482 |
2.67e-140 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 413.87 E-value: 2.67e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 26 RCYAS---YPEHTIIGMPALSPTMTQGNLAAWTKKEGDQLSPGEVIAEIETDKAQMDFEFQEDGYLAKILVPEGTKDIPV 102
Cdd:PLN02744 101 RGFSSssdLPPHQEIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKEIKV 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 103 NKPIAVYVEDKADVPAFKDFKLEDSGSDSKTSTKAQPAEPQAEKKQE-APAEETKTSAPEAKksdvAAPQGRIFASPLAK 181
Cdd:PLN02744 181 GEVIAITVEEEEDIGKFKDYKPSSSAAPAAPKAKPSPPPPKEEEVEKpASSPEPKASKPSAP----PSSGDRIFASPLAR 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 182 TIALEKGISLKDVHGTGPRGRITKADIESYLeksskqssqtsgaaaatPAAATSSTTAGSAPSPSSTASYEDVPISTMRS 261
Cdd:PLN02744 257 KLAEDNNVPLSSIKGTGPDGRIVKADIEDYL-----------------ASGGKGATAPPSTDSKAPALDYTDIPNTQIRK 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 262 IIGERLLQSTQGIPSYIVSSKISISKLLKLRQSLNAT--ANDKYKLSINDLLVKAITVAAKRVPDANAYWLpnENVIRKF 339
Cdd:PLN02744 320 VTASRLLQSKQTIPHYYLTVDTRVDKLMALRSQLNSLqeASGGKKISVNDLVIKAAALALRKVPQCNSSWT--DDYIRQY 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 340 KNVDVSVAVATPTGLLTPIVKNCEAKGLSQISNEIKELVKRARINKLAPEEFQGGTICISNMGMNNAVNMFTSIINPPQS 419
Cdd:PLN02744 398 HNVNINVAVQTENGLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLGGPFGIKQFCAIINPPQS 477
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398365063 420 TILAIATVERVAVEdAAAENGFSFDNQVTITGTFDHRTIDGAKGAEFMKELKTVIENPLEMLL 482
Cdd:PLN02744 478 AILAVGSAEKRVIP-GSGPDQYNFASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
39-482 |
3.11e-133 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 391.08 E-value: 3.11e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 39 MPALSPTMTQGNLAAWTKKEGDQLSPGEVIAEIETDKAQMDFEFQEDGYLAKILVPEGTKdIPVNKPIAVYVEDKADVPA 118
Cdd:PRK11856 7 MPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDV-VPVGSVIAVIEEEGEAEAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 119 fkdfkledsgsdsktsTKAQPAEPQAEKKQEAPAEETKTSAPEAKKSDVAAPQGRIFASPLAKTIALEKGISLKDVHGTG 198
Cdd:PRK11856 86 ----------------AAAEAAPEAPAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 199 PRGRITKADIESYLEKSSKQSSQTSGAAAATPAAATSSttagsapspsstasYEDVPISTMRSIIGERLLQSTQGIPSYI 278
Cdd:PRK11856 150 PGGRITKEDVEAAAAAAAPAAAAAAAAAAAPPAAAAEG--------------EERVPLSGMRKAIAKRMVESKREIPHFT 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 279 VSSKISISKLLKLRQSLNATAndkYKLSINDLLVKAITVAAKRVPDANAYWlpNENVIRKFKNVDVSVAVATPTGLLTPI 358
Cdd:PRK11856 216 LTDEVDVTALLALRKQLKAIG---VKLTVTDFLIKAVALALKKFPELNASW--DDDAIVLKKYVNIGIAVATDGGLIVPV 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 359 VKNCEAKGLSQISNEIKELVKRARINKLAPEEFQGGTICISNMGMnNAVNMFTSIINPPQSTILAI-ATVERVAVEDaaa 437
Cdd:PRK11856 291 IRDADKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGM-FGGDYFTPIINPPEVAILGVgAIVERPVVVD--- 366
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 398365063 438 eNGFSFDNQVTITGTFDHRTIDGAKGAEFMKELKTVIENPLEMLL 482
Cdd:PRK11856 367 -GEIVVRKVMPLSLSFDHRVIDGADAARFLKALKELLENPALLLL 410
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
267-481 |
1.02e-85 |
|
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to three copies of a lipoyl binding domain followed by the catalytic domain.
