|
Name |
Accession |
Description |
Interval |
E-value |
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
59-472 |
3.38e-154 |
|
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: 445.78 E-value: 3.38e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 59 VVGMPALSPTMNQGNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSKDVQVGQPIAVTVEDLED 138
Cdd:TIGR01349 1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 139 I----KNIPADASFGGEQKEQSIASEAQkvETDAAKESSII------------------TRI--SPAAKLLIKEHRLDQS 194
Cdd:TIGR01349 81 VadafKNYKLESSASPAPKPSEIAPTAP--PSAPKPSPAPQkqspepsspaplsdkesgDRIfaSPLAKKLAKEKGIDLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 195 VLNASGPRGTLLKGDVLAAL--KLGASSSSTKQKNAPAAPssqpthdfqaqsVTIPQQNDAYEDIPNSQIRKVIAKRLLE 272
Cdd:TIGR01349 159 AVAGSGPNGRIVKKDIESFVpqSPASANQQAAATTPATYP------------AAAPVSTGSYEDVPLSNIRKIIAKRLLE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 273 SKQTTPHLYLSQDVILDPLLAFRNELKEQHG--VKVSVNDIVIKAVALALRNVPEANAYWNNDKEQAQKcvSVDISIAVA 350
Cdd:TIGR01349 227 SKQTIPHYYVSIECNVDKLLALRKELNAMASevYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYK--NVDISVAVA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 351 TEKGLMTPIIRNADQKTISAISSEVKQLAEKARAGKLAPNEFQGGTFSISNLGMYPVDHFCAIINPPQSGILAVGRGNKI 430
Cdd:TIGR01349 305 TPDGLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDV 384
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1002278355 431 iePVVDSDGTEKATVVTKMSLTLSADHRVFDGQVGGKFFTEL 472
Cdd:TIGR01349 385 --AVVDNDEEKGFAVASIMSVTLSCDHRVIDGAVGAEFLKSF 424
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
50-468 |
9.34e-140 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 412.71 E-value: 9.34e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 50 SSTGFPPHLVVGMPALSPTMNQGNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSKDVQVGQPI 129
Cdd:PLN02744 105 SSSDLPPHQEIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKEIKVGEVI 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 130 AVTVEDLEDI---KNIPADASFGG---------------EQKEQSIASEAQKVETDAAKESSIITRISPAAKLLIKEHRL 191
Cdd:PLN02744 185 AITVEEEEDIgkfKDYKPSSSAAPaapkakpsppppkeeEVEKPASSPEPKASKPSAPPSSGDRIFASPLARKLAEDNNV 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 192 DQSVLNASGPRGTLLKGDVLAALKLGASSSSTKQKNAPAAPSSqpthdfqaqsvtipqqndAYEDIPNSQIRKVIAKRLL 271
Cdd:PLN02744 265 PLSSIKGTGPDGRIVKADIEDYLASGGKGATAPPSTDSKAPAL------------------DYTDIPNTQIRKVTASRLL 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 272 ESKQTTPHLYLSQDVILDPLLAFRNEL----KEQHGVKVSVNDIVIKAVALALRNVPEANAYWNNDKEQAQKcvSVDISI 347
Cdd:PLN02744 327 QSKQTIPHYYLTVDTRVDKLMALRSQLnslqEASGGKKISVNDLVIKAAALALRKVPQCNSSWTDDYIRQYH--NVNINV 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 348 AVATEKGLMTPIIRNADQKTISAISSEVKQLAEKARAGKLAPNEFQGGTFSISNL-GMYPVDHFCAIINPPQSGILAVGR 426
Cdd:PLN02744 405 AVQTENGLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLgGPFGIKQFCAIINPPQSAILAVGS 484
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1002278355 427 GNKiiePVVDSDGTEKATVVTKMSLTLSADHRVFDGQVGGKF 468
Cdd:PLN02744 485 AEK---RVIPGSGPDQYNFASFMSVTLSCDHRVIDGAIGAEW 523
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
270-472 |
8.05e-84 |
|
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: 257.47 E-value: 8.05e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 270 LLESKQTTPHLYLSQDVILDPLLAFRNELKEQH---GVKVSVNDIVIKAVALALRNVPEANAYWNNDKEQAQKCVSVDIS 346
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAadeETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 347 IAVATEKGLMTPIIRNADQKTISAISSEVKQLAEKARAGKLAPNEFQGGTFSISNLGMYPVDHFCAIINPPQSGILAVGR 426
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1002278355 427 GNKiiEPVVDSDGTEKATVvtkMSLTLSADHRVFDGQVGGKFFTEL 472
Cdd:pfam00198 161 IRK--RPVVVDGEIVVRKV---MPLSLSFDHRVIDGAEAARFLNTL 201
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
62-131 |
1.27e-27 |
|
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: 105.18 E-value: 1.27e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 62 MPALSPTMNQGNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSKdVQVGQPIAV 131
Cdd:cd06849 5 MPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAV 73
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
62-131 |
2.85e-25 |
|
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: 98.60 E-value: 2.85e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 62 MPALSPTMNQGNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSKdVQVGQPIAV 131
Cdd:COG0508 7 MPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDT-VPVGAVIAV 75
