|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
1-299 |
3.53e-91 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 277.06 E-value: 3.53e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704423962 1 QPARGGRGVATPLARRLAREAGLDLAQVSGSGPGGRIKAADVRQAPRAPEAAPAVSPdtaapAPAARAPLAPAAGEQRIE 80
Cdd:PRK11856 118 AAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEAAAAAAAPAAAAAA-----AAAAAPPAAAAEGEERVP 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704423962 81 ASALVQSMARRMTQAKQ-VPHFYLSAEAEVSALLALRQRLNAQAdaPRLTLNHFVIAAVARALAAMPHQNRIWNDDHIVQ 159
Cdd:PRK11856 193 LSGMRKAIAKRMVESKReIPHFTLTDEVDVTALLALRKQLKAIG--VKLTVTDFLIKAVALALKKFPELNASWDDDAIVL 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704423962 160 FQGIDVGVAVSTERGLMAPVLHGLDHASLDDIAAQSDALLGRVRAGKATREDMSGGAISISNAGMFNVTYMAPIINPPQS 239
Cdd:PRK11856 271 KKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEV 350
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 704423962 240 AILGVGSIRElfRP-DEQGAPALRREMGLVLAADHRLHDGASALAFLNHVIDLLQDPYRLL 299
Cdd:PRK11856 351 AILGVGAIVE--RPvVVDGEIVVRKVMPLSLSFDHRVIDGADAARFLKALKELLENPALLL 409
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
92-299 |
7.19e-69 |
|
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: 213.17 E-value: 7.19e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704423962 92 MTQAKQ-VPHFYLSAEAEVSALLALRQRLNAQA--DAPRLTLNHFVIAAVARALAAMPHQNRIWNDDH--IVQFQGIDVG 166
Cdd:pfam00198 1 MTESKQtIPHFTLTDEVDVTELLALREELKEDAadEETKLTFLPFLVKAVALALKKFPELNASWDGEEgeIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704423962 167 VAVSTERGLMAPVLHGLDHASLDDIAAQSDALLGRVRAGKATREDMSGGAISISNAGMFNVTYMAPIINPPQSAILGVGS 246
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 704423962 247 IRElfRP-DEQGAPALRREMGLVLAADHRLHDGASALAFLNHVIDLLQDPYRLL 299
Cdd:pfam00198 161 IRK--RPvVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
3-299 |
1.16e-66 |
|
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: 214.66 E-value: 1.16e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704423962 3 ARGGRGVATPLARRLAREAGLDLAQVSGSGPGGRIKAADVRQAPRAPEAAPAVSPDTAAPAPAARAPLAPAAGEQRIEAS 82
Cdd:TIGR01349 135 ESGDRIFASPLAKKLAKEKGIDLSAVAGSGPNGRIVKKDIESFVPQSPASANQQAAATTPATYPAAAPVSTGSYEDVPLS 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704423962 83 ALVQSMARRMTQAKQ-VPHFYLSAEAEVSALLALRQRLNAQADAP-RLTLNHFVIAAVARALAAMPHQNRIWNDDHIVQF 160
Cdd:TIGR01349 215 NIRKIIAKRLLESKQtIPHYYVSIECNVDKLLALRKELNAMASEVyKLSVNDFIIKASALALREVPEANSSWTDNFIRRY 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704423962 161 QGIDVGVAVSTERGLMAPVLHGLDHASLDDIAAQSDALLGRVRAGKATREDMSGGAISISNAGMFNVTYMAPIINPPQSA 240
Cdd:TIGR01349 295 KNVDISVAVATPDGLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQAC 374
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 704423962 241 ILGVGSI--RELFRPDEQGAPALRREMGLVLAADHRLHDGASALAFLNHVIDLLQDPYRLL 299
Cdd:TIGR01349 375 ILAVGAVedVAVVDNDEEKGFAVASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEML 435
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
1-299 |
3.53e-91 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 277.06 E-value: 3.53e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704423962 1 QPARGGRGVATPLARRLAREAGLDLAQVSGSGPGGRIKAADVRQAPRAPEAAPAVSPdtaapAPAARAPLAPAAGEQRIE 80
