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Conserved domains on  [gi|1949640283|ref|NP_001128496|]
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pyruvate dehydrogenase protein X component, mitochondrial isoform 2 [Homo sapiens]

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 1.41e-136

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: 399.17  E-value: 1.41e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283   1 MPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKNIRLGSLIGLIVEEGED--- 77
Cdd:TIGR01349   4 MPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKEDvad 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283  78 ----------WKHVEIPKDVGPPPPVS--KPSEPRPSPEPQISIPVKKEHIPGTLRFRLSPAARNILEKHSLDASQGTAT 145
Cdd:TIGR01349  84 afknyklessASPAPKPSEIAPTAPPSapKPSPAPQKQSPEPSSPAPLSDKESGDRIFASPLAKKLAKEKGIDLSAVAGS 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283 146 GPRGIFTKEDALKLVQLKQTgkitesrptpaptatptaPSPLQATAGPSYPRPVIPPVSTpgqpnavGTFTEIPASNIRR 225
Cdd:TIGR01349 164 GPNGRIVKKDIESFVPQSPA------------------SANQQAAATTPATYPAAAPVST-------GSYEDVPLSNIRK 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283 226 VIAKRLTESKSTVPHAYATADCDLGAVLKVRQDLVK---DDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPKQLPFID 302
Cdd:TIGR01349 219 IIAKRLLESKQTIPHYYVSIECNVDKLLALRKELNAmasEVYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYKNVD 298

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283 303 ISVAVATDKGLLTPIIKDAAAKGIQEIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAV 382
Cdd:TIGR01349 299 ISVAVATPDGLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAV 378

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1949640283 383 GRFRPVLKLTEDEEGNAKLQqrQLITVTMSSDSRVVDDELATRFLKSFKANLENPIRL 440
Cdd:TIGR01349 379 GAVEDVAVVDNDEEKGFAVA--SIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEM 434
 
Name Accession Description Interval E-value
PDHac_trf_mito TIGR01349
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 1-440 1.41e-136

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: 399.17  E-value: 1.41e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283   1 MPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKNIRLGSLIGLIVEEGED--- 77
Cdd:TIGR01349   4 MPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKEDvad 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283  78 ----------WKHVEIPKDVGPPPPVS--KPSEPRPSPEPQISIPVKKEHIPGTLRFRLSPAARNILEKHSLDASQGTAT 145
Cdd:TIGR01349  84 afknyklessASPAPKPSEIAPTAPPSapKPSPAPQKQSPEPSSPAPLSDKESGDRIFASPLAKKLAKEKGIDLSAVAGS 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283 146 GPRGIFTKEDALKLVQLKQTgkitesrptpaptatptaPSPLQATAGPSYPRPVIPPVSTpgqpnavGTFTEIPASNIRR 225
Cdd:TIGR01349 164 GPNGRIVKKDIESFVPQSPA------------------SANQQAAATTPATYPAAAPVST-------GSYEDVPLSNIRK 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283 226 VIAKRLTESKSTVPHAYATADCDLGAVLKVRQDLVK---DDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPKQLPFID 302
Cdd:TIGR01349 219 IIAKRLLESKQTIPHYYVSIECNVDKLLALRKELNAmasEVYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYKNVD 298

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283 303 ISVAVATDKGLLTPIIKDAAAKGIQEIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAV 382
Cdd:TIGR01349 299 ISVAVATPDGLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAV 378

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1949640283 383 GRFRPVLKLTEDEEGNAKLQqrQLITVTMSSDSRVVDDELATRFLKSFKANLENPIRL 440
Cdd:TIGR01349 379 GAVEDVAVVDNDEEKGFAVA--SIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEM 434
PRK11856 PRK11856
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
 1-440 2.41e-133

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


Pssm-ID: 237001 [Multi-domain]  Cd Length: 411  Bit Score: 389.92  E-value: 2.41e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283   1 MPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnIRLGSLIGLIVEEGEdwKH 80
Cdd:PRK11856    7 MPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDV-VPVGSVIAVIEEEGE--AE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283  81 VEIPKDVGPPPPVSKPSEPRPSPEPQISIPVKKEHIPGTLRFRLSPAARNILEKHSLDASQGTATGPRGIFTKEDalklV 160
Cdd:PRK11856   84 AAAAAEAAPEAPAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKED----V 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283 161 QlkqtgkitesrptpaptatptapsplQATAGPSYPRPVIPPVSTPGQPNAVGTFTEIPASNIRRVIAKRLTESKSTVPH 240
Cdd:PRK11856  160 E--------------------------AAAAAAAPAAAAAAAAAAAPPAAAAEGEERVPLSGMRKAIAKRMVESKREIPH 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283 241 AYATADCDLGAVLKVRQDLVKDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPKQLPFIDISVAVATDKGLLTPIIKD 320
Cdd:PRK11856  214 FTLTDEVDVTALLALRKQLKAIGVKLTVTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVATDGGLIVPVIRD 293

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283 321 AAAKGIQEIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGRF--RPVLKltedeegN 398
Cdd:PRK11856  294 ADKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIveRPVVV-------D 366

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 1949640283 399 AKLQQRQLITVTMSSDSRVVDDELATRFLKSFKANLENPIRL 440
Cdd:PRK11856  367 GEIVVRKVMPLSLSFDHRVIDGADAARFLKALKELLENPALL 408
2-oxoacid_dh pfam00198
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ...
 231-440 6.53e-83

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: 253.62  E-value: 6.53e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283 231 LTESKSTVPHAYATADCDLGAVLKVRQDL----VKDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPK--QLPFIDIS 304
Cdd:pfam00198   1 MTESKQTIPHFTLTDEVDVTELLALREELkedaADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEivYKKYVNIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283 305 VAVATDKGLLTPIIKDAAAKGIQEIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGR 384
Cdd:pfam00198  81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1949640283 385 FRPVLKLTEDEegnakLQQRQLITVTMSSDSRVVDDELATRFLKSFKANLENPIRL 440
Cdd:pfam00198 161 IRKRPVVVDGE-----IVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELL 211
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 1-71 4.65e-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: 100.17  E-value: 4.65e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1949640283   1 MPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnIRLGSLIGLI 71
Cdd:cd06849     5 MPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAVI 74
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 1-72 1.90e-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: 93.21  E-value: 1.90e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1949640283   1 MPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnIRLGSLIGLIV 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 1.41e-136

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: 399.17  E-value: 1.41e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283   1 MPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKNIRLGSLIGLIVEEGED--- 77
Cdd:TIGR01349   4 MPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKEDvad 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283  78 ----------WKHVEIPKDVGPPPPVS--KPSEPRPSPEPQISIPVKKEHIPGTLRFRLSPAARNILEKHSLDASQGTAT 145
Cdd:TIGR01349  84 afknyklessASPAPKPSEIAPTAPPSapKPSPAPQKQSPEPSSPAPLSDKESGDRIFASPLAKKLAKEKGIDLSAVAGS 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283 146 GPRGIFTKEDALKLVQLKQTgkitesrptpaptatptaPSPLQATAGPSYPRPVIPPVSTpgqpnavGTFTEIPASNIRR 225
Cdd:TIGR01349 164 GPNGRIVKKDIESFVPQSPA------------------SANQQAAATTPATYPAAAPVST-------GSYEDVPLSNIRK 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283 226 VIAKRLTESKSTVPHAYATADCDLGAVLKVRQDLVK---DDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPKQLPFID 302
Cdd:TIGR01349 219 IIAKRLLESKQTIPHYYVSIECNVDKLLALRKELNAmasEVYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYKNVD 298

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283 303 ISVAVATDKGLLTPIIKDAAAKGIQEIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAV 382
Cdd:TIGR01349 299 ISVAVATPDGLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAV 378

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1949640283 383 GRFRPVLKLTEDEEGNAKLQqrQLITVTMSSDSRVVDDELATRFLKSFKANLENPIRL 440
Cdd:TIGR01349 379 GAVEDVAVVDNDEEKGFAVA--SIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEM 434
PRK11856 PRK11856
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
 1-440 2.41e-133

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


Pssm-ID: 237001 [Multi-domain]  Cd Length: 411  Bit Score: 389.92  E-value: 2.41e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283   1 MPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnIRLGSLIGLIVEEGEdwKH 80
Cdd:PRK11856    7 MPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDV-VPVGSVIAVIEEEGE--AE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283  81 VEIPKDVGPPPPVSKPSEPRPSPEPQISIPVKKEHIPGTLRFRLSPAARNILEKHSLDASQGTATGPRGIFTKEDalklV 160
Cdd:PRK11856   84 AAAAAEAAPEAPAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKED----V 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283 161 QlkqtgkitesrptpaptatptapsplQATAGPSYPRPVIPPVSTPGQPNAVGTFTEIPASNIRRVIAKRLTESKSTVPH 240
Cdd:PRK11856  160 E--------------------------AAAAAAAPAAAAAAAAAAAPPAAAAEGEERVPLSGMRKAIAKRMVESKREIPH 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283 241 AYATADCDLGAVLKVRQDLVKDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPKQLPFIDISVAVATDKGLLTPIIKD 320
Cdd:PRK11856  214 FTLTDEVDVTALLALRKQLKAIGVKLTVTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVATDGGLIVPVIRD 293

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283 321 AAAKGIQEIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGRF--RPVLKltedeegN 398
Cdd:PRK11856  294 ADKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIveRPVVV-------D 366

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 1949640283 399 AKLQQRQLITVTMSSDSRVVDDELATRFLKSFKANLENPIRL 440
Cdd:PRK11856  367 GEIVVRKVMPLSLSFDHRVIDGADAARFLKALKELLENPALL 408
PLN02744 PLN02744
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
 1-437 2.98e-108

dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex


Pssm-ID: 215397 [Multi-domain]  Cd Length: 539  Bit Score: 330.28  E-value: 2.98e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283   1 MPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKNIRLGSLIGLIVEEGED--- 77
Cdd:PLN02744  117 MPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKEIKVGEVIAITVEEEEDigk 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283  78 WKHVEIPKDVGPPPPVSKPS---EPRPSPEPQISIPVKKEHIPGTL-----RFRLSPAARNILEKHSLDASQGTATGPRG 149
Cdd:PLN02744  197 FKDYKPSSSAAPAAPKAKPSpppPKEEEVEKPASSPEPKASKPSAPpssgdRIFASPLARKLAEDNNVPLSSIKGTGPDG 276

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283 150 IFTKEDALKLvqLKQTGKitesrptpaptatptapsplQATAGPSYPRPvIPPVStpgqpnavgtFTEIPASNIRRVIAK 229
Cdd:PLN02744  277 RIVKADIEDY--LASGGK--------------------GATAPPSTDSK-APALD----------YTDIPNTQIRKVTAS 323

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283 230 RLTESKSTVPHAYATADCDLGAVLKVRQDL-----VKDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPKQLPFIDIS 304
Cdd:PLN02744  324 RLLQSKQTIPHYYLTVDTRVDKLMALRSQLnslqeASGGKKISVNDLVIKAAALALRKVPQCNSSWTDDYIRQYHNVNIN 403

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283 305 VAVATDKGLLTPIIKDAAAKGIQEIADSVKALSKKARDGKLLPEEYQGGSFSISNL-GMFGIDEFTAVINPPQACILAVG 383
Cdd:PLN02744  404 VAVQTENGLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLgGPFGIKQFCAIINPPQSAILAVG 483

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1949640283 384 RF--RPVLKLTEDEEGNAklqqrQLITVTMSSDSRVVDDELATRFLKSFKANLENP 437
Cdd:PLN02744  484 SAekRVIPGSGPDQYNFA-----SFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENP 534
2-oxoacid_dh pfam00198
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ...
 231-440 6.53e-83

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: 253.62  E-value: 6.53e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283 231 LTESKSTVPHAYATADCDLGAVLKVRQDL----VKDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPK--QLPFIDIS 304
Cdd:pfam00198   1 MTESKQTIPHFTLTDEVDVTELLALREELkedaADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEivYKKYVNIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283 305 VAVATDKGLLTPIIKDAAAKGIQEIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGR 384
Cdd:pfam00198  81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1949640283 385 FRPVLKLTEDEegnakLQQRQLITVTMSSDSRVVDDELATRFLKSFKANLENPIRL 440
Cdd:pfam00198 161 IRKRPVVVDGE-----IVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELL 211
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 10-441 8.41e-70

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 230.48  E-value: 8.41e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283  10 EGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnIRLGSLIGLIVEEGEDWKHVEIPKDVGP 89
Cdd:PRK11855  132 EVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDK-VSVGSLLVVIEVAAAAPAAAAAPAAAAP 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283  90 PPPVSKPSEPRPSPEPQISIPVKKEHIPGTLRFRLSPAARNILEKHSLDASQGTATGPRGIFTKEDALKLVQLKQTGKit 169
Cdd:PRK11855  211 AAAAAAAPAPAPAAAAAPAAAAPAAAAAPGKAPHASPAVRRLARELGVDLSQVKGTGKKGRITKEDVQAFVKGAMSAA-- 288

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283 170 esrptpaptatPTAPSPLQATAGPSYPRPVIPPVSTpgqpNAVGTFTEIPASNIRRVIAKRLTESKSTVPHAYATADCDL 249
Cdd:PRK11855  289 -----------AAAAAAAAAAGGGGLGLLPWPKVDF----SKFGEIETKPLSRIKKISAANLHRSWVTIPHVTQFDEADI 353

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283 250 GAVLKVR----QDLVKDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGpKQLPF---IDISVAVATDKGLLTPIIKDAA 322
Cdd:PRK11855  354 TDLEALRkqlkKEAEKAGVKLTMLPFFIKAVVAALKEFPVFNASLDEDG-DELTYkkyFNIGFAVDTPNGLVVPVIKDVD 432