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
59-472 |
3.38e-154 |
|
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: 445.78 E-value: 3.38e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 59 VVGMPALSPTMNQGNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSKDVQVGQPIAVTVEDLED 138
Cdd:TIGR01349 1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 139 I----KNIPADASFGGEQKEQSIASEAQkvETDAAKESSII------------------TRI--SPAAKLLIKEHRLDQS 194
Cdd:TIGR01349 81 VadafKNYKLESSASPAPKPSEIAPTAP--PSAPKPSPAPQkqspepsspaplsdkesgDRIfaSPLAKKLAKEKGIDLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 195 VLNASGPRGTLLKGDVLAAL--KLGASSSSTKQKNAPAAPssqpthdfqaqsVTIPQQNDAYEDIPNSQIRKVIAKRLLE 272
Cdd:TIGR01349 159 AVAGSGPNGRIVKKDIESFVpqSPASANQQAAATTPATYP------------AAAPVSTGSYEDVPLSNIRKIIAKRLLE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 273 SKQTTPHLYLSQDVILDPLLAFRNELKEQHG--VKVSVNDIVIKAVALALRNVPEANAYWNNDKEQAQKcvSVDISIAVA 350
Cdd:TIGR01349 227 SKQTIPHYYVSIECNVDKLLALRKELNAMASevYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYK--NVDISVAVA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 351 TEKGLMTPIIRNADQKTISAISSEVKQLAEKARAGKLAPNEFQGGTFSISNLGMYPVDHFCAIINPPQSGILAVGRGNKI 430
Cdd:TIGR01349 305 TPDGLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDV 384
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1002278355 431 iePVVDSDGTEKATVVTKMSLTLSADHRVFDGQVGGKFFTEL 472
Cdd:TIGR01349 385 --AVVDNDEEKGFAVASIMSVTLSCDHRVIDGAVGAEFLKSF 424
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
50-468 |
9.34e-140 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 412.71 E-value: 9.34e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 50 SSTGFPPHLVVGMPALSPTMNQGNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSKDVQVGQPI 129
Cdd:PLN02744 105 SSSDLPPHQEIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKEIKVGEVI 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 130 AVTVEDLEDI---KNIPADASFGG---------------EQKEQSIASEAQKVETDAAKESSIITRISPAAKLLIKEHRL 191
Cdd:PLN02744 185 AITVEEEEDIgkfKDYKPSSSAAPaapkakpsppppkeeEVEKPASSPEPKASKPSAPPSSGDRIFASPLARKLAEDNNV 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 192 DQSVLNASGPRGTLLKGDVLAALKLGASSSSTKQKNAPAAPSSqpthdfqaqsvtipqqndAYEDIPNSQIRKVIAKRLL 271
Cdd:PLN02744 265 PLSSIKGTGPDGRIVKADIEDYLASGGKGATAPPSTDSKAPAL------------------DYTDIPNTQIRKVTASRLL 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 272 ESKQTTPHLYLSQDVILDPLLAFRNEL----KEQHGVKVSVNDIVIKAVALALRNVPEANAYWNNDKEQAQKcvSVDISI 347
Cdd:PLN02744 327 QSKQTIPHYYLTVDTRVDKLMALRSQLnslqEASGGKKISVNDLVIKAAALALRKVPQCNSSWTDDYIRQYH--NVNINV 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 348 AVATEKGLMTPIIRNADQKTISAISSEVKQLAEKARAGKLAPNEFQGGTFSISNL-GMYPVDHFCAIINPPQSGILAVGR 426
Cdd:PLN02744 405 AVQTENGLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLgGPFGIKQFCAIINPPQSAILAVGS 484
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1002278355 427 GNKiiePVVDSDGTEKATVVTKMSLTLSADHRVFDGQVGGKF 468
Cdd:PLN02744 485 AEK---RVIPGSGPDQYNFASFMSVTLSCDHRVIDGAIGAEW 523
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
62-472 |
3.89e-137 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 401.09 E-value: 3.89e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 62 MPALSPTMNQGNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSKdVQVGQPIAvTVEDLEDIKN 141
Cdd:PRK11856 7 MPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDV-VPVGSVIA-VIEEEGEAEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 142 IPADASFGGEQKEQSIASEAQKVETDAA------KESSIITRISPAAKLLIKEHRLDQSVLNASGPRGTLLKGDVLAALK 215
Cdd:PRK11856 85 AAAAEAAPEAPAPEPAPAAAAAAAAAPAaaaapaAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEAAAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 216 LGASSSSTKQKNAPAAPSSQPthdfqaqsvtipqqnDAYEDIPNSQIRKVIAKRLLESKQTTPHLYLSQDVILDPLLAFR 295
Cdd:PRK11856 165 AAAPAAAAAAAAAAAPPAAAA---------------EGEERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLALR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 296 NELKEQhGVKVSVNDIVIKAVALALRNVPEANAYWNNDKEQAQKcvSVDISIAVATEKGLMTPIIRNADQKTISAISSEV 375
Cdd:PRK11856 230 KQLKAI-GVKLTVTDFLIKAVALALKKFPELNASWDDDAIVLKK--YVNIGIAVATDGGLIVPVIRDADKKSLFELAREI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 376 KQLAEKARAGKLAPNEFQGGTFSISNLGMYPVDHFCAIINPPQSGILAVGRgnkIIEPVVDSDGteKATVVTKMSLTLSA 455
Cdd:PRK11856 307 KDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGA---IVERPVVVDG--EIVVRKVMPLSLSF 381
|
410
....*....|....*..