Cdd:PRK11856 118 AAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEAAAAAAAPAAAAAA-----AAAAAPPAAAAEGEERVP 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704423962 81 ASALVQSMARRMTQAKQ-VPHFYLSAEAEVSALLALRQRLNAQAdaPRLTLNHFVIAAVARALAAMPHQNRIWNDDHIVQ 159
Cdd:PRK11856 193 LSGMRKAIAKRMVESKReIPHFTLTDEVDVTALLALRKQLKAIG--VKLTVTDFLIKAVALALKKFPELNASWDDDAIVL 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704423962 160 FQGIDVGVAVSTERGLMAPVLHGLDHASLDDIAAQSDALLGRVRAGKATREDMSGGAISISNAGMFNVTYMAPIINPPQS 239
Cdd:PRK11856 271 KKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEV 350
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 704423962 240 AILGVGSIRElfRP-DEQGAPALRREMGLVLAADHRLHDGASALAFLNHVIDLLQDPYRLL 299
Cdd:PRK11856 351 AILGVGAIVE--RPvVVDGEIVVRKVMPLSLSFDHRVIDGADAARFLKALKELLENPALLL 409
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
92-299 |
7.19e-69 |
|
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: 213.17 E-value: 7.19e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704423962 92 MTQAKQ-VPHFYLSAEAEVSALLALRQRLNAQA--DAPRLTLNHFVIAAVARALAAMPHQNRIWNDDH--IVQFQGIDVG 166
Cdd:pfam00198 1 MTESKQtIPHFTLTDEVDVTELLALREELKEDAadEETKLTFLPFLVKAVALALKKFPELNASWDGEEgeIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704423962 167 VAVSTERGLMAPVLHGLDHASLDDIAAQSDALLGRVRAGKATREDMSGGAISISNAGMFNVTYMAPIINPPQSAILGVGS 246
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 704423962 247 IRElfRP-DEQGAPALRREMGLVLAADHRLHDGASALAFLNHVIDLLQDPYRLL 299
Cdd:pfam00198 161 IRK--RPvVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
3-299 |
1.16e-66 |
|
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: 214.66 E-value: 1.16e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704423962 3 ARGGRGVATPLARRLAREAGLDLAQVSGSGPGGRIKAADVRQAPRAPEAAPAVSPDTAAPAPAARAPLAPAAGEQRIEAS 82
Cdd:TIGR01349 135 ESGDRIFASPLAKKLAKEKGIDLSAVAGSGPNGRIVKKDIESFVPQSPASANQQAAATTPATYPAAAPVSTGSYEDVPLS 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704423962 83 ALVQSMARRMTQAKQ-VPHFYLSAEAEVSALLALRQRLNAQADAP-RLTLNHFVIAAVARALAAMPHQNRIWNDDHIVQF 160
Cdd:TIGR01349 215 NIRKIIAKRLLESKQtIPHYYVSIECNVDKLLALRKELNAMASEVyKLSVNDFIIKASALALREVPEANSSWTDNFIRRY 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704423962 161 QGIDVGVAVSTERGLMAPVLHGLDHASLDDIAAQSDALLGRVRAGKATREDMSGGAISISNAGMFNVTYMAPIINPPQSA 240
Cdd:TIGR01349 295 KNVDISVAVATPDGLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQAC 374
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 704423962 241 ILGVGSI--RELFRPDEQGAPALRREMGLVLAADHRLHDGASALAFLNHVIDLLQDPYRLL 299
Cdd:TIGR01349 375 ILAVGAVedVAVVDNDEEKGFAVASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEML 435
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
2-299 |
7.40e-52 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 178.48 E-value: 7.40e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704423962 2 PARGGRGVATPLARRLAREAGLDLAQVSGSGPGGRIKAADVR-------QAPRAPEAAPAVSPDTAAPAPAARAPLAPAA 74
