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Conserved domains on  [gi|1743165004|ref|XP_003254454|]
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pyruvate dehydrogenase protein X component, mitochondrial isoform X1 [Nomascus leucogenys]

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

 Zoom to residue level

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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 ...
 58-500 5.44e-143

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: 417.66  E-value: 5.44e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004  58 KILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKNIRLGSLIGLIVEEGED 137
Cdd:TIGR01349   1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 138 ----WKHVEIPKDVGPPP------PVSKPSESRPSPEPQISIPVKKEHIPGTLQFR-----LSPAARSILEKHSLDASQG 202
Cdd:TIGR01349  81 vadaFKNYKLESSASPAPkpseiaPTAPPSAPKPSPAPQKQSPEPSSPAPLSDKESgdrifASPLAKKLAKEKGIDLSAV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 203 TATGPRGIFTKEDALKLVQLKQTgkitesrptpapaatptaPSPLQATAGPSYPRPVIPPVSTpgqpnavGTFTEIPASN 282
Cdd:TIGR01349 161 AGSGPNGRIVKKDIESFVPQSPA------------------SANQQAAATTPATYPAAAPVST-------GSYEDVPLSN 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 283 IRRVIAKRLTESKSTVPHAYATADCDLGAVLKVRQDLVK---DDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPKQLP 359
Cdd:TIGR01349 216 IRKIIAKRLLESKQTIPHYYVSIECNVDKLLALRKELNAmasEVYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYK 295

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 360 FIDISVAVATDKGLLTPIIKDAAAKGIQEIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACI 439
Cdd:TIGR01349 296 NVDISVAVATPDGLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACI 375

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1743165004 440 LAVGRFRPVLKLTEDEEGNAKLQqhQLITVTMSSDSRVVDDELATRFLKSFKANLENPIRL 500
Cdd:TIGR01349 376 LAVGAVEDVAVVDNDEEKGFAVA--SIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEM 434
 
Name Accession Description Interval E-value
PDHac_trf_mito TIGR01349
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 58-500 5.44e-143

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: 417.66  E-value: 5.44e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004  58 KILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKNIRLGSLIGLIVEEGED 137
Cdd:TIGR01349   1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 138 ----WKHVEIPKDVGPPP------PVSKPSESRPSPEPQISIPVKKEHIPGTLQFR-----LSPAARSILEKHSLDASQG 202
Cdd:TIGR01349  81 vadaFKNYKLESSASPAPkpseiaPTAPPSAPKPSPAPQKQSPEPSSPAPLSDKESgdrifASPLAKKLAKEKGIDLSAV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 203 TATGPRGIFTKEDALKLVQLKQTgkitesrptpapaatptaPSPLQATAGPSYPRPVIPPVSTpgqpnavGTFTEIPASN 282
Cdd:TIGR01349 161 AGSGPNGRIVKKDIESFVPQSPA------------------SANQQAAATTPATYPAAAPVST-------GSYEDVPLSN 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 283 IRRVIAKRLTESKSTVPHAYATADCDLGAVLKVRQDLVK---DDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPKQLP 359
Cdd:TIGR01349 216 IRKIIAKRLLESKQTIPHYYVSIECNVDKLLALRKELNAmasEVYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYK 295

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 360 FIDISVAVATDKGLLTPIIKDAAAKGIQEIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACI 439
Cdd:TIGR01349 296 NVDISVAVATPDGLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACI 375

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1743165004 440 LAVGRFRPVLKLTEDEEGNAKLQqhQLITVTMSSDSRVVDDELATRFLKSFKANLENPIRL 500
Cdd:TIGR01349 376 LAVGAVEDVAVVDNDEEKGFAVA--SIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEM 434
PRK11856 PRK11856
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
 56-500 2.84e-139