gi 1002278355 456 DHRVFDGQVGGKFFTEL 472
Cdd:PRK11856 382 DHRVIDGADAARFLKAL 398
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
270-472 |
8.05e-84 |
|
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: 257.47 E-value: 8.05e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 270 LLESKQTTPHLYLSQDVILDPLLAFRNELKEQH---GVKVSVNDIVIKAVALALRNVPEANAYWNNDKEQAQKCVSVDIS 346
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAadeETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 347 IAVATEKGLMTPIIRNADQKTISAISSEVKQLAEKARAGKLAPNEFQGGTFSISNLGMYPVDHFCAIINPPQSGILAVGR 426
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1002278355 427 GNKiiEPVVDSDGTEKATVvtkMSLTLSADHRVFDGQVGGKFFTEL 472
Cdd:pfam00198 161 IRK--RPVVVDGEIVVRKV---MPLSLSFDHRVIDGAEAARFLNTL 201
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
63-484 |
1.93e-82 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 260.92 E-value: 1.93e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 63 PALSPTMNQGNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSkDVQVGQPIAVTVEDLEDIKNI 142
Cdd:PRK05704 8 PTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGD-TVTVGQVLGRIDEGAAAGAAA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 143 PADASfggeqKEQSIASEAQKVETDAAKESSIItrISPAAKLLIKEHRLDQSVLNASGPRGTLLKGDVLAALklgASSSS 222
Cdd:PRK05704 87 AAAAA-----AAAAAAAPAQAQAAAAAEQSNDA--LSPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAAL---AAAAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 223 TKQKNAPAAPSSQPTHDFqAQSVtipqqndayEDIPNSQIRKVIAKRLLESKQTTPHLYLSQDVILDPLLAFRNELKEQ- 301
Cdd:PRK05704 157 APAAPAAAAPAAAPAPLG-ARPE---------ERVPMTRLRKTIAERLLEAQNTTAMLTTFNEVDMTPVMDLRKQYKDAf 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 302 ---HGVKVSVNDIVIKAVALALRNVPEANAYWNND----KEQaqkcvsVDISIAVATEKGLMTPIIRNADQKTISAISSE 374
Cdd:PRK05704 227 ekkHGVKLGFMSFFVKAVVEALKRYPEVNASIDGDdivyHNY------YDIGIAVGTPRGLVVPVLRDADQLSFAEIEKK 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 375 VKQLAEKARAGKLAPNEFQGGTFSISNLGMY------PvdhfcaIINPPQSGILAVgrgNKIIE-PVVdsdgtEKATVVT 447
Cdd:PRK05704 301 IAELAKKARDGKLSIEELTGGTFTITNGGVFgslmstP------IINPPQSAILGM---HKIKErPVA-----VNGQIVI 366
|
410 420 430
....*....|....*....|....*....|....*....