Cdd:PRK11855 237 AAPGKAPHASPAVRRLARELGVDLSQVKGTGKKGRITKEDVQafvkgamSAAAAAAAAAAAAGGGGLGLLPWPKVDFSKF 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704423962 75 GE-QRIEASALVQSMARRMTQAKQ-VPHFYLSAEAEVSALLALRQRLNAQA--DAPRLTLNHFVIAAVARALAAMPHQNR 150
Cdd:PRK11855 317 GEiETKPLSRIKKISAANLHRSWVtIPHVTQFDEADITDLEALRKQLKKEAekAGVKLTMLPFFIKAVVAALKEFPVFNA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704423962 151 IWNDD--HIVQFQGIDVGVAVSTERGLMAPVLHGLDHASLDDIAAQSDALLGRVRAGKATREDMSGGAISISNAGMFNVT 228
Cdd:PRK11855 397 SLDEDgdELTYKKYFNIGFAVDTPNGLVVPVIKDVDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGT 476
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 704423962 229 YMAPIINPPQSAILGVGSIREL-FRPDEQGAPalRREMGLVLAADHRLHDGASALAFLNHVIDLLQDPYRLL 299
Cdd:PRK11855 477 AFTPIINAPEVAILGVGKSQMKpVWDGKEFVP--RLMLPLSLSYDHRVIDGATAARFTNYLKQLLADPRRML 546
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
1-299 |
5.93e-49 |
|
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: 167.60 E-value: 5.93e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704423962 1 QPARGGRGVATPLARRLAREAGLDLAQVSGSGPGGRIKAADVrqaprAPEAAPAVSPDTAAPAPAARAPLAPAAGEQRIE 80
Cdd:TIGR01347 104 PTAAANRPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDI-----IKKTEAPASAQPPAAAAAAAAPAAATRPEERVK 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704423962 81 ASALVQSMARRMTQAKQvphfylSA-------EAEVSALLALRQRLNAQ---ADAPRLTLNHFVIAAVARALAAMPHQNR 150
Cdd:TIGR01347 179 MTRLRQRIAERLKEAQN------STamlttfnEVDMSAVMELRKRYKEEfekKHGVKLGFMSFFVKAVVAALKRFPEVNA 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704423962 151 IWNDDHIVQFQGIDVGVAVSTERGLMAPVLHGLDHASLDDIAAQSDALLGRVRAGKATREDMSGGAISISNAGMFNVTYM 230
Cdd:TIGR01347 253 EIDGDDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMS 332
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704423962 231 APIINPPQSAILGVGSIRElfRP-DEQGAPALRREMGLVLAADHRLHDGASALAFLNHVIDLLQDPYRLL 299
Cdd:TIGR01347 333 TPIINPPQSAILGMHGIKE--RPvAVNGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRRLL 400
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
2-299 |
3.10e-48 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 168.88 E-value: 3.10e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704423962 2 PARGGRGVATPLARRLAREAGLDLAQVSGSGPGGRIKAADVRQAPRAPEAAPAVSPDTAAPAPAARAPLAPAAGEQRIEA 81
Cdd:PLN02744 243 PSSGDRIFASPLARKLAEDNNVPLSSIKGTGPDGRIVKADIEDYLASGGKGATAPPSTDSKAPALDYTDIPNTQIRKVTA 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704423962 82 SALVQSmarrmtqaKQ-VPHFYLSAEAEVSALLALRQRLNAQADAP---RLTLNHFVIAAVARALAAMPHQNRIWNDDHI 157
Cdd:PLN02744 323 SRLLQS--------KQtIPHYYLTVDTRVDKLMALRSQLNSLQEASggkKISVNDLVIKAAALALRKVPQCNSSWTDDYI 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704423962 158 VQFQGIDVGVAVSTERGLMAPVLHGLDHASLDDIAAQSDALLGRVRAGKATREDMSGGAISISN-AGMFNVTYMAPIINP 236
Cdd:PLN02744 395 RQYHNVNINVAVQTENGLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNlGGPFGIKQFCAIINP 474
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 704423962 237 PQSAILGVGSIRELFRPDE-QGAPALRREMGLVLAADHRLHDGASALAFLNHVIDLLQDPYRLL 299
Cdd:PLN02744 475 PQSAILAVGSAEKRVIPGSgPDQYNFASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESML 538
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
