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Conserved domains on  [gi|1435033878|ref|XP_025783855|]
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pyruvate dehydrogenase protein X component, mitochondrial isoform X2 [Puma concolor]

Protein Classification

pyruvate dehydrogenase complex E2/E3BP family protein( domain architecture ID 1000906)

2-oxoacid dehydrogenase family protein similar to pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase (E2) and dihydrolipoamide dehydrogenase-binding protein (E3BP)

CATH:  2.40.50.100
Gene Ontology:  GO:0045254

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PDHac_trf_mito super family cl36877
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
1-440 2.28e-138

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]


The actual alignment was detected with superfamily member TIGR01349:

Pssm-ID: 273567 [Multi-domain]  Cd Length: 436  Bit Score: 403.79  E-value: 2.28e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878   1 MPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKNIRLGALIGLLVEEGED--- 77
Cdd:TIGR01349   4 MPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKEDvad 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878  78 ----------WKHVEIPKDVGPPSPASKPSVPcPSPEPQI---STAVEKEHIPGKLQFRLSPAARNILEKHSLDASQGTA 144
Cdd:TIGR01349  84 afknyklessASPAPKPSEIAPTAPPSAPKPS-PAPQKQSpepSSPAPLSDKESGDRIFASPLAKKLAKEKGIDLSAVAG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 145 TGPRGIFTKEDALKLVqlketgkitESRPTPAPlatpavplpPQAMATPPYTRPMIPPVSTpgqpnvvGTFTEIPASNIR 224
Cdd:TIGR01349 163 SGPNGRIVKKDIESFV---------PQSPASAN---------QQAAATTPATYPAAAPVST-------GSYEDVPLSNIR 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 225 RVIAKRLTESKSTVPHAYATTDCDLGAVLKARQSL---VRDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPKQLPFI 301
Cdd:TIGR01349 218 KIIAKRLLESKQTIPHYYVSIECNVDKLLALRKELnamASEVYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYKNV 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 302 DISVAVATDKGLITPIIKDAAAKGIREIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILA 381
Cdd:TIGR01349 298 DISVAVATPDGLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILA 377
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1435033878 382 VGRFRPVLKLTRDEEgnAQLQRHQLITVTMSSDSRVVDDELATRFLESFKANLENPIRL 440
Cdd:TIGR01349 378 VGAVEDVAVVDNDEE--KGFAVASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEM 434
 
Name Accession Description Interval E-value
PDHac_trf_mito TIGR01349
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
1-440 2.28e-138

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: 403.79  E-value: 2.28e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878   1 MPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKNIRLGALIGLLVEEGED--- 77
Cdd:TIGR01349   4 MPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKEDvad 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878  78 ----------WKHVEIPKDVGPPSPASKPSVPcPSPEPQI---STAVEKEHIPGKLQFRLSPAARNILEKHSLDASQGTA 144
Cdd:TIGR01349  84 afknyklessASPAPKPSEIAPTAPPSAPKPS-PAPQKQSpepSSPAPLSDKESGDRIFASPLAKKLAKEKGIDLSAVAG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 145 TGPRGIFTKEDALKLVqlketgkitESRPTPAPlatpavplpPQAMATPPYTRPMIPPVSTpgqpnvvGTFTEIPASNIR 224
Cdd:TIGR01349 163 SGPNGRIVKKDIESFV---------PQSPASAN---------QQAAATTPATYPAAAPVST-------GSYEDVPLSNIR 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 225 RVIAKRLTESKSTVPHAYATTDCDLGAVLKARQSL---VRDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPKQLPFI 301
Cdd:TIGR01349 218 KIIAKRLLESKQTIPHYYVSIECNVDKLLALRKELnamASEVYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYKNV 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 302 DISVAVATDKGLITPIIKDAAAKGIREIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILA 381
Cdd:TIGR01349 298 DISVAVATPDGLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILA 377
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1435033878 382 VGRFRPVLKLTRDEEgnAQLQRHQLITVTMSSDSRVVDDELATRFLESFKANLENPIRL 440
Cdd:TIGR01349 378 VGAVEDVAVVDNDEE--KGFAVASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEM 434
PRK11856 PRK11856
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
1-440 4.09e-134

branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed


Pssm-ID: 237001 [Multi-domain]  Cd Length: 411  Bit Score: 391.85  E-value: 4.09e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878   1 MPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnIRLGALIGLLVEEGEdwKH 80
Cdd:PRK11856    7 MPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDV-VPVGSVIAVIEEEGE--AE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878  81 VEIPKDVGPPSPASKPSVPCPSPEPQISTAVEKEHIPGKLQFRLSPAARNILEKHSLDASQGTATGPRGIFTKEDALKLV 160
Cdd:PRK11856   84 AAAAAEAAPEAPAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEAAA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 161 qlketgkiteSRPTPAPLATPAVPLPPQAMATPPYTRpmippvstpgqpnvvgtfteIPASNIRRVIAKRLTESKSTVPH 240
Cdd:PRK11856  164 ----------AAAAPAAAAAAAAAAAPPAAAAEGEER--------------------VPLSGMRKAIAKRMVESKREIPH 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 241 AYATTDCDLGAVLKARQSLVRDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPKQLPFIDISVAVATDKGLITPIIKD 320
Cdd:PRK11856  214 FTLTDEVDVTALLALRKQLKAIGVKLTVTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVATDGGLIVPVIRD 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 321 AAAKGIREIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGRF--RPVLKltrdeegN 398
Cdd:PRK11856  294 ADKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIveRPVVV-------D 366
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 1435033878 399 AQLQRHQLITVTMSSDSRVVDDELATRFLESFKANLENPIRL 440
Cdd:PRK11856  367 GEIVVRKVMPLSLSFDHRVIDGADAARFLKALKELLENPALL 408
2-oxoacid_dh pfam00198
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ...
231-440 3.42e-82

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: 252.08  E-value: 3.42e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 231 LTESKSTVPHAYATTDCDLGAVLKARQSL----VRDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPK--QLPFIDIS 304
Cdd:pfam00198   1 MTESKQTIPHFTLTDEVDVTELLALREELkedaADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEivYKKYVNIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 305 VAVATDKGLITPIIKDAAAKGIREIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGR 384
Cdd:pfam00198  81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1435033878 385 --FRPVLKltrdeegNAQLQRHQLITVTMSSDSRVVDDELATRFLESFKANLENPIRL 440
Cdd:pfam00198 161 irKRPVVV-------DGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELL 211
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
1-71 4.07e-26

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: 100.56  E-value: 4.07e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1435033878   1 MPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnIRLGALIGLL 71
Cdd:cd06849     5 MPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAVI 74
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
1-72 2.82e-23

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: 92.82  E-value: 2.82e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1435033878   1 MPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnIRLGALIGLLV 72
Cdd:COG0508     7 MPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDT-VPVGAVIAVIA 77
 
Name Accession Description Interval E-value
PDHac_trf_mito TIGR01349
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
1-440 2.28e-138

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: 403.79  E-value: 2.28e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878   1 MPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKNIRLGALIGLLVEEGED--- 77
Cdd:TIGR01349   4 MPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKEDvad 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878  78 ----------WKHVEIPKDVGPPSPASKPSVPcPSPEPQI---STAVEKEHIPGKLQFRLSPAARNILEKHSLDASQGTA 144
Cdd:TIGR01349  84 afknyklessASPAPKPSEIAPTAPPSAPKPS-PAPQKQSpepSSPAPLSDKESGDRIFASPLAKKLAKEKGIDLSAVAG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 145 TGPRGIFTKEDALKLVqlketgkitESRPTPAPlatpavplpPQAMATPPYTRPMIPPVSTpgqpnvvGTFTEIPASNIR 224
Cdd:TIGR01349 163 SGPNGRIVKKDIESFV---------PQSPASAN---------QQAAATTPATYPAAAPVST-------GSYEDVPLSNIR 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 225 RVIAKRLTESKSTVPHAYATTDCDLGAVLKARQSL---VRDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPKQLPFI 301
Cdd:TIGR01349 218 KIIAKRLLESKQTIPHYYVSIECNVDKLLALRKELnamASEVYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYKNV 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 302 DISVAVATDKGLITPIIKDAAAKGIREIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILA 381
Cdd:TIGR01349 298 DISVAVATPDGLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILA 377
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1435033878 382 VGRFRPVLKLTRDEEgnAQLQRHQLITVTMSSDSRVVDDELATRFLESFKANLENPIRL 440
Cdd:TIGR01349 378 VGAVEDVAVVDNDEE--KGFAVASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEM 434
PRK11856 PRK11856
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
1-440 4.09e-134

branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed


Pssm-ID: 237001 [Multi-domain]  Cd Length: 411  Bit Score: 391.85  E-value: 4.09e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878   1 MPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnIRLGALIGLLVEEGEdwKH 80
Cdd:PRK11856    7 MPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDV-VPVGSVIAVIEEEGE--AE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878  81 VEIPKDVGPPSPASKPSVPCPSPEPQISTAVEKEHIPGKLQFRLSPAARNILEKHSLDASQGTATGPRGIFTKEDALKLV 160
Cdd:PRK11856   84 AAAAAEAAPEAPAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEAAA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 161 qlketgkiteSRPTPAPLATPAVPLPPQAMATPPYTRpmippvstpgqpnvvgtfteIPASNIRRVIAKRLTESKSTVPH 240
Cdd:PRK11856  164 ----------AAAAPAAAAAAAAAAAPPAAAAEGEER--------------------VPLSGMRKAIAKRMVESKREIPH 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 241 AYATTDCDLGAVLKARQSLVRDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPKQLPFIDISVAVATDKGLITPIIKD 320
Cdd:PRK11856  214 FTLTDEVDVTALLALRKQLKAIGVKLTVTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVATDGGLIVPVIRD 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 321 AAAKGIREIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGRF--RPVLKltrdeegN 398
Cdd:PRK11856  294 ADKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIveRPVVV-------D 366
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 1435033878 399 AQLQRHQLITVTMSSDSRVVDDELATRFLESFKANLENPIRL 440
Cdd:PRK11856  367 GEIVVRKVMPLSLSFDHRVIDGADAARFLKALKELLENPALL 408
PLN02744 PLN02744
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
1-437 2.32e-111

dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex


Pssm-ID: 215397 [Multi-domain]  Cd Length: 539  Bit Score: 338.37  E-value: 2.32e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878   1 MPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKNIRLGALIGLLVEEGED--- 77
Cdd:PLN02744  117 MPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKEIKVGEVIAITVEEEEDigk 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878  78 WKHVEIPKDVGPPSPASKPSVPCP----------SPEPQISTAVEKEHiPGKLQFRlSPAARNILEKHSLDASQGTATGP 147
Cdd:PLN02744  197 FKDYKPSSSAAPAAPKAKPSPPPPkeeevekpasSPEPKASKPSAPPS-SGDRIFA-SPLARKLAEDNNVPLSSIKGTGP 274
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 148 RGIFTKEDALKLVQLKETGkitESRPTPAPLATPAVplppqamatppytrpmippvstpgqpnvvgTFTEIPASNIRRVI 227
Cdd:PLN02744  275 DGRIVKADIEDYLASGGKG---ATAPPSTDSKAPAL------------------------------DYTDIPNTQIRKVT 321
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 228 AKRLTESKSTVPHAYATTDCDLGAVLKARQSL-----VRDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPKQLPFID 302
Cdd:PLN02744  322 ASRLLQSKQTIPHYYLTVDTRVDKLMALRSQLnslqeASGGKKISVNDLVIKAAALALRKVPQCNSSWTDDYIRQYHNVN 401
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 303 ISVAVATDKGLITPIIKDAAAKGIREIADSVKALSKKARDGKLLPEEYQGGSFSISNL-GMFGIDEFTAVINPPQACILA 381
Cdd:PLN02744  402 INVAVQTENGLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLgGPFGIKQFCAIINPPQSAILA 481
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 382 VG----RFRPvlkltrdEEGNAQLQRHQLITVTMSSDSRVVDDELATRFLESFKANLENP 437
Cdd:PLN02744  482 VGsaekRVIP-------GSGPDQYNFASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENP 534
2-oxoacid_dh pfam00198
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ...
231-440 3.42e-82

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: 252.08  E-value: 3.42e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 231 LTESKSTVPHAYATTDCDLGAVLKARQSL----VRDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPK--QLPFIDIS 304
Cdd:pfam00198   1 MTESKQTIPHFTLTDEVDVTELLALREELkedaADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEivYKKYVNIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 305 VAVATDKGLITPIIKDAAAKGIREIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGR 384
Cdd:pfam00198  81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1435033878 385 --FRPVLKltrdeegNAQLQRHQLITVTMSSDSRVVDDELATRFLESFKANLENPIRL 440
Cdd:pfam00198 161 irKRPVVV-------DGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELL 211
sucB TIGR01347
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ...
2-441 3.52e-73

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: 235.40  E-value: 3.52e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878   2 PSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnirlgaligllVEEGEDWKHV 81
Cdd:TIGR01347   6 PELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDT-----------VESGQVLAIL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878  82 EIPKDVGPPSPA----SKPSVPCPSPEPQISTAVEKEHipgklqfrLSPAARNILEKHSLDASQGTATGPRGIFTKEDAL 157
Cdd:TIGR01347  75 EEGNDATAAPPAksgeEKEETPAASAAAAPTAAANRPS--------LSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDII 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 158 KLvqlketgkiTESRPTPAPLATPAVPLPPQAmatppYTRPMippvstpgqpnvvgtfTEIPASNIRRVIAKRLTESKST 237
Cdd:TIGR01347 147 KK---------TEAPASAQPPAAAAAAAAPAA-----ATRPE----------------ERVKMTRLRQRIAERLKEAQNS 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 238 VphAYATT--DCDLGAVLKAR-----QSLVRDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPKQLPFIDISVAVATD 310
Cdd:TIGR01347 197 T--AMLTTfnEVDMSAVMELRkrykeEFEKKHGVKLGFMSFFVKAVVAALKRFPEVNAEIDGDDIVYKDYYDISVAVSTD 274
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 311 KGLITPIIKDAAAKGIREIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGRF--RPV 388
Cdd:TIGR01347 275 RGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIkeRPV 354
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1435033878 389 LKltrdeegNAQLQRHQLITVTMSSDSRVVDDELATRFLESFKANLENPIRLA 441
Cdd:TIGR01347 355 AV-------NGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRRLL 400
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
10-441 4.67e-73