Pssm-ID: 425518 [Multi-domain] Cd Length: 212 Bit Score: 262.09 E-value: 1.02e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 267 LLQSTQGIPSYIVSSKISISKLLKLRQSLNATANDKY-KLSINDLLVKAITVAAKRVPDANAYWLPNENVIRKFKNVDVS 345
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEEtKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 346 VAVATPTGLLTPIVKNCEAKGLSQISNEIKELVKRARINKLAPEEFQGGTICISNMGMNNaVNMFTSIINPPQSTILAIA 425
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFG-VTFFTPIINPPQVAILGVG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 398365063 426 TVERVAVedaAAENGFSFDNQVTITGTFDHRTIDGAKGAEFMKELKTVIENPLEML 481
Cdd:pfam00198 160 RIRKRPV---VVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
37-482 |
2.38e-72 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This model describes the TCA cycle 2-oxoglutarate system E2 component, dihydrolipoamide succinyltransferase. It is closely related to the pyruvate dehydrogenase E2 component, dihydrolipoamide acetyltransferase. The seed for this model includes mitochondrial and Gram-negative bacterial forms. Mycobacterial candidates are highly derived, differ in having and extra copy of the lipoyl-binding domain at the N-terminus. They score below the trusted cutoff, but above the noise cutoff and above all examples of dihydrolipoamide acetyltransferase. [Energy metabolism, TCA cycle]
Pssm-ID: 273565 [Multi-domain] Cd Length: 403 Bit Score: 234.63 E-value: 2.38e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 37 IGMPALSPTMTQGNLAAWTKKEGDQLSPGEVIAEIETDKAQMDFEFQEDGYLAKILVPEGTKdIPVNKPIAVYVEdkadv 116
Cdd:TIGR01347 3 IKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDT-VESGQVLAILEE----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 117 pafkdfkledsgsdSKTSTKAQPAEPQAEKkqeapaEETKTSAPEAKKsdvAAPQGRIFASPLAKTIALEKGISLKDVHG 196
Cdd:TIGR01347 77 --------------GNDATAAPPAKSGEEK------EETPAASAAAAP---TAAANRPSLSPAARRLAKEHGIDLSAVPG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 197 TGPRGRITKADIESYLEKSSKQSSQTSGAAAATPAAATSSTtagsapspsstasyEDVPISTMRSIIGERLLQSTQGIPS 276
Cdd:TIGR01347 134 TGVTGRVTKEDIIKKTEAPASAQPPAAAAAAAAPAAATRPE--------------ERVKMTRLRQRIAERLKEAQNSTAM 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 277 YIVSSKISISKLLKLRQSLNATANDKY--KLSINDLLVKAITVAAKRVPDANAYWLPNENVIRKfkNVDVSVAVATPTGL 354
Cdd:TIGR01347 200 LTTFNEVDMSAVMELRKRYKEEFEKKHgvKLGFMSFFVKAVVAALKRFPEVNAEIDGDDIVYKD--YYDISVAVSTDRGL 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 355 LTPIVKNCEAKGLSQISNEIKELVKRARINKLAPEEFQGGTICISNMGMNNAVnMFTSIINPPQSTILAIATV-ERVAVE 433
Cdd:TIGR01347 278 VVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSL-MSTPIINPPQSAILGMHGIkERPVAV 356
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 398365063 434 DAAAENgfsfDNQVTITGTFDHRTIDGAKGAEFMKELKTVIENPLEMLL 482
Cdd:TIGR01347 357 NGQIEI----RPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRRLLL 401
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
5-482 |