gi 1002278355 448 K--MSLTLSADHRVFDGQVGGKFFTELSQNFGDIRRLLL 484
Cdd:PRK05704 367 RpmMYLALSYDHRIIDGKEAVGFLVTIKELLEDPERLLL 405
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
60-484 |
5.66e-82 |
|
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: 259.67 E-value: 5.66e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 60 VGMPALSPTMNQGNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSKdVQVGQPIAVtVEDLEDI 139
Cdd:TIGR01347 3 IKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDT-VESGQVLAI-LEEGNDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 140 KNIPADASfgGEQKEQSIASEAQKVETDAAKESSIitriSPAAKLLIKEHRLDQSVLNASGPRGTLLKGDVLAALKLGAS 219
Cdd:TIGR01347 81 TAAPPAKS--GEEKEETPAASAAAAPTAAANRPSL----SPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKTEAPAS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 220 SSstkqknAPAAPSSQPTHDFQAQSVtipqqndayEDIPNSQIRKVIAKRLLESKQTTPHLYLSQDVILDPLLAFRNELK 299
Cdd:TIGR01347 155 AQ------PPAAAAAAAAPAAATRPE---------ERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 300 EQ----HGVKVSVNDIVIKAVALALRNVPEANAYWNNDKEQAQKcvSVDISIAVATEKGLMTPIIRNADQKTISAISSEV 375
Cdd:TIGR01347 220 EEfekkHGVKLGFMSFFVKAVVAALKRFPEVNAEIDGDDIVYKD--YYDISVAVSTDRGLVVPVVRNADRMSFADIEKEI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 376 KQLAEKARAGKLAPNEFQGGTFSISNLGMYPVDHFCAIINPPQSGILAVgrgNKIIE-PVVDSDGTEkatVVTKMSLTLS 454
Cdd:TIGR01347 298 ADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGM---HGIKErPVAVNGQIE---IRPMMYLALS 371
|
410 420 430
....*....|....*....|....*....|
gi 1002278355 455 ADHRVFDGQVGGKFFTELSQNFGDIRRLLL 484
Cdd:TIGR01347 372 YDHRLIDGKEAVTFLVTIKELLEDPRRLLL 401
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
72-484 |
3.08e-78 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 253.98 E-value: 3.08e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 72 GNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSKdVQVGQPIAVtVEDLEDIKNIPADASFGGE 151
Cdd:PRK11855 133 VEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDK-VSVGSLLVV-IEVAAAAPAAAAAPAAAAP 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 152 QKEQSIASEA--------QKVETDAAKESSIITRISPAAKLLIKEHRLDQSVLNASGPRGTLLKGDVLAALKLGASSSST 223
Cdd:PRK11855 211 AAAAAAAPAPapaaaaapAAAAPAAAAAPGKAPHASPAVRRLARELGVDLSQVKGTGKKGRITKEDVQAFVKGAMSAAAA 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 224 KQKNAPAAPS------SQPTHDFqAQSVTIpqqndayEDIPNSQIRKVIAKRLLESKQTTPHLYLSQDVILDPLLAFRNE 297
Cdd:PRK11855 291 AAAAAAAAGGgglgllPWPKVDF-SKFGEI-------ETKPLSRIKKISAANLHRSWVTIPHVTQFDEADITDLEALRKQ 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 298 LKEQH---GVKVSVNDIVIKAVALALRNVPEANAYWNND-KEQAQKcVSVDISIAVATEKGLMTPIIRNADQKTISAISS 373
Cdd:PRK11855 363 LKKEAekaGVKLTMLPFFIKAVVAALKEFPVFNASLDEDgDELTYK-KYFNIGFAVDTPNGLVVPVIKDVDKKSLLEIAR 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 374 EVKQLAEKARAGKLAPNEFQGGTFSISNLGMYPVDHFCAIINPPQSGILAVGRGnkIIEPVvdSDGTEkatVVTK--MSL 451
Cdd:PRK11855 442 EIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKS--QMKPV--WDGKE---FVPRlmLPL 514
|
410 420 430
....*....|....*....|....*....|...
gi 1002278355 452 TLSADHRVFDGQVGGKFFTELSQNFGDIRRLLL 484
Cdd:PRK11855 515 SLSYDHRVIDGATAARFTNYLKQLLADPRRMLL 547
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
60-484 |
2.08e-65 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 222.19 E-value: 2.08e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 60 VGMPALSPTmnQGNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSKdVQVGQPIAVtvedLEDI 139
Cdd:PRK11854 209 VNVPDIGGD--EVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDK-VKTGSLIMR----FEVE 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 140 KNIPADASfGGEQKEQSIASEAQKVETDAA-----------KESSIITRISPAAKLLIKEHRLDQSVLNASGPRGTLLKG 208