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 238.95  E-value: 4.67e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878  10 EGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnIRLGALIGLLVEEGEDWKHVEIPKDVGP 89
Cdd:PRK11855  132 EVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDK-VSVGSLLVVIEVAAAAPAAAAAPAAAAP 210
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878  90 PSPASKPSVPCPSPEPQISTAVEKEHIPGKLQFRLSPAARNILEKHSLDASQGTATGPRGIFTKEDALKLVQLKETGKIT 169
Cdd:PRK11855  211 AAAAAAAPAPAPAAAAAPAAAAPAAAAAPGKAPHASPAVRRLARELGVDLSQVKGTGKKGRITKEDVQAFVKGAMSAAAA 290
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 170 ESRPTPAPLATPAVPLPPQAMATppytrpmippvstpgqpNVVGTFTEIPASNIRRVIAKRLTESKSTVPHAYATTDCDL 249
Cdd:PRK11855  291 AAAAAAAAGGGGLGLLPWPKVDF-----------------SKFGEIETKPLSRIKKISAANLHRSWVTIPHVTQFDEADI 353
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 250 GAVLKARQSL----VRDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGpKQLPF---IDISVAVATDKGLITPIIKDAA 322
Cdd:PRK11855  354 TDLEALRKQLkkeaEKAGVKLTMLPFFIKAVVAALKEFPVFNASLDEDG-DELTYkkyFNIGFAVDTPNGLVVPVIKDVD 432
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 323 AKGIREIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGRF--RPVlkltrdeEGNAQ 400
Cdd:PRK11855  433 KKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSqmKPV-------WDGKE 505
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 1435033878 401 LQRHQLITVTMSSDSRVVDDELATRFLESFKANLENPIRLA 441
Cdd:PRK11855  506 FVPRLMLPLSLSYDHRVIDGATAARFTNYLKQLLADPRRML 546
PRK05704 PRK05704
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
2-440 6.14e-72

2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;


Pssm-ID: 235571 [Multi-domain]  Cd Length: 407  Bit Score: 232.03  E-value: 6.14e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878   2 PSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSkNIRLGALIGLLVEEGEdwkhv 81
Cdd:PRK05704    8 PTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGD-TVTVGQVLGRIDEGAA----- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878  82 eipkdVGPPSPASKPSVPCPSPEPQISTAVEKEHIPGKLqfrlSPAARNILEKHSLDASQGTATGPRGIFTKEDALKLVQ 161
Cdd:PRK05704   82 -----AGAAAAAAAAAAAAAAAPAQAQAAAAAEQSNDAL----SPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAALA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 162 LKETgkitesrPTPAPLATPAVPLPPQAMATPPYTRPMippvstpgqpnvvgtfteipaSNIRRVIAKRLTESKSTVphA 241
Cdd:PRK05704  153 AAAA-------APAAPAAAAPAAAPAPLGARPEERVPM---------------------TRLRKTIAERLLEAQNTT--A 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 242 YATT--DCDLGAVLKAR-----QSLVRDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPKQLPFIDISVAVATDKGLI 314
Cdd:PRK05704  203 MLTTfnEVDMTPVMDLRkqykdAFEKKHGVKLGFMSFFVKAVVEALKRYPEVNASIDGDDIVYHNYYDIGIAVGTPRGLV 282
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 315 TPIIKDAAAKGIREIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGRF--RPVLKlt 392
Cdd:PRK05704  283 VPVLRDADQLSFAEIEKKIAELAKKARDGKLSIEELTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHKIkeRPVAV-- 360
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 1435033878 393 rdeegNAQLQRHQLITVTMSSDSRVVDDELATRFLESFKANLENPIRL 440
Cdd:PRK05704  361 -----NGQIVIRPMMYLALSYDHRIIDGKEAVGFLVTIKELLEDPERL 403
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
10-440 2.25e-55