1.75e-66 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 219.55 E-value: 1.75e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 5 VRVVPRISRSSVLTRSLRLQLRCYASYPEH---------TIIGMPALSPTMTQGNLAAWTKKEGDQLSPGEVIAEIETDK 75
Cdd:PTZ00144 6 VKRLNKPLLSSVKGMFRRFSLRKLQPACSAhfsksyfsiKVIKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 76 AQMDFEFQEDGYLAKILVPEGTkDIPVNKPIavYVEDKADVPAfkdfkleDSGSDSKTSTKAQPAEPQAEKKQEAPAEET 155
Cdd:PTZ00144 86 VSVDIRAPASGVITKIFAEEGD-TVEVGAPL--SEIDTGGAPP-------AAAPAAAAAAKAEKTTPEKPKAAAPTPEPP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 156 KTSAPEAKKSdVAAPQGRIFASPLAKTIAlekgislkdvhGTGPRGRitkadiesyleksskqssqtsgaaaatpaaats 235
Cdd:PTZ00144 156 AASKPTPPAA-AKPPEPAPAAKPPPTPVA-----------RADPRET--------------------------------- 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 236 sttagsapspsstasyeDVPISTMRSIIGERLLQSTQGIPSYIVSSKISISKLLKLRQSLNATANDKY--KLSINDLLVK 313
Cdd:PTZ00144 191 -----------------RVPMSRMRQRIAERLKASQNTCAMLTTFNECDMSALMELRKEYKDDFQKKHgvKLGFMSAFVK 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 314 AITVAAKRVPDANAYWLPNENVIRKFknVDVSVAVATPTGLLTPIVKNCEAKGLSQISNEIKELVKRARINKLAPEEFQG 393
Cdd:PTZ00144 254 ASTIALKKMPIVNAYIDGDEIVYRNY--VDISVAVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTG 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 394 GTICISNMGMNNAVnMFTSIINPPQSTILAI-ATVERVAVEdaaaengfsfDNQVTITG------TFDHRTIDGAKGAEF 466
Cdd:PTZ00144 332 GTFTISNGGVFGSL-MGTPIINPPQSAILGMhAIKKRPVVV----------GNEIVIRPimylalTYDHRLIDGRDAVTF 400
|
490
....*....|....*.
gi 398365063 467 MKELKTVIENPLEMLL 482
Cdd:PTZ00144 401 LKKIKDLIEDPARMLL 416
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
47-482 |
3.97e-62 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 211.61 E-value: 3.97e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 47 TQGNLAAWTKKEGDQLSPGEVIAEIETDKAQMDFEFQEDGYLAKILVPEGTKdIPVNKPIavyvedkadvpafkdFKLED 126
Cdd:PRK11855 131 TEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDK-VSVGSLL---------------VVIEV 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 127 SGSDSKTSTKAQPAEPQAEK-KQEAPAEETKTSAPEAKKSDVAAPQGRIFASPLAKTIALEKGISLKDVHGTGPRGRITK 205
Cdd:PRK11855 195 AAAAPAAAAAPAAAAPAAAAaAAPAPAPAAAAAPAAAAPAAAAAPGKAPHASPAVRRLARELGVDLSQVKGTGKKGRITK 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 206 ADIESYLEKSSKQSSQTSGAAAATPAAATSSTTAGSAPSPSSTASyEDVPISTMRSIIGERLLQSTQGIPSYIVSSKISI 285
Cdd:PRK11855 275 EDVQAFVKGAMSAAAAAAAAAAAAGGGGLGLLPWPKVDFSKFGEI-ETKPLSRIKKISAANLHRSWVTIPHVTQFDEADI 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 286 SKLLKLRQSLNATANDK-YKLSINDLLVKAITVAAKRVPDANA-YWLPNENVIRKfKNVDVSVAVATPTGLLTPIVKNCE 363
Cdd:PRK11855 354 TDLEALRKQLKKEAEKAgVKLTMLPFFIKAVVAALKEFPVFNAsLDEDGDELTYK-KYFNIGFAVDTPNGLVVPVIKDVD 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 364 AKGLSQISNEIKELVKRARINKLAPEEFQGGTICISNMGMNNAVNmFTSIINPPQSTILAiatVERVAVEDAAAENGFSF 443
Cdd:PRK11855 433 KKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTA-FTPIINAPEVAILG---VGKSQMKPVWDGKEFVP 508
|
410 420 430
....*....|....*....|....*....|....*....