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


Pssm-ID: 237001 [Multi-domain]  Cd Length: 411  Bit Score: 407.25  E-value: 2.84e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004  56 PIKILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnIRLGSLIGLIVEEG 135
Cdd:PRK11856    2 MFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDV-VPVGSVIAVIEEEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 136 EdwKHVEIPKDVGPPPPVSKPSESRPSPEPQISIPVKKEHIPGTLQFRLSPAARSILEKHSLDASQGTATGPRGIFTKED 215
Cdd:PRK11856   81 E--AEAAAAAEAAPEAPAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKED 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 216 alklVQlkqtgkitesrptpapaatptapsplQATAGPSYPRPVIPPVSTPGQPNAVGTFTEIPASNIRRVIAKRLTESK 295
Cdd:PRK11856  159 ----VE--------------------------AAAAAAAPAAAAAAAAAAAPPAAAAEGEERVPLSGMRKAIAKRMVESK 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 296 STVPHAYATADCDLGAVLKVRQDLVKDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPKQLPFIDISVAVATDKGLLT 375
Cdd:PRK11856  209 REIPHFTLTDEVDVTALLALRKQLKAIGVKLTVTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVATDGGLIV 288

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 376 PIIKDAAAKGIQEIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGRF--RPVLKlte 453
Cdd:PRK11856  289 PVIRDADKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIveRPVVV--- 365

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 1743165004 454 deegNAKLQQHQLITVTMSSDSRVVDDELATRFLKSFKANLENPIRL 500
Cdd:PRK11856  366 ----DGEIVVRKVMPLSLSFDHRVIDGADAARFLKALKELLENPALL 408
2-oxoacid_dh pfam00198
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ...
 291-500 1.39e-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: 254.78  E-value: 1.39e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 291 LTESKSTVPHAYATADCDLGAVLKVRQDL----VKDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPK--QLPFIDIS 364
Cdd:pfam00198   1 MTESKQTIPHFTLTDEVDVTELLALREELkedaADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEivYKKYVNIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 365 VAVATDKGLLTPIIKDAAAKGIQEIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGR 444
Cdd:pfam00198  81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1743165004 445 FRPVLKLTEDEegnakLQQHQLITVTMSSDSRVVDDELATRFLKSFKANLENPIRL 500
Cdd:pfam00198 161 IRKRPVVVDGE-----IVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELL 211
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 57-131 3.56e-28

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: 106.72  E-value: 3.56e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1743165004  57 IKILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnIRLGSLIGLI 131
Cdd:cd06849     1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAVI 74
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 56-132 1.89e-25

Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 440274 [Multi-domain]  Cd Length: 77  Bit Score: 99.37  E-value: 1.89e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1743165004  56 PIKILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnIRLGSLIGLIV 132
Cdd:COG0508     2 AIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDT-VPVGAVIAVIA 77
 
Name Accession Description Interval E-value
PDHac_trf_mito TIGR01349
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 58-500 5.44e-143

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: 417.66  E-value: 5.44e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004  58 KILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKNIRLGSLIGLIVEEGED 137
Cdd:TIGR01349   1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 138 ----WKHVEIPKDVGPPP------PVSKPSESRPSPEPQISIPVKKEHIPGTLQFR-----LSPAARSILEKHSLDASQG 202
Cdd:TIGR01349  81 vadaFKNYKLESSASPAPkpseiaPTAPPSAPKPSPAPQKQSPEPSSPAPLSDKESgdrifASPLAKKLAKEKGIDLSAV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 203 TATGPRGIFTKEDALKLVQLKQTgkitesrptpapaatptaPSPLQATAGPSYPRPVIPPVSTpgqpnavGTFTEIPASN 282
Cdd:TIGR01349 161 AGSGPNGRIVKKDIESFVPQSPA------------------SANQQAAATTPATYPAAAPVST-------GSYEDVPLSN 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 283 IRRVIAKRLTESKSTVPHAYATADCDLGAVLKVRQDLVK---DDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPKQLP 359
Cdd:TIGR01349 216 IRKIIAKRLLESKQTIPHYYVSIECNVDKLLALRKELNAmasEVYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYK 295

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 360 FIDISVAVATDKGLLTPIIKDAAAKGIQEIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACI 439
Cdd:TIGR01349 296 NVDISVAVATPDGLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACI 375