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 194.07  E-value: 2.25e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878  10 EGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnIRLGALIGLLVEEGEDWKHVEIPKDVGP 89
Cdd:PRK11854  218 EVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDK-VKTGSLIMRFEVEGAAPAAAPAKQEAAA 296
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878  90 PSPASKPSVPcPSPEPQISTAVEKEHIPGKLQFRLSPAARNILEKHSLDASQGTATGPRGIFTKEDALKLVqlKETGKIT 169
Cdd:PRK11854  297 PAPAAAKAEA-PAAAPAAKAEGKSEFAENDAYVHATPLVRRLAREFGVNLAKVKGTGRKGRILKEDVQAYV--KDAVKRA 373
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 170 ESRPTPAPLATPAVPLPPqamatppytrpmIPPVStpgqPNVVGTFTEIPASNIRRVIAKRLTESKSTVPHA--YATTD- 246
Cdd:PRK11854  374 EAAPAAAAAGGGGPGLLP------------WPKVD----FSKFGEIEEVELGRIQKISGANLHRNWVMIPHVtqFDKADi 437
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 247 CDLGAVLKARQSLV---RDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGpKQL---PFIDISVAVATDKGLITPIIKD 320
Cdd:PRK11854  438 TELEAFRKQQNAEAekrKLGVKITPLVFIMKAVAAALEQMPRFNSSLSEDG-QRLtlkKYVNIGIAVDTPNGLVVPVFKD 516
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 321 AAAKGIREIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGR--FRPVlkltrdeEGN 398
Cdd:PRK11854  517 VNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKsaMEPV-------WNG 589
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 1435033878 399 AQLQRHQLITVTMSSDSRVVDDELATRFLESFKANLENPIRL 440
Cdd:PRK11854  590 KEFAPRLMLPLSLSYDHRVIDGADGARFITIINDRLSDIRRL 631
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
9-440 1.13e-52

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: 185.08  E-value: 1.13e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878   9 EEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnIRLGALIGLLVEEGEDWKHVEIPKDVG 88
Cdd:TIGR01348 128 EKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDS-VPTGDLILTLSVAGSTPATAPAPASAQ 206
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878  89 PP--SPASKPSVPCPSPEPQISTAVEKEHIPGKLQFRL---SPAARNILEKHSLDASQGTATGPRGIFTKEDALKLVQlk 163
Cdd:TIGR01348 207 PAaqSPAATQPEPAAAPAAAKAQAPAPQQAGTQNPAKVdhaAPAVRRLAREFGVDLSAVKGTGIKGRILREDVQRFVK-- 284
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 164 etgkiTESRPTPAPLATPAVPLPpqamatppytrpMIPPVstpgqPNV----VGTFTEIPASNIRRVIAKRLTESKSTVP 239
Cdd:TIGR01348 285 -----EPSVRAQAAAASAAGGAP------------GALPW-----PNVdfskFGEVEEVDMSRIRKISGANLTRNWTMIP 342
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 240 HA--YATTD-CDLGAVLKARQSLVR-DDIKVSVNDFIIKAAAVTLKQMPDVNVSWDgEGPKQL---PFIDISVAVATDKG 312
Cdd:TIGR01348 343 HVthFDKADiTEMEAFRKQQNAAVEkEGVKLTVLHILMKAVAAALKKFPKFNASLD-LGGEQLilkKYVNIGVAVDTPNG 421
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 313 LITPIIKDAAAKGIREIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGR--FRPVLK 390
Cdd:TIGR01348 422 LLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKsgMEPVWN 501
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 1435033878 391 LTrdeegnaQLQRHQLITVTMSSDSRVVDDELATRFLESFKANLENPIRL 440
Cdd:TIGR01348 502 GK-------EFEPRLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRL 544
PTZ00144 PTZ00144
dihydrolipoamide succinyltransferase; Provisional
2-440 1.04e-51

dihydrolipoamide succinyltransferase; Provisional


Pssm-ID: 240289 [Multi-domain]  Cd Length: 418  Bit Score: 179.49  E-value: 1.04e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878   2 PSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnirlgaligllVEEGEDWkhV 81
Cdd:PTZ00144   50 PTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDT-----------VEVGAPL--S 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878  82 EIPKDVGPPS-PASKPSVPCPSPEPQISTAVEKEHIPGKlqfrlspaarnilekhsldasqgtatgprgiftkedalklv 160
Cdd:PTZ00144  117 EIDTGGAPPAaAPAAAAAAKAEKTTPEKPKAAAPTPEPP----------------------------------------- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 161 qlketgkiTESRPTPAPLATPAvplppqamATPPYTRPMIPPVSTPGQPNvvgtfTEIPASNIRRVIAKRLTESKSTvpH 240
Cdd:PTZ00144  156 --------AASKPTPPAAAKPP--------EPAPAAKPPPTPVARADPRE-----TRVPMSRMRQRIAERLKASQNT--C 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 241 AYATT--DCDLGAVLKARQSL-----VRDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPKQLPFIDISVAVATDKGL 313
Cdd:PTZ00144  213 AMLTTfnECDMSALMELRKEYkddfqKKHGVKLGFMSAFVKASTIALKKMPIVNAYIDGDEIVYRNYVDISVAVATPTGL 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 314 ITPIIKDAAAKGIREIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACIL---AVGRfRPVLK 390
Cdd:PTZ00144  293 VVPVIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILgmhAIKK-RPVVV 371
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 1435033878 391 ltrdeegNAQLQRHQLITVTMSSDSRVVDDELATRFLESFKANLENPIRL 440
Cdd:PTZ00144  372 -------GNEIVIRPIMYLALTYDHRLIDGRDAVTFLKKIKDLIEDPARM 414
SucB_Actino TIGR02927
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ...
1-435 3.20e-47