Cdd:PRK11854 282 GAAPAAAP-AKQEAAAPAPAAAKAEAPAAApaakaegksefAENDAYVHATPLVRRLAREFGVNLAKVKGTGRKGRILKE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 209 DVLAALKlgasSSSTKQKNAPAAPSSQ---------PTHDFQAQSVTipqqndayEDIPNSQIRKVIAKRLLESKQTTPH 279
Cdd:PRK11854 361 DVQAYVK----DAVKRAEAAPAAAAAGgggpgllpwPKVDFSKFGEI--------EEVELGRIQKISGANLHRNWVMIPH 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 280 LYLSQDVILDPLLAFRNE-----LKEQHGVKVSVNDIVIKAVALALRNVPEANAYWNNDKEQAQKCVSVDISIAVATEKG 354
Cdd:PRK11854 429 VTQFDKADITELEAFRKQqnaeaEKRKLGVKITPLVFIMKAVAAALEQMPRFNSSLSEDGQRLTLKKYVNIGIAVDTPNG 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 355 LMTPIIRNADQKTISAISSEVKQLAEKARAGKLAPNEFQGGTFSISNLGMYPVDHFCAIINPPQSGILAVGRGNKiiEPV 434
Cdd:PRK11854 509 LVVPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKSAM--EPV 586
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1002278355 435 vdsDGTEKATVVTKMSLTLSADHRVFDGQVGGKFFTELSQNFGDIRRLLL 484
Cdd:PRK11854 587 ---WNGKEFAPRLMLPLSLSYDHRVIDGADGARFITIINDRLSDIRRLVL 633
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
58-484 |
3.11e-59 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 200.68 E-value: 3.11e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 58 LVVGMPALSPTMNQGNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSkDVQVGQPIAVtvedle 137
Cdd:PTZ00144 45 KVIKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGD-TVEVGAPLSE------ 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 138 dIKNIPADASFGGEQKEQSIASEAQKVETDAAKESSiitrisPAAKllikehrldqsvlnasgprgtllkgdvlaalklg 217
Cdd:PTZ00144 118 -IDTGGAPPAAAPAAAAAAKAEKTTPEKPKAAAPTP------EPPA---------------------------------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 218 ASSSSTKQKNAPAAPSSQPTHDFQAQSVTIPQQndayEDIPNSQIRKVIAKRLLESKQTTPHLYLSQDVILDPLLAFRNE 297
Cdd:PTZ00144 157 ASKPTPPAAAKPPEPAPAAKPPPTPVARADPRE----TRVPMSRMRQRIAERLKASQNTCAMLTTFNECDMSALMELRKE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 298 LKEQ----HGVKVSVNDIVIKAVALALRNVPEANAYWNNDkeqaqkCVS----VDISIAVATEKGLMTPIIRNADQKTIS 369
Cdd:PTZ00144 233 YKDDfqkkHGVKLGFMSAFVKASTIALKKMPIVNAYIDGD------EIVyrnyVDISVAVATPTGLVVPVIRNCENKSFA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 370 AISSEVKQLAEKARAGKLAPNEFQGGTFSISNLGMYPVDHFCAIINPPQSGIL--------AVGRGNKI-IEPVvdsdgt 440
Cdd:PTZ00144 307 EIEKELADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILgmhaikkrPVVVGNEIvIRPI------ 380
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1002278355 441 ekatvvtkMSLTLSADHRVFDGQVGGKFFTELSQNFGDIRRLLL 484
Cdd:PTZ00144 381 --------MYLALTYDHRLIDGRDAVTFLKKIKDLIEDPARMLL 416
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
138-474 |
8.80e-53 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 181.64 E-value: 8.80e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 138 DIKNIPADASFGGEQKEQsiaseaqkVETdaAKESSIItRISPAAKLLIKEHRLDQSVLNASGPRGTLLKGDVLAALklg 217
Cdd:PRK14843 22 NLYDVSGSGANGRVHKED--------VET--YKDTNVV-RISPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALL--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 218 asssSTKQKNAPAAPSSQPTHDFQAQSVTIPQQNdaYEDIPNSQIRKVIAKRLLESKQTTPHLYLSQDVILDPLLAFRNE 297
Cdd:PRK14843 88 ----PENIENDSIKSPAQIEKVEEVPDNVTPYGE--IERIPMTPMRKVIAQRMVESYLTAPTFTLNYEVDMTEMLALRKK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 298 L----KEQHGVKVSVNDIVIKAVALALRNVPEANAYWNNDKEQAQKCVSVDISIAVATEKGLMTPIIRNADQKTISAISS 373
Cdd:PRK14843 162 VlepiMEATGKKTTVTDLLSLAVVKTLMKHPYINASLTEDGKTIITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 374 EVKQLAEKARAGKLAPNEFQGGTFSISNLGMYPVDHFCAIINPPQSGILAVgrGNKIIEPVVDSDgteKATVVTKMSLTL 453
Cdd:PRK14843 242 AFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQPNSAILGV--SSTIEKPVVVNG---EIVIRPIMSLGL 316
|
330 340
....*....|....*....|.