7-299 |
6.28e-47 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 162.97 E-value: 6.28e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704423962 7 RGV-ATPLARRLAREAGLDLAQVSGSGPGGRIKAADVRQAPRA-------PEAAPAVSPDTAAPAPAARAPLAPAAGEQR 78
Cdd:PLN02528 108 SGVlSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAAQkgvvkdsSSAEEATIAEQEEFSTSVSTPTEQSYEDKT 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704423962 79 IEASALVQSMARRMTQAKQVPHFYLSAEAEVSALLALRQRL-NAQADA-PRLTLNHFVIAAVARALAAMPHQNRIWNDDH 156
Cdd:PLN02528 188 IPLRGFQRAMVKTMTAAAKVPHFHYVEEINVDALVELKASFqENNTDPtVKHTFLPFLIKSLSMALSKYPLLNSCFNEET 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704423962 157 I-VQFQGI-DVGVAVSTERGLMAPVLHGLDHASLDDIAAQSDALLGRVRAGKATREDMSGGAISISNAGMFNVTYMAPII 234
Cdd:PLN02528 268 SeIRLKGShNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVL 347
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 704423962 235 NPPQSAILGVGSIRELFRPDEQGAPALRREMGLVLAADHRLHDGASALAFLNHVIDLLQDPYRLL 299
Cdd:PLN02528 348 NLPEVAIIALGRIQKVPRFVDDGNVYPASIMTVTIGADHRVLDGATVARFCNEWKSYVEKPELLM 412
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
10-299 |
3.22e-42 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 149.98 E-value: 3.22e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704423962 10 ATPLARRLAREAGLDLAQVSGSGPGGRIKAADVrqaPRAPEAAPAVSPDTAAPAPAARAPLAPAAGEQRIEASALVQSMA 89
Cdd:PRK05704 115 LSPAARKLAAENGLDASAVKGTGKGGRVTKEDV---LAALAAAAAAPAAPAAAAPAAAPAPLGARPEERVPMTRLRKTIA 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704423962 90 RRMTQAKQVphfylSA------EAEVSALLALRQRLNAQ---ADAPRLTLNHFVIAAVARALAAMPHQNRIWNDDHIVQF 160
Cdd:PRK05704 192 ERLLEAQNT-----TAmlttfnEVDMTPVMDLRKQYKDAfekKHGVKLGFMSFFVKAVVEALKRYPEVNASIDGDDIVYH 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704423962 161 QGIDVGVAVSTERGLMAPVLHGLDHASLDDIAAQSDALLGRVRAGKATREDMSGGAISISNAGMFNVTYMAPIINPPQSA 240
Cdd:PRK05704 267 NYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELAKKARDGKLSIEELTGGTFTITNGGVFGSLMSTPIINPPQSA 346
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 704423962 241 ILGVGSIRElfRP-DEQGAPALRREMGLVLAADHRLHDGASALAFLNHVIDLLQDPYRLL 299
Cdd:PRK05704 347 ILGMHKIKE--RPvAVNGQIVIRPMMYLALSYDHRIIDGKEAVGFLVTIKELLEDPERLL 404
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
10-299 |
7.27e-40 |
|
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: 146.17 E-value: 7.27e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704423962 10 ATPLARRLAREAGLDLAQVSGSGPGGRIKAADVRQAPRAPEAAPAVSPDTAAPAPAARAPLAPAA----GE-QRIEASAL 84
Cdd:TIGR01348 247 AAPAVRRLAREFGVDLSAVKGTGIKGRILREDVQRFVKEPSVRAQAAAASAAGGAPGALPWPNVDfskfGEvEEVDMSRI 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704423962 85 VQSMARRMTQA-KQVPHFYLSAEAEVSALLALRQRLNAQADAP--RLTLNHFVIAAVARALAAMPHQNRIWNDD--HIVQ 159
Cdd:TIGR01348 327 RKISGANLTRNwTMIPHVTHFDKADITEMEAFRKQQNAAVEKEgvKLTVLHILMKAVAAALKKFPKFNASLDLGgeQLIL 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704423962 160 FQGIDVGVAVSTERGLMAPVLHGLDHASLDDIAAQSDALLGRVRAGKATREDMSGGAISISNAGMFNVTYMAPIINPPQS 239
Cdd:TIGR01348 407 KKYVNIGVAVDTPNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEV 486