gi 398365063 444 DNQVTITGTFDHRTIDGAKGAEFMKELKTVIENPLEMLL 482
Cdd:PRK11855 509 RLMLPLSLSYDHRVIDGATAARFTNYLKQLLADPRRMLL 547
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
40-482 |
8.66e-61 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 204.30 E-value: 8.66e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 40 PALSPTMTQGNLAAWTKKEGDQLSPGEVIAEIETDKAQMDFEFQEDGYLAKILVPEGTkDIPVNKPIAVYVEDKAdvpaf 119
Cdd:PRK05704 8 PTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGD-TVTVGQVLGRIDEGAA----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 120 kdfkledSGSDSKTSTKAQPAEPQAEKKQEAPAEETKTSApeakksdvaapqgrifASPLAKTIALEKGISLKDVHGTGP 199
Cdd:PRK05704 82 -------AGAAAAAAAAAAAAAAAPAQAQAAAAAEQSNDA----------------LSPAARKLAAENGLDASAVKGTGK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 200 RGRITKADIESYLEKSSKQSSQTSGAAAATPAAATSSTTAgsapspsstasyEDVPISTMRSIIGERLLQSTQGIPSYIV 279
Cdd:PRK05704 139 GGRVTKEDVLAALAAAAAAPAAPAAAAPAAAPAPLGARPE------------ERVPMTRLRKTIAERLLEAQNTTAMLTT 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 280 SSKISISKLLKLRQSLNATANDKY--KLSINDLLVKAITVAAKRVPDANAYWLPNENVIRKFknVDVSVAVATPTGLLTP 357
Cdd:PRK05704 207 FNEVDMTPVMDLRKQYKDAFEKKHgvKLGFMSFFVKAVVEALKRYPEVNASIDGDDIVYHNY--YDIGIAVGTPRGLVVP 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 358 IVKNCEAKGLSQISNEIKELVKRARINKLAPEEFQGGTICISNMGMNNAVnMFTSIINPPQSTILAI-ATVERVAVEdaa 436
Cdd:PRK05704 285 VLRDADQLSFAEIEKKIAELAKKARDGKLSIEELTGGTFTITNGGVFGSL-MSTPIINPPQSAILGMhKIKERPVAV--- 360
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 398365063 437 aengfsfDNQVTITG------TFDHRTIDGAKGAEFMKELKTVIENPLEMLL 482
Cdd:PRK05704 361 -------NGQIVIRPmmylalSYDHRIIDGKEAVGFLVTIKELLEDPERLLL 405
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
47-476 |
4.52e-51 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 183.28 E-value: 4.52e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 47 TQGNLAAWTKKEGDQLSPGEVIAEIETDKAQMDFEFQEDGYLAKILVPEGTKdIPVNKPIAVyVEDKADVPAfkdfkled 126
Cdd:PRK11854 217 DEVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDK-VKTGSLIMR-FEVEGAAPA-------- 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 127 SGSDSKTSTKAQPAEPQAEKKQEAPAeetktsAPEAKKSDVAAPQGRIFASPLAKTIALEKGISLKDVHGTGPRGRITKA 206
Cdd:PRK11854 287 AAPAKQEAAAPAPAAAKAEAPAAAPA------AKAEGKSEFAENDAYVHATPLVRRLAREFGVNLAKVKGTGRKGRILKE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 207 DIESYLEKSSKQSSQTSGAAAATPAAATSSTTAGSAPSPSSTAsyEDVPISTMRSIIGERLLQSTQGIPSYIVSSKISIS 286
Cdd:PRK11854 361 DVQAYVKDAVKRAEAAPAAAAAGGGGPGLLPWPKVDFSKFGEI--EEVELGRIQKISGANLHRNWVMIPHVTQFDKADIT 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 287 KLLKLRQSLNATA-NDKY--KLSINDLLVKAITVAAKRVPDANAYWLPN-ENVIRKfKNVDVSVAVATPTGLLTPIVKNC 362
Cdd:PRK11854 439 ELEAFRKQQNAEAeKRKLgvKITPLVFIMKAVAAALEQMPRFNSSLSEDgQRLTLK-KYVNIGIAVDTPNGLVVPVFKDV 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 363 EAKGLSQISNEIKELVKRARINKLAPEEFQGGTICISNMGMNNAVNmFTSIINPPQSTILAIATVERVAVEDAAAengFS 442
Cdd:PRK11854 518 NKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTH-FTPIVNAPEVAILGVSKSAMEPVWNGKE---FA 593
|
410 420 430
....*....|....*....|....*....|....
gi 398365063 443 FDNQVTITGTFDHRTIDGAKGAEFMKELKTVIEN 476
Cdd:PRK11854 594 PRLMLPLSLSYDHRVIDGADGARFITIINDRLSD 627
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
33-475 |
7.76e-48 |
|
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model represents an Actinobacterial clade of E2 enzyme, a component of the 2-oxoglutarate dehydrogenase complex involved in the TCA cycle. These proteins have multiple domains including the catalytic domain (pfam00198), one or two biotin domains (pfam00364) and an E3-component binding domain (pfam02817).