gi 1002278355 454 SADHRVFDGQVGGKFFTELSQ 474
Cdd:PRK14843 317 TIDHRVVDGMAGAKFMKDLKE 337
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
82-484 |
9.83e-53 |
|
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: 186.62 E-value: 9.83e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 82 GEKIEVGDVICEIETDKATLEF----------------ESLEEGYLAKILAPEGSKDVQVGQPIAVTvedledikniPAD 145
Cdd:TIGR01348 140 GDTVSADQSLITLESDKASMEVpapasgvvksvkvkvgDSVPTGDLILTLSVAGSTPATAPAPASAQ----------PAA 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 146 ASFGGEQKEQSIASEAQKVETDAAKES-----SIITRISPAAKLLIKEHRLDQSVLNASGPRGTLLKGDVLAALKlgass 220
Cdd:TIGR01348 210 QSPAATQPEPAAAPAAAKAQAPAPQQAgtqnpAKVDHAAPAVRRLAREFGVDLSAVKGTGIKGRILREDVQRFVK----- 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 221 ssTKQKNAPAAPSSqpTHDFQAQSVTIPQQN----DAYEDIPNSQIRKVIAKRLLESKQTTPHLYLSQDVILDPLLAFR- 295
Cdd:TIGR01348 285 --EPSVRAQAAAAS--AAGGAPGALPWPNVDfskfGEVEEVDMSRIRKISGANLTRNWTMIPHVTHFDKADITEMEAFRk 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 296 --NELKEQHGVKVSVNDIVIKAVALALRNVPEANAYWNNDKEQAQKCVSVDISIAVATEKGLMTPIIRNADQKTISAISS 373
Cdd:TIGR01348 361 qqNAAVEKEGVKLTVLHILMKAVAAALKKFPKFNASLDLGGEQLILKKYVNIGVAVDTPNGLLVPVIKDVDRKGITELAL 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 374 EVKQLAEKARAGKLAPNEFQGGTFSISNLGMYPVDHFCAIINPPQSGILAVGRGnkIIEPVvdSDGTEKATVVTkMSLTL 453
Cdd:TIGR01348 441 ELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKS--GMEPV--WNGKEFEPRLM-LPLSL 515
|
410 420 430
....*....|....*....|....*....|.
gi 1002278355 454 SADHRVFDGQVGGKFFTELSQNFGDIRRLLL 484
Cdd:TIGR01348 516 SYDHRVIDGADAARFTTYICESLADIRRLLL 546
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
76-484 |
1.42e-47 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 169.51 E-value: 1.42e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 76 KWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSKdVQVGQP-IAVTVEDLEDIKNIPADASFGGEqKE 154
Cdd:PLN02528 17 RWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDI-VKVGETlLKIMVEDSQHLRSDSLLLPTDSS-NI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 155 QSIASEAQKVETdaakESSIITriSPAAKLLIKEHRLDQSVLNASGPRGTLLKGDVL--AALKLGASSSSTKQKNAPAAP 232
Cdd:PLN02528 95 VSLAESDERGSN----LSGVLS--TPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLkyAAQKGVVKDSSSAEEATIAEQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 233 SSQPTHdfqaqSVTIPQQNDAYEDIPNSQIRKVIAKRLLESKQTtPHLYLSQDVILDPLLAFR---NELKEQHGVKVSVN 309
Cdd:PLN02528 169 EEFSTS-----VSTPTEQSYEDKTIPLRGFQRAMVKTMTAAAKV-PHFHYVEEINVDALVELKasfQENNTDPTVKHTFL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 310 DIVIKAVALALRNVPEANAYWNNDKEQAQKCVSVDISIAVATEKGLMTPIIRNADQKTISAISSEVKQLAEKARAGKLAP 389
Cdd:PLN02528 243 PFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAAENKLNP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 390 NEFQGGTFSISNLGMYPVDHFCAIINPPQSGILAVGRGNKIiePVVDSDGTEKATVVtkMSLTLSADHRVFDGQVGGKFF 469
Cdd:PLN02528 323 EDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKV--PRFVDDGNVYPASI--MTVTIGADHRVLDGATVARFC 398
|
410
....*....|....*
gi 1002278355 470 TELSQNFGDIRRLLL 484
Cdd:PLN02528 399 NEWKSYVEKPELLML 413
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
60-470 |
4.21e-42 |
|
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: 157.87 E-value: 4.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 60 VGMPALSPTMNQGNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEgSKDVQVGQPIAVTVEDLED- 138
Cdd:TIGR02927 5 VKMPALGESVTEGTVTSWLKAVGDTVEADEPLLEVSTDKVDTEIPSPAAGVLLEIRAPE-DDTVEVGGVLAIIGEPGEAg 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 139 ---------------------------------------------------------------IKNI------------- 142
Cdd:TIGR02927 84 sepapaapepeaapepeapapaptpaaeapapaapqaggsgeatevkmpelgesvtegtvtswLKAVgdtvevdepllev 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 143 ----------------------------------------------------PADASFGGEQKEQSIASEAQKVETDAAK 170
Cdd:TIGR02927 164 stdkvdteipspvagtlleirapeddtvevgtvlaiigdanaapaepaeeeaPAPSEAGSEPAPDPAARAPHAAPDPPAP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 171 -----------------ESSIITRISPAAKLLIKEHRLDQSVLNASGPRGTLLKGDVLAALKLGASSSSTKQKNAPAAPS 233