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 704423962 240 AILGVGsiRELFRP---DEQGAPalRREMGLVLAADHRLHDGASALAFLNHVIDLLQDPYRLL 299
Cdd:TIGR01348 487 AILGVS--KSGMEPvwnGKEFEP--RLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRLL 545
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
10-299 |
1.51e-36 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 137.83 E-value: 1.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704423962 10 ATPLARRLAREAGLDLAQVSGSGPGGRIKAADVRQAPRAPEAAPAVSPDTAAPAPAARAPLA------PAAGE------- 76
Cdd:PRK11854 330 ATPLVRRLAREFGVNLAKVKGTGRKGRILKEDVQAYVKDAVKRAEAAPAAAAAGGGGPGLLPwpkvdfSKFGEieevelg 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704423962 77 --QRIEASALVqsmaRRMTQAKQVPHFYlsaEAEVSALLALRQRLNAQADAPRLTLN----HFVIAAVARALAAMPHQNR 150
Cdd:PRK11854 410 riQKISGANLH----RNWVMIPHVTQFD---KADITELEAFRKQQNAEAEKRKLGVKitplVFIMKAVAAALEQMPRFNS 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704423962 151 IWNDD--HIVQFQGIDVGVAVSTERGLMAPVLHGLDHASLDDIAAQSDALLGRVRAGKATREDMSGGAISISNAGMFNVT 228
Cdd:PRK11854 483 SLSEDgqRLTLKKYVNIGIAVDTPNGLVVPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTT 562
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 704423962 229 YMAPIINPPQSAILGVGSIRelFRPDEQG-APALRREMGLVLAADHRLHDGASALAFLNHVIDLLQDPYRLL 299
Cdd:PRK11854 563 HFTPIVNAPEVAILGVSKSA--MEPVWNGkEFAPRLMLPLSLSYDHRVIDGADGARFITIINDRLSDIRRLV 632
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
76-299 |
9.08e-35 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 130.57 E-value: 9.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704423962 76 EQRIEASALVQSMARRMTQAKQ----VPHFylsAEAEVSALLALRQRLNAQ---ADAPRLTLNHFVIAAVARALAAMPHQ 148
Cdd:PTZ00144 189 ETRVPMSRMRQRIAERLKASQNtcamLTTF---NECDMSALMELRKEYKDDfqkKHGVKLGFMSAFVKASTIALKKMPIV 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704423962 149 NRIWNDDHIVQFQGIDVGVAVSTERGLMAPVLHGLDHASLDDIAAQSDALLGRVRAGKATREDMSGGAISISNAGMFNVT 228
Cdd:PTZ00144 266 NAYIDGDEIVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISNGGVFGSL 345
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 704423962 229 YMAPIINPPQSAILGVGSI--RELFRPDEQgapALRREMGLVLAADHRLHDGASALAFLNHVIDLLQDPYRLL 299
Cdd:PTZ00144 346 MGTPIINPPQSAILGMHAIkkRPVVVGNEI---VIRPIMYLALTYDHRLIDGRDAVTFLKKIKDLIEDPARML 415
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
11-299 |
1.34e-33 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 125.79 E-value: 1.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704423962 11 TPLARRLAREAGLDLAQVSGSGPGGRIKAADVRQAPRAPEAAPAVSPDTAAPAPAARAPLAPAAGE-QRIEASALVQSMA 89
Cdd:PRK14843 52 SPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALLPENIENDSIKSPAQIEKVEEVPDNVTPYGEiERIPMTPMRKVIA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704423962 90 RRMTQAK-QVPHFYLSAEAEVSALLALRQRL---NAQADAPRLTLNHFVIAAVARALAAMPHQNRIWNDD--HIVQFQGI 163
Cdd:PRK14843 132 QRMVESYlTAPTFTLNYEVDMTEMLALRKKVlepIMEATGKKTTVTDLLSLAVVKTLMKHPYINASLTEDgkTIITHNYV 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704423962 164 DVGVAVSTERGLMAPVLHGLDHASLDDIAAQSDALLGRVRAGKATREDMSGGAISISNAGMFNVTYMAPIINPPQSAILG 243
Cdd:PRK14843 212 NLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQPNSAILG 291