Pssm-ID: 200219 [Multi-domain] Cd Length: 579 Bit Score: 173.66 E-value: 7.76e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 33 EHTIIGMPALSPTMTQGNLAAWTKKEGDQLSPGEVIAEIETDKAQMDFEFQEDGYLAKILVPEgTKDIPVNKPIAVyVED 112
Cdd:TIGR02927 125 EATEVKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPE-DDTVEVGTVLAI-IGD 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 113 KADVPAFKDFKLEDSGSDSKTSTKAQPA--EPQAEKKQEAPAEETKTSAPEAKKSDVAAPQGRIFASPLAKTIALEKGIS 190
Cdd:TIGR02927 203 ANAAPAEPAEEEAPAPSEAGSEPAPDPAarAPHAAPDPPAPAPAPAKTAAPAAAAPVSSGDSGPYVTPLVRKLAKDKGVD 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 191 LKDVHGTGPRGRITKADIESYLEKSSKQSSQTSGAAAATPAAATSSTTAGSAPSPSSTASYEDvPISTMRSIIGERLLQS 270
Cdd:TIGR02927 283 LSTVKGTGVGGRIRKQDVLAAAKAAEEARAAAAAPAAAAAPAAPAAAAKPAEPDTAKLRGTTQ-KMNRIRQITADKTIES 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 271 TQGIPSYIVSSKISISKLLKLRQSLNATANDKY--KLSINDLLVKAITVAAKRVPDANAYWLPNENVIRKFKNVDVSVAV 348
Cdd:TIGR02927 362 LQTSAQLTQVHEVDMTRVAALRARAKNDFLEKNgvNLTFLPFFVQAVTEALKAHPNVNASYNAETKEVTYHDVEHVGIAV 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 349 ATPTGLLTPIVKNCEAKGLSQISNEIKELVKRARINKLAPEEFQGGTICISNMGMNNAVnMFTSIINPPQSTILAIATVE 428
Cdd:TIGR02927 442 DTPRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGAL-FDTPILNPPQAAILGTGAIV 520
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 398365063 429 R--VAVEDAAAENGFSFDNQVTITGTFDHRTIDGAKGAEFMKELKTVIE 475
Cdd:TIGR02927 521 KrpRVIKDEDGGESIAIRSVCYLPLTYDHRLVDGADAGRFLTTIKKRLE 569
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
57-482 |
9.78e-48 |
|
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]
Pssm-ID: 273566 [Multi-domain] Cd Length: 546 Bit Score: 172.75 E-value: 9.78e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 57 KEGDQLSPGEVIAEIETDKAQMDFEFQEDGYLAKILVPEGTKdIPVNKPIAVYVEDKADVPAfkdfkledsgsdSKTSTK 136
Cdd:TIGR01348 138 KVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDS-VPTGDLILTLSVAGSTPAT------------APAPAS 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 137 AQPAEPQAEKKQEAPAeetktSAPEAKKSDVAAPQGR--------IFASPLAKTIALEKGISLKDVHGTGPRGRITKADI 208
Cdd:TIGR01348 205 AQPAAQSPAATQPEPA-----AAPAAAKAQAPAPQQAgtqnpakvDHAAPAVRRLAREFGVDLSAVKGTGIKGRILREDV 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 209 ESYLEKSSKQSSQTSGAAAATPAAATSSTTAGSAPSPSStasyEDVPISTMRSIIGERLLQSTQGIPSYIVSSKISISKL 288
Cdd:TIGR01348 280 QRFVKEPSVRAQAAAASAAGGAPGALPWPNVDFSKFGEV----EEVDMSRIRKISGANLTRNWTMIPHVTHFDKADITEM 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 289 LKLRQSLNATANDK-YKLSINDLLVKAITVAAKRVPDANAYWLPN-ENVIRKfKNVDVSVAVATPTGLLTPIVKNCEAKG 366
Cdd:TIGR01348 356 EAFRKQQNAAVEKEgVKLTVLHILMKAVAAALKKFPKFNASLDLGgEQLILK-KYVNIGVAVDTPNGLLVPVIKDVDRKG 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 367 LSQISNEIKELVKRARINKLAPEEFQGGTICISNMGmNNAVNMFTSIINPPQSTILAiatVERVAVEDAAAENGFSFDNQ 446
Cdd:TIGR01348 435 ITELALELSDLAKKARDGKLTPDEMQGACFTISSLG-GIGGTAFTPIVNAPEVAILG---VSKSGMEPVWNGKEFEPRLM 510
|
410 420 430
....*....|....*....|....*....|....*.