Cdd:TIGR02927 244 apapaktaapaaaapvsSGDSGPYVTPLVRKLAKDKGVDLSTVKGTGVGGRIRKQDVLAAAKAAEEARAAAAAPAAAAAP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 234 SQPTHDFQAQSVTIPQQNDAYEDIpnSQIRKVIAKRLLESKQTTPHLYLSQDVILDPLLAFR----NELKEQHGVKVSVN 309
Cdd:TIGR02927 324 AAPAAAAKPAEPDTAKLRGTTQKM--NRIRQITADKTIESLQTSAQLTQVHEVDMTRVAALRarakNDFLEKNGVNLTFL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 310 DIVIKAVALALRNVPEANAYWNNDKEQAQKCVSVDISIAVATEKGLMTPIIRNADQKTISAISSEVKQLAEKARAGKLAP 389
Cdd:TIGR02927 402 PFFVQAVTEALKAHPNVNASYNAETKEVTYHDVEHVGIAVDTPRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKP 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 390 NEFQGGTFSISNLGMYPVDHFCAIINPPQSGILAVGRGNKIIEPVVDSDGTEKATVVTKMSLTLSADHRVFDGQVGGKFF 469
Cdd:TIGR02927 482 DELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAIVKRPRVIKDEDGGESIAIRSVCYLPLTYDHRLVDGADAGRFL 561
|
.
gi 1002278355 470 T 470
Cdd:TIGR02927 562 T 562
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
47-484 |
9.70e-42 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 154.91 E-value: 9.70e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 47 RWL----SSTGFPPHLVVgmPALSPTMNQGNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSKd 122
Cdd:PLN02226 79 RWVrpfsSESGDTVEAVV--PHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDT- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 123 VQVGQPIAVTvedlediknipadasfggeqkeqsiaseaqkvetdaAKESSIITRISPAAKLlikehrldqsvlnasgPR 202
Cdd:PLN02226 156 VEPGTKVAII------------------------------------SKSEDAASQVTPSQKI----------------PE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 203 GTLLKGDVLAALKLGASSSSTKQKNAPAAPSSQPTHDFQAQSVTIPQQnDAYEDIPNSQIRKVIAKRLLESKQTTPHLYL 282
Cdd:PLN02226 184 TTDPKPSPPAEDKQKPKVESAPVAEKPKAPSSPPPPKQSAKEPQLPPK-ERERRVPMTRLRKRVATRLKDSQNTFALLTT 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 283 SQDVILDPLLAFRNELK----EQHGVKVSVNDIVIKAVALALRNVPEANAYWNNDKEQAQKcvSVDISIAVATEKGLMTP 358
Cdd:PLN02226 263 FNEVDMTNLMKLRSQYKdafyEKHGVKLGLMSGFIKAAVSALQHQPVVNAVIDGDDIIYRD--YVDISIAVGTSKGLVVP 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 359 IIRNADQKTISAISSEVKQLAEKARAGKLAPNEFQGGTFSISNLGMYPVDHFCAIINPPQSGILavGRGNKIIEPVVDSd 438
Cdd:PLN02226 341 VIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAIL--GMHSIVSRPMVVG- 417
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1002278355 439 gtekATVVTK--MSLTLSADHRVFDGQVGGKFFTELSQNFGDIRRLLL 484
Cdd:PLN02226 418 ----GSVVPRpmMYVALTYDHRLIDGREAVYFLRRVKDVVEDPQRLLL 461
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
178-474 |
9.80e-38 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 139.93 E-value: 9.80e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 178 ISPAAKLLIKEHRLDQSVLNASGPRGTLLKGDVLaalKLGASSSSTKQKNAPAAPSSQPTHDFQAQSVTIPQQNDAYEDi 257
Cdd:PRK11857 4 ATPIARALAKKLGIDISLLKGSGRDGKILAEDVE---NFIKSLKSAPTPAEAASVSSAQQAAKTAAPAAAPPKLEGKRE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 258 PNSQIRKVIAKRLLESKQTTPHLYLSQDVILDPLLAFRNELKEQ----HGVKVSVNDIVIKAVALALRNVPEANAYWNND 333
Cdd:PRK11857 80 KVAPIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPvlktEGVKLTFLPFIAKAILIALKEFPIFAAKYDEA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 334 KEQAQKCVSVDISIAVATEKGLMTPIIRNADQKTISAISSEVKQLAEKARAGKLAPNEFQGGTFSISNLGMYPVDHFCAI 413
Cdd:PRK11857 160 TSELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLYGVPV 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002278355 414 INPPQSGILAVGrgnKIIEPVVDSDGTEKATVVtkMSLTLSADHRVFDGQVGGKFFTELSQ 474
Cdd:PRK11857 240 INYPELAIAGVG---AIIDKAIVKNGQIVAGKV--MHLTVAADHRWIDGATIGRFASRVKE 295
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
62-174 |
1.57e-35 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 137.74 E-value: 1.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 62 MPALSPTMNQGNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSKDVQVGQPIAVTVEDLEDIKN 141
Cdd:PRK11892 7 MPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEGVKVNTPIAVLLEEGESASD 86
|
90 100 110
....*....|....*....|....*....|...