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1743165004 440 LAVGRFRPVLKLTEDEEGNAKLQqhQLITVTMSSDSRVVDDELATRFLKSFKANLENPIRL 500
Cdd:TIGR01349 376 LAVGAVEDVAVVDNDEEKGFAVA--SIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEM 434
PRK11856 PRK11856
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
 56-500 2.84e-139

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


Pssm-ID: 237001 [Multi-domain]  Cd Length: 411  Bit Score: 407.25  E-value: 2.84e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004  56 PIKILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnIRLGSLIGLIVEEG 135
Cdd:PRK11856    2 MFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDV-VPVGSVIAVIEEEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 136 EdwKHVEIPKDVGPPPPVSKPSESRPSPEPQISIPVKKEHIPGTLQFRLSPAARSILEKHSLDASQGTATGPRGIFTKED 215
Cdd:PRK11856   81 E--AEAAAAAEAAPEAPAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKED 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 216 alklVQlkqtgkitesrptpapaatptapsplQATAGPSYPRPVIPPVSTPGQPNAVGTFTEIPASNIRRVIAKRLTESK 295
Cdd:PRK11856  159 ----VE--------------------------AAAAAAAPAAAAAAAAAAAPPAAAAEGEERVPLSGMRKAIAKRMVESK 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 296 STVPHAYATADCDLGAVLKVRQDLVKDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPKQLPFIDISVAVATDKGLLT 375
Cdd:PRK11856  209 REIPHFTLTDEVDVTALLALRKQLKAIGVKLTVTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVATDGGLIV 288

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 376 PIIKDAAAKGIQEIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGRF--RPVLKlte 453
Cdd:PRK11856  289 PVIRDADKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIveRPVVV--- 365

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 1743165004 454 deegNAKLQQHQLITVTMSSDSRVVDDELATRFLKSFKANLENPIRL 500
Cdd:PRK11856  366 ----DGEIVVRKVMPLSLSFDHRVIDGADAARFLKALKELLENPALL 408
PLN02744 PLN02744
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
 58-497 5.27e-113

dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex


Pssm-ID: 215397 [Multi-domain]  Cd Length: 539  Bit Score: 344.53  E-value: 5.27e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004  58 KILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKNIRLGSLIGLIVEEGED 137
Cdd:PLN02744  114 EIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKEIKVGEVIAITVEEEED 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 138 ---WKHVEIPKDVGPPPPVSKPS----------ESRPSPEPQISIPVKKEHiPGTLQFRlSPAARSILEKHSLDASQGTA 204
Cdd:PLN02744  194 igkFKDYKPSSSAAPAAPKAKPSppppkeeeveKPASSPEPKASKPSAPPS-SGDRIFA-SPLARKLAEDNNVPLSSIKG 271

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 205 TGPRGIFTKEDALKLvqLKQTGKitesrptpapaatptapsplQATAGPSYPRPvIPPVStpgqpnavgtFTEIPASNIR 284
Cdd:PLN02744  272 TGPDGRIVKADIEDY--LASGGK--------------------GATAPPSTDSK-APALD----------YTDIPNTQIR 318

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 285 RVIAKRLTESKSTVPHAYATADCDLGAVLKVRQDL-----VKDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPKQLP 359
Cdd:PLN02744  319 KVTASRLLQSKQTIPHYYLTVDTRVDKLMALRSQLnslqeASGGKKISVNDLVIKAAALALRKVPQCNSSWTDDYIRQYH 398

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 360 FIDISVAVATDKGLLTPIIKDAAAKGIQEIADSVKALSKKARDGKLLPEEYQGGSFSISNL-GMFGIDEFTAVINPPQAC 438
Cdd:PLN02744  399 NVNINVAVQTENGLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLgGPFGIKQFCAIINPPQSA 478