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283 323 AKGIQEIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGRF--RPVlklTEDEEgnak 400
Cdd:PRK11855  433 KKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSqmKPV---WDGKE---- 505

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 1949640283 401 LQQRQLITVTMSSDSRVVDDELATRFLKSFKANLENPIRLA 441
Cdd:PRK11855  506 FVPRLMLPLSLSYDHRVIDGATAARFTNYLKQLLADPRRML 546
sucB TIGR01347
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ...
 2-441 9.88e-70

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: 226.54  E-value: 9.88e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283   2 PSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnirlgsligliVEEGEDWKHV 81
Cdd:TIGR01347   6 PELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDT-----------VESGQVLAIL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283  82 EIPKDVGPPPP----VSKPSEPRPSPEPQISIPVKKEHipgtlrfrLSPAARNILEKHSLDASQGTATGPRGIFTKEDAL 157
Cdd:TIGR01347  75 EEGNDATAAPPaksgEEKEETPAASAAAAPTAAANRPS--------LSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDII 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283 158 KlvqlkqtgkitesrptpaptatptapsplqATAGPSYPRPVIPPVSTPGQPNAVGTFTEIPASNIRRVIAKRLTESKST 237
Cdd:TIGR01347 147 K------------------------------KTEAPASAQPPAAAAAAAAPAAATRPEERVKMTRLRQRIAERLKEAQNS 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283 238 VPHAYATADCDLGAVLKVR-----QDLVKDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPKQLPFIDISVAVATDKG 312
Cdd:TIGR01347 197 TAMLTTFNEVDMSAVMELRkrykeEFEKKHGVKLGFMSFFVKAVVAALKRFPEVNAEIDGDDIVYKDYYDISVAVSTDRG 276

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283 313 LLTPIIKDAAAKGIQEIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGRF--RPVLK 390
Cdd:TIGR01347 277 LVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIkeRPVAV 356

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1949640283 391 ltedeegNAKLQQRQLITVTMSSDSRVVDDELATRFLKSFKANLENPIRLA 441
Cdd:TIGR01347 357 -------NGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRRLL 400
PRK05704 PRK05704
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
2-440 4.47e-69

2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;


Pssm-ID: 235571 [Multi-domain]  Cd Length: 407  Bit Score: 224.71  E-value: 4.47e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283   2 PSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSkNIRLGSLIGLIVEEGEdwkhv 81
Cdd:PRK05704    8 PTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGD-TVTVGQVLGRIDEGAA----- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283  82 eipkdVGPPPPVSKPSEPRPSPEPQISIPVKKEHIPGTLrfrlSPAARNILEKHSLDASQGTATGPRGIFTKEDALKLVQ 161
Cdd:PRK05704   82 -----AGAAAAAAAAAAAAAAAPAQAQAAAAAEQSNDAL----SPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAALA 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283 162 lkqtgkitesrptpaptatptapSPLQATAGPSYPRPVIPPVSTPGQPNavgtfTEIPASNIRRVIAKRLTESKSTvpha 241
Cdd:PRK05704  153 -----------------------AAAAAPAAPAAAAPAAAPAPLGARPE-----ERVPMTRLRKTIAERLLEAQNT---- 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283 242 yaTA------DCDLGAVLKVR---QDLV--KDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPKQLPFIDISVAVATD 310
Cdd:PRK05704  201 --TAmlttfnEVDMTPVMDLRkqyKDAFekKHGVKLGFMSFFVKAVVEALKRYPEVNASIDGDDIVYHNYYDIGIAVGTP 278

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283 311 KGLLTPIIKDAAAKGIQEIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGRF--RPV 388
Cdd:PRK05704  279 RGLVVPVLRDADQLSFAEIEKKIAELAKKARDGKLSIEELTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHKIkeRPV 358

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1949640283 389 LKltedeegNAKLQQRQLITVTMSSDSRVVDDELATRFLKSFKANLENPIRL 440
Cdd:PRK05704  359 AV-------NGQIVIRPMMYLALSYDHRIIDGKEAVGFLVTIKELLEDPERL 403
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 10-440 3.48e-54

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 190.60  E-value: 3.48e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283  10 EGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnIRLGSLIGLIVEEGEDWKHVEIPKDVGP 89
Cdd:PRK11854  218 EVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDK-VKTGSLIMRFEVEGAAPAAAPAKQEAAA 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283  90 PPPVSKPSEPRPSPEPQiSIPVKKEHIPGTLRFRLSPAARNILEKHSLDASQGTATGPRGIFTKEDALKLVqlKQTGKIT 169
Cdd:PRK11854  297 PAPAAAKAEAPAAAPAA-KAEGKSEFAENDAYVHATPLVRRLAREFGVNLAKVKGTGRKGRILKEDVQAYV--KDAVKRA 373