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 704423962 244 VGSIRElfRPDE-QGAPALRREMGLVLAADHRLHDGASALAFLNHVIDLLQDPYRLL 299
Cdd:PRK14843 292 VSSTIE--KPVVvNGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISML 346
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
10-295 |
5.12e-32 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 120.67 E-value: 5.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704423962 10 ATPLARRLAREAGLDLAQVSGSGPGGRIKAADVR------QAPRAPEAAPAVSPDTAAPAPAARAPLAPAAGEQRIEASA 83
Cdd:PRK11857 4 ATPIARALAKKLGIDISLLKGSGRDGKILAEDVEnfikslKSAPTPAEAASVSSAQQAAKTAAPAAAPPKLEGKREKVAP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704423962 84 LVQSMARRMTQA-KQVPHFYLSAEAEVSALLALRQRLN---AQADAPRLTLNHFVIAAVARALAAMPHQNRIWND--DHI 157
Cdd:PRK11857 84 IRKAIARAMTNSwSNVAYVNLVNEIDMTKLWDLRKSVKdpvLKTEGVKLTFLPFIAKAILIALKEFPIFAAKYDEatSEL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704423962 158 VQFQGIDVGVAVSTERGLMAPVLHGLDHASLDDIAAQSDALLGRVRAGKATREDMSGGAISISNAGMFNVTYMAPIINPP 237
Cdd:PRK11857 164 VYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLYGVPVINYP 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 704423962 238 QSAILGVGSIRELFRPdEQGAPALRREMGLVLAADHRLHDGASALAFLNHVIDLLQDP 295
Cdd:PRK11857 244 ELAIAGVGAIIDKAIV-KNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEKP 300
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
76-299 |
7.66e-28 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 112.16 E-value: 7.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704423962 76 EQRIEASALVQSMARRMTQAKQVPHFYLS-AEAEVSALLALRQRLN---AQADAPRLTLNHFVIAAVARALAAMPHQNRI 151
Cdd:PLN02226 234 ERRVPMTRLRKRVATRLKDSQNTFALLTTfNEVDMTNLMKLRSQYKdafYEKHGVKLGLMSGFIKAAVSALQHQPVVNAV 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704423962 152 WNDDHIVQFQGIDVGVAVSTERGLMAPVLHGLDHASLDDIAAQSDALLGRVRAGKATREDMSGGAISISNAGMFNVTYMA 231
Cdd:PLN02226 314 IDGDDIIYRDYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLIST 393
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 704423962 232 PIINPPQSAILGVGSIRElfRPDEQGAPALRREMGLV-LAADHRLHDGASALAFLNHVIDLLQDPYRLL 299
Cdd:PLN02226 394 PIINPPQSAILGMHSIVS--RPMVVGGSVVPRPMMYVaLTYDHRLIDGREAVYFLRRVKDVVEDPQRLL 460
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
10-43 |
2.25e-13 |
|
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: 63.09 E-value: 2.25e-13
10 20 30
....*....|....*....|....*....|....
gi 704423962 10 ATPLARRLAREAGLDLAQVSGSGPGGRIKAADVR 43
Cdd:pfam02817 3 ASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
156-293 |
5.53e-10 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 60.29 E-value: 5.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704423962 156 HIVQFQGIDVGVAVSTE-----RGLMAPVLHGLDHASLDDIAAQSDALLGRVRAGKATREDMSGGAISISNAGMFNVTYM 230
Cdd:PRK12270 202 TLVTPAHVNLGLAIDLPkkdgsRQLVVPAIKGAETMDFAQFWAAYEDIVRRARDGKLTADDFQGTTISLTNPGGIGTVHS 281
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704423962 231 APIINPPQSAILGVGSIRelFRPDEQGAPALRR-EMG------LVLAADHRLHDGASALAFLNHVIDLLQ 293
Cdd:PRK12270 282 VPRLMKGQGAIIGVGAME--YPAEFQGASEERLaELGiskvmtLTSTYDHRIIQGAESGEFLRTIHQLLL 349
|
|
| |