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1743165004 439 ILAVGRF--RPVLKLTEDEEGNAklqqhQLITVTMSSDSRVVDDELATRFLKSFKANLENP 497
Cdd:PLN02744  479 ILAVGSAekRVIPGSGPDQYNFA-----SFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENP 534
2-oxoacid_dh pfam00198
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ...
 291-500 1.39e-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: 254.78  E-value: 1.39e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 291 LTESKSTVPHAYATADCDLGAVLKVRQDL----VKDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPK--QLPFIDIS 364
Cdd:pfam00198   1 MTESKQTIPHFTLTDEVDVTELLALREELkedaADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEivYKKYVNIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 365 VAVATDKGLLTPIIKDAAAKGIQEIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGR 444
Cdd:pfam00198  81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1743165004 445 FRPVLKLTEDEegnakLQQHQLITVTMSSDSRVVDDELATRFLKSFKANLENPIRL 500
Cdd:pfam00198 161 IRKRPVVVDGE-----IVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELL 211
sucB TIGR01347
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ...
 57-501 2.78e-74

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: 240.02  E-value: 2.78e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004  57 IKILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnirlgsligliVEEGE 136
Cdd:TIGR01347   1 IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDT-----------VESGQ 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 137 DWKHVEIPKDVGPPPPvskpSESRPSPEPQISIPVKKEhiPGTLQFR--LSPAARSILEKHSLDASQGTATGPRGIFTKE 214
Cdd:TIGR01347  70 VLAILEEGNDATAAPP----AKSGEEKEETPAASAAAA--PTAAANRpsLSPAARRLAKEHGIDLSAVPGTGVTGRVTKE 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 215 DALKlvqlkqtgkitesrptpapaatptapsplqATAGPSYPRPVIPPVSTPGQPNAVGTFTEIPASNIRRVIAKRLTES 294
Cdd:TIGR01347 144 DIIK------------------------------KTEAPASAQPPAAAAAAAAPAAATRPEERVKMTRLRQRIAERLKEA 193

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 295 KSTVPHAYATADCDLGAVLKVR-----QDLVKDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPKQLPFIDISVAVAT 369
Cdd:TIGR01347 194 QNSTAMLTTFNEVDMSAVMELRkrykeEFEKKHGVKLGFMSFFVKAVVAALKRFPEVNAEIDGDDIVYKDYYDISVAVST 273

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 370 DKGLLTPIIKDAAAKGIQEIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGRF--RP 447
Cdd:TIGR01347 274 DRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIkeRP 353

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1743165004 448 VLKltedeegNAKLQQHQLITVTMSSDSRVVDDELATRFLKSFKANLENPIRLA 501
Cdd:TIGR01347 354 VAV-------NGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRRLL 400
PRK05704 PRK05704
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
57-500 1.03e-72

2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;


Pssm-ID: 235571 [Multi-domain]  Cd Length: 407  Bit Score: 235.88  E-value: 1.03e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004  57 IKILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSkNIRLGSLIGLIVEEGE 136
Cdd:PRK05704    3 VEIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGD-TVTVGQVLGRIDEGAA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 137 dwkhveiPKDVGPPPPVSKPSESRPSPEPQISIPVKKEHIpgtlqfrLSPAARSILEKHSLDASQGTATGPRGIFTKEDA 216
Cdd:PRK05704   82 -------AGAAAAAAAAAAAAAAAPAQAQAAAAAEQSNDA-------LSPAARKLAAENGLDASAVKGTGKGGRVTKEDV 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 217 LKLVQlkqtgkitesrptpapaatptapSPLQATAGPSYPRPVIPPVSTPGQPNavgtfTEIPASNIRRVIAKRLTESKS 296
Cdd:PRK05704  148 LAALA-----------------------AAAAAPAAPAAAAPAAAPAPLGARPE-----ERVPMTRLRKTIAERLLEAQN 199

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 297 TvphayaTA------DCDLGAVLKVR---QDLV--KDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGP--KQlpFIDI 363
Cdd:PRK05704  200 T------TAmlttfnEVDMTPVMDLRkqyKDAFekKHGVKLGFMSFFVKAVVEALKRYPEVNASIDGDDIvyHN--YYDI 271

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 364 SVAVATDKGLLTPIIKDAAAKGIQEIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVG 443
Cdd:PRK05704  272 GIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELAKKARDGKLSIEELTGGTFTITNGGVFGSLMSTPIINPPQSAILGMH 351

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1743165004 444 RF--RPVLKltedeegNAKLQQHQLITVTMSSDSRVVDDELATRFLKSFKANLENPIRL 500
Cdd:PRK05704  352 KIkeRPVAV-------NGQIVIRPMMYLALSYDHRIIDGKEAVGFLVTIKELLEDPERL 403
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 70-501 1.10e-72