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283 170 ESrptpaptatptaPSPLQATAGPSYPRPVIPPVStpgqPNAVGTFTEIPASNIRRVIAKRLTESKSTVPHA--YATADC 247
Cdd:PRK11854  374 EA------------APAAAAAGGGGPGLLPWPKVD----FSKFGEIEEVELGRIQKISGANLHRNWVMIPHVtqFDKADI 437

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283 248 DLGAVLKVRQDLV----KDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGpKQL---PFIDISVAVATDKGLLTPIIKD 320
Cdd:PRK11854  438 TELEAFRKQQNAEaekrKLGVKITPLVFIMKAVAAALEQMPRFNSSLSEDG-QRLtlkKYVNIGIAVDTPNGLVVPVFKD 516

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283 321 AAAKGIQEIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGR--FRPVlkltedeEGN 398
Cdd:PRK11854  517 VNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKsaMEPV-------WNG 589

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 1949640283 399 AKLQQRQLITVTMSSDSRVVDDELATRFLKSFKANLENPIRL 440
Cdd:PRK11854  590 KEFAPRLMLPLSLSYDHRVIDGADGARFITIINDRLSDIRRL 631
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 9-440 5.70e-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: 183.15  E-value: 5.70e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283   9 EEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnIRLGSLIGLIVEEGEDWKHVEIPKDVG 88
Cdd:TIGR01348 128 EKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDS-VPTGDLILTLSVAGSTPATAPAPASAQ 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283  89 PPPPVSKPSEPRP-----SPEPQISIPVKKEHIPGTLRFRLSPAARNILEKHSLDASQGTATGPRGIFTKEDALKLVqlK 163
Cdd:TIGR01348 207 PAAQSPAATQPEPaaapaAAKAQAPAPQQAGTQNPAKVDHAAPAVRRLAREFGVDLSAVKGTGIKGRILREDVQRFV--K 284

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283 164 QTGKITESrptpaptatptapsplqATAGPSYPRPVIPPVstpgqPNA----VGTFTEIPASNIRRVIAKRLTESKSTVP 239
Cdd:TIGR01348 285 EPSVRAQA-----------------AAASAAGGAPGALPW-----PNVdfskFGEVEEVDMSRIRKISGANLTRNWTMIP 342

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283 240 HA--YATADCDLGAVLKVRQDLV--KDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDgEGPKQL---PFIDISVAVATDKG 312
Cdd:TIGR01348 343 HVthFDKADITEMEAFRKQQNAAveKEGVKLTVLHILMKAVAAALKKFPKFNASLD-LGGEQLilkKYVNIGVAVDTPNG 421

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283 313 LLTPIIKDAAAKGIQEIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGR--FRPVLK 390
Cdd:TIGR01348 422 LLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKsgMEPVWN 501

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 1949640283 391 LTEdeegnakLQQRQLITVTMSSDSRVVDDELATRFLKSFKANLENPIRL 440
Cdd:TIGR01348 502 GKE-------FEPRLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRL 544
PTZ00144 PTZ00144
dihydrolipoamide succinyltransferase; Provisional
 2-440 1.63e-49

dihydrolipoamide succinyltransferase; Provisional


Pssm-ID: 240289 [Multi-domain]  Cd Length: 418  Bit Score: 173.72  E-value: 1.63e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283   2 PSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSknirlgsliglIVEEGEDWkhV 81
Cdd:PTZ00144   50 PTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGD-----------TVEVGAPL--S 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283  82 EIPKDVGPPPPvskpseprpspepqisIPVKKEHIPGTLRFRLSPAARNIlekhsldasqgtatgprgiftkedalklvq 161
Cdd:PTZ00144  117 EIDTGGAPPAA----------------APAAAAAAKAEKTTPEKPKAAAP------------------------------ 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283 162 lKQTGKITESrptpaptatPTAPSPLQATAGPSYPRPVIPPVSTPGQPNavgtfTEIPASNIRRVIAKRLTESKSTVPHA 241
Cdd:PTZ00144  151 -TPEPPAASK---------PTPPAAAKPPEPAPAAKPPPTPVARADPRE-----TRVPMSRMRQRIAERLKASQNTCAML 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283 242 YATADCDLGAVLKVRQDL-----VKDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPKQLPFIDISVAVATDKGLLTP 316
Cdd:PTZ00144  216 TTFNECDMSALMELRKEYkddfqKKHGVKLGFMSAFVKASTIALKKMPIVNAYIDGDEIVYRNYVDISVAVATPTGLVVP 295