gi 398365063 447 VTITGTFDHRTIDGAKGAEFMKELKTVIENPLEMLL 482
Cdd:TIGR01348 511 LPLSLSYDHRVIDGADAARFTTYICESLADIRRLLL 546
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
51-482 |
1.38e-44 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 161.43 E-value: 1.38e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 51 LAAWTKKEGDQLSPGEVIAEIETDKAQMDFEFQEDGYLAKILVPEGtkDI-PVNKPIavyvedkadvpafkdFKLEDSGS 129
Cdd:PLN02528 15 LLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPG--DIvKVGETL---------------LKIMVEDS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 130 dsktstkaQPAEPQAEKKQEAPAEETKTSAPEAKKSDVaapqGRIFASPLAKTIALEKGISLKDVHGTGPRGRITKADIE 209
Cdd:PLN02528 78 --------QHLRSDSLLLPTDSSNIVSLAESDERGSNL----SGVLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 210 SYLekssKQSSQTSGAAAATPAAATSSTTAGSAPSPSSTASYED--VPISTMRSIIGERLLQSTQgIPSYIVSSKISISK 287
Cdd:PLN02528 146 KYA----AQKGVVKDSSSAEEATIAEQEEFSTSVSTPTEQSYEDktIPLRGFQRAMVKTMTAAAK-VPHFHYVEEINVDA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 288 LLKLRQSL-NATANDKYKLSINDLLVKAITVAAKRVPDANAYWLPNENVIRKFKNVDVSVAVATPTGLLTPIVKNCEAKG 366
Cdd:PLN02528 221 LVELKASFqENNTDPTVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLS 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 367 LSQISNEIKELVKRARINKLAPEEFQGGTICISNMGmnnAVN-MFTS-IINPPQSTILAIATVERVA--VEDAAAENGfs 442
Cdd:PLN02528 301 LLEITKELSRLQHLAAENKLNPEDITGGTITLSNIG---AIGgKFGSpVLNLPEVAIIALGRIQKVPrfVDDGNVYPA-- 375
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 398365063 443 fdNQVTITGTFDHRTIDGAKGAEFMKELKTVIENPLEMLL 482
Cdd:PLN02528 376 --SIMTVTIGADHRVLDGATVARFCNEWKSYVEKPELLML 413
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
164-482 |
5.10e-44 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 158.14 E-value: 5.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 164 KSDVAA--PQGRIFASPLAKTIALEKGISLKDVHGTGPRGRITKADIESYLeksskqssQTSGAAAATPAAATSSTTAGS 241
Cdd:PRK14843 37 KEDVETykDTNVVRISPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALL--------PENIENDSIKSPAQIEKVEEV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 242 APSPSSTASYEDVPISTMRSIIGERLLQSTQGIPSYIVSSKISISKLLKLRQSLNAT--ANDKYKLSINDLLVKAITVAA 319
Cdd:PRK14843 109 PDNVTPYGEIERIPMTPMRKVIAQRMVESYLTAPTFTLNYEVDMTEMLALRKKVLEPimEATGKKTTVTDLLSLAVVKTL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 320 KRVPDANAYWLPNENVIRKFKNVDVSVAVATPTGLLTPIVKNCEAKGLSQISNEIKELVKRARINKLAPEEFQGGTICIS 399
Cdd:PRK14843 189 MKHPYINASLTEDGKTIITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTIS 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 400 NMGMnNAVNMFTSIINPPQSTILAI-ATVERVAVedaaaENG-FSFDNQVTITGTFDHRTIDGAKGAEFMKELKTVIENP 477
Cdd:PRK14843 269 NLGM-FGVQSFGPIINQPNSAILGVsSTIEKPVV-----VNGeIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETP 342
|
....*
gi 398365063 478 LEMLL 482
Cdd:PRK14843 343 ISMLI 347
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
37-178 |
1.13e-37 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 143.52 E-value: 1.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 37 IGMPALSPTMTQGNLAAWTKKEGDQLSPGEVIAEIETDKAQMDFEFQEDGYLAKILVPEGTKDIPVNKPIAVYVEDkadv 116
Cdd:PRK11892 5 ILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEGVKVNTPIAVLLEE---- 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398365063 117 pafkdfkledsGSDSKTSTKAQPAEPQAEKKQEAPAEETKTSAPEAKKSDVAAPQGRIFASP 178
Cdd:PRK11892 81 -----------GESASDAGAAPAAAAEAAAAAPAAAAAAAAKKAAPAPAAPAAPAAEVAADP 131
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
9-482 |
1.54e-31 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 126.41 E-value: 1.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 9 PRISRS-SVLTRSLRLQLRCYASYPEHTIIGM-PALSPTMTQGNLAAWTKKEGDQLSPGEVIAEIETDKAQMDFEFQEDG 86