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 240.11  E-value: 1.10e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004  70 EGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnIRLGSLIGLIVEEGEDWKHVEIPKDVGP 149
Cdd:PRK11855  132 EVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDK-VSVGSLLVVIEVAAAAPAAAAAPAAAAP 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 150 PPPVSKPSESRPSPEPQISIPVKKEHIPGTLQFRLSPAARSILEKHSLDASQGTATGPRGIFTKEDALKLVQLKQTGKIT 229
Cdd:PRK11855  211 AAAAAAAPAPAPAAAAAPAAAAPAAAAAPGKAPHASPAVRRLARELGVDLSQVKGTGKKGRITKEDVQAFVKGAMSAAAA 290

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 230 esrptpapaatptAPSPLQATAGPSYPRPVIPPVSTpgqpNAVGTFTEIPASNIRRVIAKRLTESKSTVPHAYATADCDL 309
Cdd:PRK11855  291 -------------AAAAAAAAGGGGLGLLPWPKVDF----SKFGEIETKPLSRIKKISAANLHRSWVTIPHVTQFDEADI 353

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 310 GAVLKVR----QDLVKDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGpKQLPF---IDISVAVATDKGLLTPIIKDAA 382
Cdd:PRK11855  354 TDLEALRkqlkKEAEKAGVKLTMLPFFIKAVVAALKEFPVFNASLDEDG-DELTYkkyFNIGFAVDTPNGLVVPVIKDVD 432

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 383 AKGIQEIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGRF--RPVlklTEDEEGNAK 460
Cdd:PRK11855  433 KKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSqmKPV---WDGKEFVPR 509

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 1743165004 461 LqqhqLITVTMSSDSRVVDDELATRFLKSFKANLENPIRLA 501
Cdd:PRK11855  510 L----MLPLSLSYDHRVIDGATAARFTNYLKQLLADPRRML 546
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 61-500 1.01e-57

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 202.15  E-value: 1.01e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004  61 MPSLSPTmeEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnIRLGSLIGLIVEEGEDWKH 140
Cdd:PRK11854  211 VPDIGGD--EVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDK-VKTGSLIMRFEVEGAAPAA 287

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 141 VEIPKDVGPPPPVSKPSESrPSPEPQISIPVKKEHIPGTLQFRLSPAARSILEKHSLDASQGTATGPRGIFTKEDALKLV 220
Cdd:PRK11854  288 APAKQEAAAPAPAAAKAEA-PAAAPAAKAEGKSEFAENDAYVHATPLVRRLAREFGVNLAKVKGTGRKGRILKEDVQAYV 366

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 221 qlKQTGKITESrptpapaatptaPSPLQATAGPSYPRPVIPPVStpgqPNAVGTFTEIPASNIRRVIAKRLTESKSTVPH 300
Cdd:PRK11854  367 --KDAVKRAEA------------APAAAAAGGGGPGLLPWPKVD----FSKFGEIEEVELGRIQKISGANLHRNWVMIPH 428

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 301 A--YATADCDLGAVLKVRQDLV----KDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGpKQL---PFIDISVAVATDK 371
Cdd:PRK11854  429 VtqFDKADITELEAFRKQQNAEaekrKLGVKITPLVFIMKAVAAALEQMPRFNSSLSEDG-QRLtlkKYVNIGIAVDTPN 507

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 372 GLLTPIIKDAAAKGIQEIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGR--FRPVl 449
Cdd:PRK11854  508 GLVVPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKsaMEPV- 586

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1743165004 450 kltedeEGNAKLQQHQLITVTMSSDSRVVDDELATRFLKSFKANLENPIRL 500
Cdd:PRK11854  587 ------WNGKEFAPRLMLPLSLSYDHRVIDGADGARFITIINDRLSDIRRL 631
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 69-500 2.77e-54