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283 317 IIKDAAAKGIQEIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACIL---AVGRfRPVLKlte 393
Cdd:PTZ00144  296 VIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILgmhAIKK-RPVVV--- 371

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 1949640283 394 deegNAKLQQRQLITVTMSSDSRVVDDELATRFLKSFKANLENPIRL 440
Cdd:PTZ00144  372 ----GNEIVIRPIMYLALTYDHRLIDGRDAVTFLKKIKDLIEDPARM 414
PLN02528 PLN02528
2-oxoisovalerate dehydrogenase E2 component
 10-440 5.62e-45

2-oxoisovalerate dehydrogenase E2 component


Pssm-ID: 215289 [Multi-domain]  Cd Length: 416  Bit Score: 161.43  E-value: 5.62e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283  10 EGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnIRLG-SLIGLIVEEGEDWKHVEIPKDVG 88
Cdd:PLN02528   12 ECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDI-VKVGeTLLKIMVEDSQHLRSDSLLLPTD 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283  89 PPPPVSKPSEPrpspepqisipVKKEHIPGTLRfrlSPAARNILEKHSLDASQGTATGPRGIFTKEDALKLVQLKQTGKI 168
Cdd:PLN02528   91 SSNIVSLAESD-----------ERGSNLSGVLS---TPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAAQKGVVKD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283 169 TESRPTPAPTATPTAPSPLQATAGPSYPRPVippvstpgqpnavgtfteIPASNIRRVIAKRLTESKStVPHAYATADCD 248
Cdd:PLN02528  157 SSSAEEATIAEQEEFSTSVSTPTEQSYEDKT------------------IPLRGFQRAMVKTMTAAAK-VPHFHYVEEIN 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283 249 LGAVLKVRQDL----VKDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPK--QLPFIDISVAVATDKGLLTPIIKDAA 322
Cdd:PLN02528  218 VDALVELKASFqennTDPTVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEirLKGSHNIGVAMATEHGLVVPNIKNVQ 297

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283 323 AKGIQEIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGRFRPVLKLTEDEE-GNAKl 401
Cdd:PLN02528  298 SLSLLEITKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPRFVDDGNvYPAS- 376

                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 1949640283 402 qqrqLITVTMSSDSRVVDDELATRFLKSFKANLENPIRL 440
Cdd:PLN02528  377 ----IMTVTIGADHRVLDGATVARFCNEWKSYVEKPELL 411
SucB_Actino TIGR02927
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ...
 1-435 7.96e-43

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: 159.02  E-value: 7.96e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283   1 MPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEgSKNIRLGSLIGLIVEEG----E 76
Cdd:TIGR02927 131 MPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPE-DDTVEVGTVLAIIGDANaapaE 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283  77 DWKHVEIPKDVGPPPPVSKPSEPRPSPEPQISIPVKKEHIP-----------GTLRFRLSPAARNILEKHSLDASQGTAT 145
Cdd:TIGR02927 210 PAEEEAPAPSEAGSEPAPDPAARAPHAAPDPPAPAPAPAKTaapaaaapvssGDSGPYVTPLVRKLAKDKGVDLSTVKGT 289

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283 146 GPRGIFTKEDALKLVQlkqtgKITESRPTPAPTAtptapsplqATAGPSYPRPVIPPVStPGQPNAVGTFTEipASNIRR 225
Cdd:TIGR02927 290 GVGGRIRKQDVLAAAK-----AAEEARAAAAAPA---------AAAAPAAPAAAAKPAE-PDTAKLRGTTQK--MNRIRQ 352

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283 226 VIAKRLTESKSTVPHAYATADCDLGAVLKVRQD-----LVKDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGpKQLPF 300
Cdd:TIGR02927 353 ITADKTIESLQTSAQLTQVHEVDMTRVAALRARakndfLEKNGVNLTFLPFFVQAVTEALKAHPNVNASYNAET-KEVTY 431

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283 301 ID---ISVAVATDKGLLTPIIKDAAAKGIQEIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQA 377
Cdd:TIGR02927 432 HDvehVGIAVDTPRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDTPILNPPQA 511