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: 170.96  E-value: 3.20e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878   1 MPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEgSKNIRLGALIGLLveeGEDWKH 80
Cdd:TIGR02927 131 MPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPE-DDTVEVGTVLAII---GDANAA 206
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878  81 VEIPKDVGPPSPASKPSVPCPSPEPQISTAVEKEHIPGKLQFRLSPAA------------------RNILEKHSLDASQG 142
Cdd:TIGR02927 207 PAEPAEEEAPAPSEAGSEPAPDPAARAPHAAPDPPAPAPAPAKTAAPAaaapvssgdsgpyvtplvRKLAKDKGVDLSTV 286
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 143 TATGPRGIFTKEDALKLVQlketgKITESRPTPAPLATPAVPLPPQAMATPPytrpmippvsTPGQPNVVGTFTEipASN 222
Cdd:TIGR02927 287 KGTGVGGRIRKQDVLAAAK-----AAEEARAAAAAPAAAAAPAAPAAAAKPA----------EPDTAKLRGTTQK--MNR 349
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 223 IRRVIAKRLTESKSTVPHAYATTDCDLGAVLKARQS-----LVRDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGpKQ 297
Cdd:TIGR02927 350 IRQITADKTIESLQTSAQLTQVHEVDMTRVAALRARakndfLEKNGVNLTFLPFFVQAVTEALKAHPNVNASYNAET-KE 428
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 298 LPFID---ISVAVATDKGLITPIIKDAAAKGIREIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINP 374
Cdd:TIGR02927 429 VTYHDvehVGIAVDTPRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDTPILNP 508
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1435033878 375 PQACILAVGRFRPVLKLTRDEEGNAQLQRHQLITVTMSSDSRVVDDELATRFLESFKANLE 435
Cdd:TIGR02927 509 PQAAILGTGAIVKRPRVIKDEDGGESIAIRSVCYLPLTYDHRLVDGADAGRFLTTIKKRLE 569
PLN02528 PLN02528
2-oxoisovalerate dehydrogenase E2 component
10-440 8.57e-45

2-oxoisovalerate dehydrogenase E2 component


Pssm-ID: 215289 [Multi-domain]  Cd Length: 416  Bit Score: 161.04  E-value: 8.57e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878  10 EGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnIRLG-ALIGLLVEEGEDwkhvEIPKDVG 88
Cdd:PLN02528   12 ECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDI-VKVGeTLLKIMVEDSQH----LRSDSLL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878  89 PPSPASKPSVPCPSPEpqistavEKEHIPGKLQfrlSPAARNILEKHSLDASQGTATGPRGIFTKEDALKLVQLKEtgki 168
Cdd:PLN02528   87 LPTDSSNIVSLAESDE-------RGSNLSGVLS---TPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAAQKG---- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 169 tesrptpaplatpAVPLPPQA-MATPPYTRPMIPPVSTP-GQPNVVGTfteIPASNIRRVIAKRLTESKStVPHAYATTD 246
Cdd:PLN02528  153 -------------VVKDSSSAeEATIAEQEEFSTSVSTPtEQSYEDKT---IPLRGFQRAMVKTMTAAAK-VPHFHYVEE 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 247 CDLGAVLKARQSL----VRDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPK--QLPFIDISVAVATDKGLITPIIKD 320
Cdd:PLN02528  216 INVDALVELKASFqennTDPTVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEirLKGSHNIGVAMATEHGLVVPNIKN 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 321 AAAKGIREIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGRFRpvlKLTR-DEEGNA 399
Cdd:PLN02528  296 VQSLSLLEITKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQ---KVPRfVDDGNV 372
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 1435033878 400 QLQRhqLITVTMSSDSRVVDDELATRFLESFKANLENPIRL 440
Cdd:PLN02528  373 YPAS--IMTVTIGADHRVLDGATVARFCNEWKSYVEKPELL 411
PRK14843 PRK14843
dihydrolipoamide acetyltransferase; Provisional
121-440 2.57e-40