Cdd:PLN02226 64 SGISRSaSLVSSTLQRWVRPFSSESGDTVEAVvPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASG 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 87 YLAKILVPEGTKDIPVNKpiavyvedKADVPAFKDFKLEDSGSDSKTSTKAQPAEPQAEKKQEAPAEetktSAPEAKKSD 166
Cdd:PLN02226 144 VIQEFLVKEGDTVEPGTK--------VAIISKSEDAASQVTPSQKIPETTDPKPSPPAEDKQKPKVE----SAPVAEKPK 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 167 VAAPqgrifaSPLAKTIALEKGISLKDvhgtgpRGRitkadiesyleksskqssqtsgaaaatpaaatssttagsapsps 246
Cdd:PLN02226 212 APSS------PPPPKQSAKEPQLPPKE------RER-------------------------------------------- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 247 stasyeDVPISTMRSIIGERLLQSTQGIPSYIVSSKISISKLLKLRQSLNATANDKY--KLSINDLLVKAITVAAKRVPD 324
Cdd:PLN02226 236 ------RVPMTRLRKRVATRLKDSQNTFALLTTFNEVDMTNLMKLRSQYKDAFYEKHgvKLGLMSGFIKAAVSALQHQPV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 325 ANAYWLPNENVIRKFknVDVSVAVATPTGLLTPIVKNCEAKGLSQISNEIKELVKRARINKLAPEEFQGGTICISNMGMN 404
Cdd:PLN02226 310 VNAVIDGDDIIYRDY--VDISIAVGTSKGLVVPVIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVY 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398365063 405 NAVnMFTSIINPPQSTILAI-ATVERVAVEDAAAENgfsfDNQVTITGTFDHRTIDGAKGAEFMKELKTVIENPLEMLL 482
Cdd:PLN02226 388 GSL-ISTPIINPPQSAILGMhSIVSRPMVVGGSVVP----RPMMYVALTYDHRLIDGREAVYFLRRVKDVVEDPQRLLL 461
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
173-481 |
1.06e-27 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 112.58 E-value: 1.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 173 RIFASPLAKTIALEKGISLKDVHGTGPRGRITKADIESYLEKSSKQSSQTSGAAAATPAAATSSTTAGSAPSPSSTASYe 252
Cdd:PRK11857 1 KILATPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIKSLKSAPTPAEAASVSSAQQAAKTAAPAAAPPKLEGKRE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 253 dvPISTMRSIIGERLLQSTQGIPSYIVSSKISISKLLKLRQSL--NATANDKYKLSINDLLVKAITVAAKRVPDANAYWL 330
Cdd:PRK11857 80 --KVAPIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVkdPVLKTEGVKLTFLPFIAKAILIALKEFPIFAAKYD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 331 PNENVIRKFKNVDVSVAVATPTGLLTPIVKNCEAKGLSQISNEIKELVKRARINKLAPEEFQGGTICISNMGMNNAVnMF 410
Cdd:PRK11857 158 EATSELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSL-YG 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398365063 411 TSIINPPQSTILAI-ATVERVAVEDAAAENGfsfdNQVTITGTFDHRTIDGAKGAEFMKELKTVIENPlEML 481
Cdd:PRK11857 237 VPVINYPELAIAGVgAIIDKAIVKNGQIVAG----KVMHLTVAADHRWIDGATIGRFASRVKELLEKP-EIL 303
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
35-108 |
3.01e-25 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 98.63 E-value: 3.01e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398365063 35 TIIGMPALSPTMTQGNLAAWTKKEGDQLSPGEVIAEIETDKAQMDFEFQEDGYLAKILVPEGTKdIPVNKPIAV 108
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAV 73
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
35-108 |
2.10e-20 |
|
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440274 [Multi-domain] Cd Length: 77 Bit Score: 85.12 E-value: 2.10e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398365063 35 TIIGMPALSPTMTQGNLAAWTKKEGDQLSPGEVIAEIETDKAQMDFEFQEDGYLAKILVPEGTKdIPVNKPIAV 108
Cdd:COG0508 3 IEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDT-VPVGAVIAV 75
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
35-117 |
4.13e-16 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 79.60 E-value: 4.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 35 TIIGMPALSPTMTQGNLAAWTKKEGDQLSPGEVIAEIETDKAQMDFEFQEDGYLAKILVPEGTkDIPVNKPIAVyVEDkA 114
Cdd:PRK14875 3 TPITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGE-TLPVGALLAV-VAD-A 79
|
...