gi 1002278355 142 IPADASFGGEQKEQSIASEAQKVETDAAKESSI 174
Cdd:PRK11892 87 AGAAPAAAAEAAAAAPAAAAAAAAKKAAPAPAA 119
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
62-131 |
1.27e-27 |
|
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: 105.18 E-value: 1.27e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 62 MPALSPTMNQGNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSKdVQVGQPIAV 131
Cdd:cd06849 5 MPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAV 73
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
62-131 |
2.85e-25 |
|
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: 98.60 E-value: 2.85e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 62 MPALSPTMNQGNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSKdVQVGQPIAV 131
Cdd:COG0508 7 MPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDT-VPVGAVIAV 75
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
60-168 |
2.48e-16 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 80.37 E-value: 2.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 60 VGMPALSPTMNQGNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSkDVQVGQPIAV----TVED 135
Cdd:PRK14875 5 ITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGE-TLPVGALLAVvadaEVSD 83
|
90 100 110
....*....|....*....|....*....|....*.
gi 1002278355 136 LED---IKNIPADASFGGEQkEQSIASEAQKVETDA 168
Cdd:PRK14875 84 AEIdafIAPFARRFAPEGID-EEDAGPAPRKARIGG 118
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
59-131 |
2.82e-16 |
|
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: 73.40 E-value: 2.82e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002278355 59 VVGMPALSPTMNQGnIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSKdVQVGQPIAV 131
Cdd:pfam00364 2 EIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDT-VEVGDPLAK 72
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
60-129 |
1.91e-15 |
|
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: 70.93 E-value: 1.91e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 60 VGMPALSPTMNQGNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSKdVQVGQPI 129
Cdd:cd06663 2 ILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTK-VEGDTPL 70
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
296-474 |
8.21e-10 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 61.44 E-value: 8.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 296 NELKEQHGVKVSVNDIVIKAVALALRNVPEANAYWN--NDKEQAQKCVSVDISIAVATEK-----GLMTPIIRNADQKTI 368
Cdd:PRK12270 160 NHLKRTRGGKVSFTHLIGYALVQALKAFPNMNRHYAevDGKPTLVTPAHVNLGLAIDLPKkdgsrQLVVPAIKGAETMDF 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 369 SAISSEVKQLAEKARAGKLAPNEFQGGTFSISNLGMYPVDHFCAIINPPQSGILAVGRgnkiIEPVVDSDGTEKATV--- 445
Cdd:PRK12270 240 AQFWAAYEDIVRRARDGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGA----MEYPAEFQGASEERLael 315
|
170 180 190
....*....|....*....|....*....|.
gi 1002278355 446 -VTK-MSLTLSADHRVFDGQVGGKFFTELSQ 474
Cdd:PRK12270 316 gISKvMTLTSTYDHRIIQGAESGEFLRTIHQ 346
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
71-131 |
3.49e-06 |
|
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: 44.33 E-value: 3.49e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002278355 71 QGNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSKdVQVGQPIAV 131
Cdd:cd06850 7 PGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQ-VEAGQLLVV 66
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
177-211 |
1.55e-05 |
|
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: 41.90 E-value: 1.55e-05
10 20 30
....*....|....*....|....*....|....*
gi 1002278355 177 RISPAAKLLIKEHRLDQSVLNASGPRGTLLKGDVL 211
Cdd:pfam02817 2 LASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
22-131 |
2.61e-04 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 43.68 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002278355 22 GRCVSSSRPSYLASLGRHYKVPME-IRWLSSTGFPPHLVVGmpALSPTMnQGNIAKWRKQEGEKIEVGDVICEIETDKAT 100
Cdd:PRK09282 483 GVKAEGKRPFYLRVDGMPEEVVVEpLKEIVVGGRPRASAPG--AVTSPM-PGTVVKVKVKEGDKVKAGDTVLVLEAMKME 559
|
90 100 110
....*....|....*....|....*....|.
gi 1002278355 101 LEFESLEEGYLAKILAPEGsKDVQVGQPIAV 131
Cdd:PRK09282 560 NEIQAPVDGTVKEILVKEG-DRVNPGDVLME 589
|
|
| |