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1949640283 378 CILAVGRFRPVLKLTEDEEGNAKLQQRQLITVTMSSDSRVVDDELATRFLKSFKANLE 435
Cdd:TIGR02927 512 AILGTGAIVKRPRVIKDEDGGESIAIRSVCYLPLTYDHRLVDGADAGRFLTTIKKRLE 569
PRK14843 PRK14843
dihydrolipoamide acetyltransferase; Provisional
 123-440 3.61e-42

dihydrolipoamide acetyltransferase; Provisional


Pssm-ID: 184847 [Multi-domain]  Cd Length: 347  Bit Score: 152.37  E-value: 3.61e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283 123 RLSPAARNILEKHSLDASQGTATGPRGIFTKEDALKLVqlkqtgkitesrptpaptatptapSPLQATAGPSYPRPVIPP 202
Cdd:PRK14843   50 RISPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALL------------------------PENIENDSIKSPAQIEKV 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283 203 VSTPGQPNAVGTFTEIPASNIRRVIAKRLTESKSTVPHAYATADCDLGAVLKVRQDLVkDDI------KVSVNDFIIKAA 276
Cdd:PRK14843  106 EEVPDNVTPYGEIERIPMTPMRKVIAQRMVESYLTAPTFTLNYEVDMTEMLALRKKVL-EPImeatgkKTTVTDLLSLAV 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283 277 AVTLKQMPDVNVSWDGEGPKQLP--FIDISVAVATDKGLLTPIIKDAAAKGIQEIADSVKALSKKARDGKLLPEEYQGGS 354
Cdd:PRK14843  185 VKTLMKHPYINASLTEDGKTIIThnYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNST 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283 355 FSISNLGMFGIDEFTAVINPPQACILAVGRF--RPVLKltedeegNAKLQQRQLITVTMSSDSRVVDDELATRFLKSFKA 432
Cdd:PRK14843  265 FTISNLGMFGVQSFGPIINQPNSAILGVSSTieKPVVV-------NGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKE 337


                  ....*...
gi 1949640283 433 NLENPIRL 440
Cdd:PRK14843  338 LIETPISM 345
PLN02226 PLN02226
2-oxoglutarate dehydrogenase E2 component
 1-440 1.51e-35

2-oxoglutarate dehydrogenase E2 component


Pssm-ID: 177871 [Multi-domain]  Cd Length: 463  Bit Score: 136.81  E-value: 1.51e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283   1 MPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSkNIRLGSLIGLIVEEGEDWKH 80
Cdd:PLN02226   96 VPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGD-TVEPGTKVAIISKSEDAASQ 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283  81 VEiPKDVGPPPPVSKPseprpspepqisipvkkehipgtlrfrlSPAARNILEkhsldasqgtatgPRgiftkedalklv 160
Cdd:PLN02226  175 VT-PSQKIPETTDPKP----------------------------SPPAEDKQK-------------PK------------ 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283 161 qlKQTGKITESrptpaptatptapsplqatagPSYPRPVIPPVSTPGQPNAVGTFTE--IPASNIRRVIAKRLTESKSTV 238
Cdd:PLN02226  201 --VESAPVAEK---------------------PKAPSSPPPPKQSAKEPQLPPKERErrVPMTRLRKRVATRLKDSQNTF 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283 239 PHAYATADCDLGAVLKVRQD-----LVKDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPKQLPFIDISVAVATDKGL 313
Cdd:PLN02226  258 ALLTTFNEVDMTNLMKLRSQykdafYEKHGVKLGLMSGFIKAAVSALQHQPVVNAVIDGDDIIYRDYVDISIAVGTSKGL 337

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283 314 LTPIIKDAAAKGIQEIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGRF--RPVLKl 391
Cdd:PLN02226  338 VVPVIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIvsRPMVV- 416

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 1949640283 392 tedeegNAKLQQRQLITVTMSSDSRVVDDELATRFLKSFKANLENPIRL 440
Cdd:PLN02226  417 ------GGSVVPRPMMYVALTYDHRLIDGREAVYFLRRVKDVVEDPQRL 459
PRK11857 PRK11857
dihydrolipoamide acetyltransferase; Reviewed
 125-437 1.26e-30

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237002 [Multi-domain]  Cd Length: 306  Bit Score: 119.90  E-value: 1.26e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283 125 SPAARNILEKHSLDASQGTATGPRGIFTKEDALKLVqlkqtgkitESRPTPAPTATPTAPSPLQATAgpSYPRPVIPPVS 204
Cdd:PRK11857    5 TPIARALAKKLGIDISLLKGSGRDGKILAEDVENFI---------KSLKSAPTPAEAASVSSAQQAA--KTAAPAAAPPK 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283 205 TPGQPNAVGTfteipasnIRRVIAKRLTESKSTVPHAYATADCDLGAVLKVRQDLVKD-----DIKVSVNDFIIKAAAVT 279
Cdd:PRK11857   74 LEGKREKVAP--------IRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPvlkteGVKLTFLPFIAKAILIA 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283 280 LKQMPDVNVSWDgEGPKQLPF---IDISVAVATDKGLLTPIIKDAAAKGIQEIADSVKALSKKARDGKLLPEEYQGGSFS 356
Cdd:PRK11857  146 LKEFPIFAAKYD-EATSELVYpdtLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFT 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283 357 ISNLGMFGIDEFTAVINPPQACILAVGRF--RPVLKltedeegNAKLQQRQLITVTMSSDSRVVDDELATRFLKSFKANL 434
Cdd:PRK11857  225 ITNYGSVGSLYGVPVINYPELAIAGVGAIidKAIVK-------NGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELL 297