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: 191.24  E-value: 2.77e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004  69 EEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnIRLGSLIglIVEEGEDWKHVEIPKDVG 148
Cdd:TIGR01348 128 EKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDS-VPTGDLI--LTLSVAGSTPATAPAPAS 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 149 PPPPVSKPSESRPSP-------EPQISIPVKKEHIPGTLQFRLSPAARSILEKHSLDASQGTATGPRGIFTKEDALKLVq 221
Cdd:TIGR01348 205 AQPAAQSPAATQPEPaaapaaaKAQAPAPQQAGTQNPAKVDHAAPAVRRLAREFGVDLSAVKGTGIKGRILREDVQRFV- 283

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 222 lKQTGKITESrptpapaatptapsplqATAGPSYPRPVIPPVstpgqPNA----VGTFTEIPASNIRRVIAKRLTESKST 297
Cdd:TIGR01348 284 -KEPSVRAQA-----------------AAASAAGGAPGALPW-----PNVdfskFGEVEEVDMSRIRKISGANLTRNWTM 340

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 298 VPHA--YATADCDLGAVLKVRQDLV--KDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDgEGPKQL---PFIDISVAVATD 370
Cdd:TIGR01348 341 IPHVthFDKADITEMEAFRKQQNAAveKEGVKLTVLHILMKAVAAALKKFPKFNASLD-LGGEQLilkKYVNIGVAVDTP 419

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 371 KGLLTPIIKDAAAKGIQEIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGR--FRPV 448
Cdd:TIGR01348 420 NGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKsgMEPV 499

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1743165004 449 LKLTEdeegnakLQQHQLITVTMSSDSRVVDDELATRFLKSFKANLENPIRL 500
Cdd:TIGR01348 500 WNGKE-------FEPRLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRL 544
PTZ00144 PTZ00144
dihydrolipoamide succinyltransferase; Provisional
 59-500 1.95e-50

dihydrolipoamide succinyltransferase; Provisional


Pssm-ID: 240289 [Multi-domain]  Cd Length: 418  Bit Score: 177.57  E-value: 1.95e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004  59 ILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSknirlgsliglIVEEGEDW 138
Cdd:PTZ00144   47 IKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGD-----------TVEVGAPL 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 139 khVEIPKDVGPPP-PVSKPSESRPSPEPQISIPVKKEHIPGTLQFRLSPAArsilekhsldasqgtatgprgiftkedal 217
Cdd:PTZ00144  116 --SEIDTGGAPPAaAPAAAAAAKAEKTTPEKPKAAAPTPEPPAASKPTPPA----------------------------- 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 218 klvqlkqtgkitesrptpapaatptapsPLQATAGPSYPRPVIPPVSTPGQPNavgtfTEIPASNIRRVIAKRLTESKST 297
Cdd:PTZ00144  165 ----------------------------AAKPPEPAPAAKPPPTPVARADPRE-----TRVPMSRMRQRIAERLKASQNT 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 298 VPHAYATADCDLGAVLKVRQDL-----VKDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPKQLPFIDISVAVATDKG 372
Cdd:PTZ00144  212 CAMLTTFNECDMSALMELRKEYkddfqKKHGVKLGFMSAFVKASTIALKKMPIVNAYIDGDEIVYRNYVDISVAVATPTG 291

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 373 LLTPIIKDAAAKGIQEIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACIL---AVGRfRPVL 449
Cdd:PTZ00144  292 LVVPVIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILgmhAIKK-RPVV 370

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1743165004 450 KltedeegNAKLQQHQLITVTMSSDSRVVDDELATRFLKSFKANLENPIRL 500
Cdd:PTZ00144  371 V-------GNEIVIRPIMYLALTYDHRLIDGRDAVTFLKKIKDLIEDPARM 414
SucB_Actino TIGR02927
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ...
 54-495 1.52e-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: 173.27  E-value: 1.52e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004  54 GDPIKILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEgSKNIRLGSLIGLIve 133
Cdd:TIGR02927 124 GEATEVKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPE-DDTVEVGTVLAII-- 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 134 eGEDWKHVEIPKDVGPPPPVSKPSESRPSPEPQISIPVKKEHIPGTLQFRLSPAA------------------RSILEKH 195
Cdd:TIGR02927 201 -GDANAAPAEPAEEEAPAPSEAGSEPAPDPAARAPHAAPDPPAPAPAPAKTAAPAaaapvssgdsgpyvtplvRKLAKDK 279