gi 398365063 115 DVP 117
Cdd:PRK14875 80 EVS 82
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
36-98 |
1.51e-14 |
|
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases, and the H-protein of the glycine cleavage system (GCS). These domains transport CO2, acyl, or methylamine, respectively, between components of the complex/protein via a biotinyl or lipoyl group, which is covalently attached to a highly conserved lysine residue.
Pssm-ID: 133456 [Multi-domain] Cd Length: 73 Bit Score: 68.24 E-value: 1.51e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398365063 36 IIGMPALSPTMTQGNLAAWTKKEGDQLSPGEVIAEIETDKAQMDFEFQEDGYLAKILVPEGTK 98
Cdd:cd06663 1 TILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTK 63
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
174-209 |
2.11e-14 |
|
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid dehydrogenases responsible for the binding of the E3 subunit.
Pssm-ID: 460710 [Multi-domain] Cd Length: 36 Bit Score: 66.94 E-value: 2.11e-14
10 20 30
....*....|....*....|....*....|....*.
gi 398365063 174 IFASPLAKTIALEKGISLKDVHGTGPRGRITKADIE 209
Cdd:pfam02817 1 VLASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
304-468 |
4.50e-14 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 74.93 E-value: 4.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 304 KLSINDLLVKAITVAAKRVPDANAYWL-----PNEnVIRKFKNVDVSVAVATPTG---LLTPIVKNCEAKGLSQISNEIK 375
Cdd:PRK12270 169 KVSFTHLIGYALVQALKAFPNMNRHYAevdgkPTL-VTPAHVNLGLAIDLPKKDGsrqLVVPAIKGAETMDFAQFWAAYE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365063 376 ELVKRARINKLAPEEFQGGTICISNMGMNNAVNmftSI--INPPQSTILAIATVE-----RVAVEDAAAENGFSfdNQVT 448
Cdd:PRK12270 248 DIVRRARDGKLTADDFQGTTISLTNPGGIGTVH---SVprLMKGQGAIIGVGAMEypaefQGASEERLAELGIS--KVMT 322
|
170 180
....*....|....*....|
gi 398365063 449 ITGTFDHRTIDGAKGAEFMK 468
Cdd:PRK12270 323 LTSTYDHRIIQGAESGEFLR 342
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
37-108 |
2.05e-13 |
|
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.
Pssm-ID: 395290 [Multi-domain] Cd Length: 73 Bit Score: 65.31 E-value: 2.05e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398365063 37 IGMPALSPTMTQGnLAAWTKKEGDQLSPGEVIAEIETDKAQMDFEFQEDGYLAKILVPEGTKdIPVNKPIAV 108
Cdd:pfam00364 3 IKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDT-VEVGDPLAK 72
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
48-96 |
1.31e-03 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 37.01 E-value: 1.31e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 398365063 48 QGNLAAWTKKEGDQLSPGEVIAEIETDKAQMDFEFQEDGYLAKILVPEG 96
Cdd:cd06850 7 PGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEG 55
|
|
| |