dihydrolipoamide acetyltransferase; Provisional


Pssm-ID: 184847 [Multi-domain]  Cd Length: 347  Bit Score: 147.36  E-value: 2.57e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 121 QFRLSPAARNILEKHSLDASQGTATGPRGIFTKEDALKLVqlketgkitesrptPAPLATPAVPLPPQAMATppytrpmi 200
Cdd:PRK14843   48 VVRISPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALL--------------PENIENDSIKSPAQIEKV-------- 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 201 ppVSTPGQPNVVGTFTEIPASNIRRVIAKRLTESKSTVPHAYATTDCDLGAVLKARQSLVrDDI------KVSVNDFIIK 274
Cdd:PRK14843  106 --EEVPDNVTPYGEIERIPMTPMRKVIAQRMVESYLTAPTFTLNYEVDMTEMLALRKKVL-EPImeatgkKTTVTDLLSL 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 275 AAAVTLKQMPDVNVSWDGEGPKQLP--FIDISVAVATDKGLITPIIKDAAAKGIREIADSVKALSKKARDGKLLPEEYQG 352
Cdd:PRK14843  183 AVVKTLMKHPYINASLTEDGKTIIThnYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQN 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 353 GSFSISNLGMFGIDEFTAVINPPQACILAVGRF--RPVLKltrdeegNAQLQRHQLITVTMSSDSRVVDDELATRFLESF 430
Cdd:PRK14843  263 STFTISNLGMFGVQSFGPIINQPNSAILGVSSTieKPVVV-------NGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDL 335
                         330
                  ....*....|
gi 1435033878 431 KANLENPIRL 440
Cdd:PRK14843  336 KELIETPISM 345
PLN02226 PLN02226
2-oxoglutarate dehydrogenase E2 component
1-440 5.43e-38

2-oxoglutarate dehydrogenase E2 component


Pssm-ID: 177871 [Multi-domain]  Cd Length: 463  Bit Score: 143.74  E-value: 5.43e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878   1 MPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSkNIRLGALIGLLVEEGEDWKH 80
Cdd:PLN02226   96 VPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGD-TVEPGTKVAIISKSEDAASQ 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878  81 VEiPKDVGPPSPASKPSVPC-PSPEPQIstavekehipgklqfrlspaarnilekhsldasqgtatgprgiftkedalkl 159
Cdd:PLN02226  175 VT-PSQKIPETTDPKPSPPAeDKQKPKV---------------------------------------------------- 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 160 vqlkETGKITESRPTPAPlatpavPLPPQAMATppytRPMIPPVSTPgqpnvvgtfTEIPASNIRRVIAKRLTESKSTVP 239
Cdd:PLN02226  202 ----ESAPVAEKPKAPSS------PPPPKQSAK----EPQLPPKERE---------RRVPMTRLRKRVATRLKDSQNTFA 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 240 HAYATTDCDLGAVLKARQS-----LVRDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPKQLPFIDISVAVATDKGLI 314
Cdd:PLN02226  259 LLTTFNEVDMTNLMKLRSQykdafYEKHGVKLGLMSGFIKAAVSALQHQPVVNAVIDGDDIIYRDYVDISIAVGTSKGLV 338
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 315 TPIIKDAAAKGIREIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGRF--RPVLKlt 392
Cdd:PLN02226  339 VPVIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIvsRPMVV-- 416
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 1435033878 393 rdeeGNAQLQRhQLITVTMSSDSRVVDDELATRFLESFKANLENPIRL 440
Cdd:PLN02226  417 ----GGSVVPR-PMMYVALTYDHRLIDGREAVYFLRRVKDVVEDPQRL 459
PRK11857 PRK11857
dihydrolipoamide acetyltransferase; Reviewed
125-437 7.90e-34

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237002 [Multi-domain]  Cd Length: 306  Bit Score: 128.76  E-value: 7.90e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 125 SPAARNILEKHSLDASQGTATGPRGIFTKEDALKLVqlketgKITESRPTPAPLATpaVPLPPQAMATPPytrPMIPPVS 204
Cdd:PRK11857    5 TPIARALAKKLGIDISLLKGSGRDGKILAEDVENFI------KSLKSAPTPAEAAS--VSSAQQAAKTAA---PAAAPPK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 205 TPGQPNVVGTfteipasnIRRVIAKRLTESKSTVPHAYATTDCDLGAVLKARQSLVRD-----DIKVSVNDFIIKAAAVT 279
Cdd:PRK11857   74 LEGKREKVAP--------IRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPvlkteGVKLTFLPFIAKAILIA 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 280 LKQMPDVNVSWDgEGPKQLPF---IDISVAVATDKGLITPIIKDAAAKGIREIADSVKALSKKARDGKLLPEEYQGGSFS 356
Cdd:PRK11857  146 LKEFPIFAAKYD-EATSELVYpdtLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFT 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878 357 ISNLGMFGIDEFTAVINPPQACILAVGRF--RPVLKltrdeegNAQLQRHQLITVTMSSDSRVVDDELATRFLESFKANL 434
Cdd:PRK11857  225 ITNYGSVGSLYGVPVINYPELAIAGVGAIidKAIVK-------NGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELL 297