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 196 SLDASQGTATGPRGIFTKEDALKLVQlkqtgKITESRPTPAPAAtptapsplqATAGPSYPRPVIPPVStPGQPNAVGTf 275
Cdd:TIGR02927 280 GVDLSTVKGTGVGGRIRKQDVLAAAK-----AAEEARAAAAAPA---------AAAAPAAPAAAAKPAE-PDTAKLRGT- 343

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 276 TEiPASNIRRVIAKRLTESKSTVPHAYATADCDLGAVLKVRQD-----LVKDDIKVSVNDFIIKAAAVTLKQMPDVNVSW 350
Cdd:TIGR02927 344 TQ-KMNRIRQITADKTIESLQTSAQLTQVHEVDMTRVAALRARakndfLEKNGVNLTFLPFFVQAVTEALKAHPNVNASY 422

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 351 DGEGpKQLPFID---ISVAVATDKGLLTPIIKDAAAKGIQEIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDE 427
Cdd:TIGR02927 423 NAET-KEVTYHDvehVGIAVDTPRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALF 501

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1743165004 428 FTAVINPPQACILAVGRFRPVLKLTEDEEGNAKLQQHQLITVTMSSDSRVVDDELATRFLKSFKANLE 495
Cdd:TIGR02927 502 DTPILNPPQAAILGTGAIVKRPRVIKDEDGGESIAIRSVCYLPLTYDHRLVDGADAGRFLTTIKKRLE 569
PLN02528 PLN02528
2-oxoisovalerate dehydrogenase E2 component
 70-500 7.30e-46

2-oxoisovalerate dehydrogenase E2 component


Pssm-ID: 215289 [Multi-domain]  Cd Length: 416  Bit Score: 165.28  E-value: 7.30e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004  70 EGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnIRLG-SLIGLIVEEGEDWKHVEIPKDVG 148
Cdd:PLN02528   12 ECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDI-VKVGeTLLKIMVEDSQHLRSDSLLLPTD 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 149 PPPPVSKPSESrpspepqisipVKKEHIPGTLQfrlSPAARSILEKHSLDASQGTATGPRGIFTKEDALKLVQLKQTGKI 228
Cdd:PLN02528   91 SSNIVSLAESD-----------ERGSNLSGVLS---TPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAAQKGVVKD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 229 TESRPTPAPAATPTAPSPLQATAGPSYPRPVIPpvstpgqpnavgtfteipASNIRRVIAKRLTESKStVPHAYATADCD 308
Cdd:PLN02528  157 SSSAEEATIAEQEEFSTSVSTPTEQSYEDKTIP------------------LRGFQRAMVKTMTAAAK-VPHFHYVEEIN 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 309 LGAVLKVRQDL----VKDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPK--QLPFIDISVAVATDKGLLTPIIKDAA 382
Cdd:PLN02528  218 VDALVELKASFqennTDPTVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEirLKGSHNIGVAMATEHGLVVPNIKNVQ 297

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 383 AKGIQEIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGRFRPVLKLTEDEE-GNAKl 461
Cdd:PLN02528  298 SLSLLEITKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPRFVDDGNvYPAS- 376

                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 1743165004 462 qqhqLITVTMSSDSRVVDDELATRFLKSFKANLENPIRL 500
Cdd:PLN02528  377 ----IMTVTIGADHRVLDGATVARFCNEWKSYVEKPELL 411
PRK14843 PRK14843
dihydrolipoamide acetyltransferase; Provisional
 179-500 1.42e-42