                  ...
gi 1949640283 435 ENP 437
Cdd:PRK11857  298 EKP 300
PRK11892 PRK11892
pyruvate dehydrogenase subunit beta; Provisional
 1-77 5.63e-30

pyruvate dehydrogenase subunit beta; Provisional


Pssm-ID: 237011 [Multi-domain]  Cd Length: 464  Bit Score: 121.18  E-value: 5.63e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1949640283   1 MPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKNIRLGSLIGLIVEEGED 77
Cdd:PRK11892    7 MPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEGVKVNTPIAVLLEEGES 83
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 1-71 4.65e-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: 100.17  E-value: 4.65e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1949640283   1 MPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnIRLGSLIGLI 71
Cdd:cd06849     5 MPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAVI 74
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 1-72 1.90e-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: 93.21  E-value: 1.90e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1949640283   1 MPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnIRLGSLIGLIV 72
Cdd:COG0508     7 MPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDT-VPVGAVIAVIA 77
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 1-75 6.54e-17

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 81.91  E-value: 6.54e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1949640283   1 MPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSkNIRLGSLIGLIVEEG 75
Cdd:PRK14875    7 MPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGE-TLPVGALLAVVADAE 80
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 1-71 3.87e-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: 67.24  E-value: 3.87e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1949640283   1 MPSLSPTMEEGnIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnIRLGSLIGLI 71
Cdd:pfam00364   5 SPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDT-VEVGDPLAKI 73
Biotinyl_lipoyl_domains cd06663
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ...
 2-60 9.42e-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: 65.93  E-value: 9.42e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1949640283   2 PSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSK 60
Cdd:cd06663     5 PDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTK 63
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 11-59 1.27e-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: 51.26  E-value: 1.27e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1949640283  11 GNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGS 59
Cdd:cd06850     8 GTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGD 56
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
 185-428 1.74e-08

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


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 56.82  E-value: 1.74e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283  185 SPLQATAGPSYPRPVIPPVSTPGQPNAVGTFTEIPASNIR---RVIAKRLTESKStVPhaYATAdcdlgavlkVRQDLVK 261
Cdd:PRK12270    82 APPKPAAAAAAAAAPAAPPAAAAAAAPAAAAVEDEVTPLRgaaAAVAKNMDASLE-VP--TATS---------VRAVPAK 149

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283  262 --DDIKVSVNDF-------------IIKAAAV-TLKQMPDVNVSWDGEGPKqlPFI----DISVAVATD-------KGLL 314
Cdd:PRK12270   150 llIDNRIVINNHlkrtrggkvsfthLIGYALVqALKAFPNMNRHYAEVDGK--PTLvtpaHVNLGLAIDlpkkdgsRQLV 227

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949640283  315 TPIIKDAAAKGIQEIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGRFR-PVLKLTE 393
Cdd:PRK12270   228 VPAIKGAETMDFAQFWAAYEDIVRRARDGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAMEyPAEFQGA 307

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1949640283  394 DEEGNAKLQQRQLITVTMSSDSRVVDDELATRFLK 428
Cdd:PRK12270   308 SEERLAELGISKVMTLTSTYDHRIIQGAESGEFLR 342
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 1-75 5.64e-06

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 48.85  E-value: 5.64e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1949640283   1 MPSLSPTmeEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnIRLGSLIGLIVEEG 75
Cdd:PRK11854    7 VPDIGAD--EVEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDK-VETGALIMIFESAD 78
E3_binding pfam02817
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ...
 123-157 1.52e-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: 1.52e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1949640283 123 RLSPAARNILEKHSLDASQGTATGPRGIFTKEDAL 157
Cdd:pfam02817   2 LASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
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 1949640283   11 GNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSK 60
Cdd:COG1038   1085 GTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQ 1134
PRK09282 PRK09282
pyruvate carboxylase subunit B; Validated
 11-58 2.87e-03

pyruvate carboxylase subunit B; Validated


Pssm-ID: 236449 [Multi-domain]  Cd Length: 592  Bit Score: 39.83  E-value: 2.87e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1949640283  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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