                  ...
gi 1435033878 435 ENP 437
Cdd:PRK11857  298 EKP 300
PRK11892 PRK11892
pyruvate dehydrogenase subunit beta; Provisional
1-110 5.34e-32

pyruvate dehydrogenase subunit beta; Provisional


Pssm-ID: 237011 [Multi-domain]  Cd Length: 464  Bit Score: 126.96  E-value: 5.34e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878   1 MPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKNIRLGALIGLLVEEGEDWKH 80
Cdd:PRK11892    7 MPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEGVKVNTPIAVLLEEGESASD 86
                          90       100       110
                  ....*....|....*....|....*....|
gi 1435033878  81 VEIPKDVGPPSPASKPSVPCPSPEPQISTA 110
Cdd:PRK11892   87 AGAAPAAAAEAAAAAPAAAAAAAAKKAAPA 116
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
1-71 4.07e-26

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: 100.56  E-value: 4.07e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1435033878   1 MPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnIRLGALIGLL 71
Cdd:cd06849     5 MPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAVI 74
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
1-72 2.82e-23

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: 92.82  E-value: 2.82e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1435033878   1 MPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnIRLGALIGLLV 72
Cdd:COG0508     7 MPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDT-VPVGAVIAVIA 77
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
1-75 2.64e-17

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 83.07  E-value: 2.64e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1435033878   1 MPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSkNIRLGALIGLLVEEG 75
Cdd:PRK14875    7 MPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGE-TLPVGALLAVVADAE 80
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
1-60 4.15e-14

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: 66.85  E-value: 4.15e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878   1 MPSLSPTMEEGnIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSK 60
Cdd:pfam00364   5 SPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDT 63
Biotinyl_lipoyl_domains cd06663
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ...
2-60 7.82e-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: 66.31  E-value: 7.82e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1435033878   2 PSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSK 60
Cdd:cd06663     5 PDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTK 63
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
125-383 6.77e-12

multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 67.61  E-value: 6.77e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878  125 SPAARNILEK-HSLDASQGTATGPRGIFTKEDALKLVQLKETGKITESRPTPAPLATPAVPLPPQAMATPPYTRPMIPPV 203
Cdd:PRK12270    26 DPSWREFFADyGPGSTAAPTAAAAAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAAPPKPAAAAAAAAAPAAPPAAAAA 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878  204 STPGQPNVVGTFTeiPASNIRRVIAKRLTESKStVPhaYATTDCDLGAVLKARQSLVRDD-------IKVSVNDFIIKAA 276
Cdd:PRK12270   106 AAPAAAAVEDEVT--PLRGAAAAVAKNMDASLE-VP--TATSVRAVPAKLLIDNRIVINNhlkrtrgGKVSFTHLIGYAL 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878  277 AVTLKQMPDVNVSWDGEGPKqlPFI----DISVAVATD-------KGLITPIIKDAAAKGIREIADSVKALSKKARDGKL 345
Cdd:PRK12270   181 VQALKAFPNMNRHYAEVDGK--PTLvtpaHVNLGLAIDlpkkdgsRQLVVPAIKGAETMDFAQFWAAYEDIVRRARDGKL 258
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1435033878  346 LPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVG 383
Cdd:PRK12270   259 TADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVG 296
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
11-59 1.04e-08

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: 51.65  E-value: 1.04e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1435033878  11 GNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGS 59
Cdd:cd06850     8 GTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGD 56
E3_binding pfam02817
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ...
123-157 1.29e-04

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: 38.82  E-value: 1.29e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1435033878 123 RLSPAARNILEKHSLDASQGTATGPRGIFTKEDAL 157
Cdd:pfam02817   2 LASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
PHA03247 PHA03247
large tegument protein UL36; Provisional
84-209 3.66e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 3.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435033878   84 PKDVGPPSPASKPSVPCPSPEP-QISTAVEKEHIPGKlQFRLSPAARnilekhsldASQGTATGPRGIFTKEDALKLVQl 162
Cdd:PHA03247  2824 PAGPLPPPTSAQPTAPPPPPGPpPPSLPLGGSVAPGG-DVRRRPPSR---------SPAAKPAAPARPPVRRLARPAVS- 2892
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1435033878  163 KETGKITESRPTPAPLATPAVPLPPQAMATPPYTRPMIPPVSTPGQP 209
Cdd:PHA03247  2893 RSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRP 2939
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
11-60 1.48e-03

Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440660 [Multi-domain]  Cd Length: 1144  Bit Score: 41.22  E-value: 1.48e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1435033878   11 GNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSK 60
Cdd:COG1038   1085 GTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQ 1134
PRK09282 PRK09282
pyruvate carboxylase subunit B; Validated
11-58 2.97e-03

pyruvate carboxylase subunit B; Validated


Pssm-ID: 236449 [Multi-domain]  Cd Length: 592  Bit Score: 39.83  E-value: 2.97e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1435033878  11 GNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEG 58
Cdd:PRK09282  531 GTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEG 578
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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