dihydrolipoamide acetyltransferase; Provisional


Pssm-ID: 184847 [Multi-domain]  Cd Length: 347  Bit Score: 154.68  E-value: 1.42e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 179 TLQFRLSPAARSILEKHSLDASQGTATGPRGIFTKEDALKLVqlkqtgkitesrptpapaatptapSPLQATAGPSYPRP 258
Cdd:PRK14843   46 TNVVRISPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALL------------------------PENIENDSIKSPAQ 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 259 VIPPVSTPGQPNAVGTFTEIPASNIRRVIAKRLTESKSTVPHAYATADCDLGAVLKVRQDLVkDDI------KVSVNDFI 332
Cdd:PRK14843  102 IEKVEEVPDNVTPYGEIERIPMTPMRKVIAQRMVESYLTAPTFTLNYEVDMTEMLALRKKVL-EPImeatgkKTTVTDLL 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 333 IKAAAVTLKQMPDVNVSWDGEGPKQLP--FIDISVAVATDKGLLTPIIKDAAAKGIQEIADSVKALSKKARDGKLLPEEY 410
Cdd:PRK14843  181 SLAVVKTLMKHPYINASLTEDGKTIIThnYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSEL 260

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 411 QGGSFSISNLGMFGIDEFTAVINPPQACILAVGRF--RPVLKltedeegNAKLQQHQLITVTMSSDSRVVDDELATRFLK 488
Cdd:PRK14843  261 QNSTFTISNLGMFGVQSFGPIINQPNSAILGVSSTieKPVVV-------NGEIVIRPIMSLGLTIDHRVVDGMAGAKFMK 333

                         330
                  ....*....|..
gi 1743165004 489 SFKANLENPIRL 500
Cdd:PRK14843  334 DLKELIETPISM 345
PLN02226 PLN02226
2-oxoglutarate dehydrogenase E2 component
 15-500 9.72e-40

2-oxoglutarate dehydrogenase E2 component


Pssm-ID: 177871 [Multi-domain]  Cd Length: 463  Bit Score: 149.52  E-value: 9.72e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004  15 RYLVGFPG-RRSVGLVKGALGwsvsrganwRWFHSTQWLRGDPIKILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEI 93
Cdd:PLN02226   58 LALPGNSGiSRSASLVSSTLQ---------RWVRPFSSESGDTVEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQI 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004  94 ETDKAVVTLDASDDGILAKIVVEEGSkNIRLGSLIGLIVEEGEDWKHVeipkdvgppppvsKPSESRP-SPEPQISIPVK 172
Cdd:PLN02226  129 ETDKVTIDIASPASGVIQEFLVKEGD-TVEPGTKVAIISKSEDAASQV-------------TPSQKIPeTTDPKPSPPAE 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 173 KEHIPGTlqfrlspaarsilekhsldasqgtatgprgiftkedalklvqlkQTGKITESrptpapaatptapsplqatag 252
Cdd:PLN02226  195 DKQKPKV--------------------------------------------ESAPVAEK--------------------- 209

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 253 PSYPRPVIPPVSTPGQPNAVGTFTE--IPASNIRRVIAKRLTESKSTVPHAYATADCDLGAVLKVRQD-----LVKDDIK 325
Cdd:PLN02226  210 PKAPSSPPPPKQSAKEPQLPPKERErrVPMTRLRKRVATRLKDSQNTFALLTTFNEVDMTNLMKLRSQykdafYEKHGVK 289

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 326 VSVNDFIIKAAAVTLKQMPDVNVSWDGEGPKQLPFIDISVAVATDKGLLTPIIKDAAAKGIQEIADSVKALSKKARDGKL 405
Cdd:PLN02226  290 LGLMSGFIKAAVSALQHQPVVNAVIDGDDIIYRDYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKTINGLAKKANEGTI 369

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 406 LPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGRF--RPVLKltedeegNAKLQQHQLITVTMSSDSRVVDDELA 483
Cdd:PLN02226  370 SIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIvsRPMVV-------GGSVVPRPMMYVALTYDHRLIDGREA 442

                         490
                  ....*....|....*..
gi 1743165004 484 TRFLKSFKANLENPIRL 500
Cdd:PLN02226  443 VYFLRRVKDVVEDPQRL 459
PRK11892 PRK11892
pyruvate dehydrogenase subunit beta; Provisional
 56-177 1.23e-34

pyruvate dehydrogenase subunit beta; Provisional


Pssm-ID: 237011 [Multi-domain]  Cd Length: 464  Bit Score: 135.43  E-value: 1.23e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004  56 PIKILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKNIRLGSLIGLIVEEG 135
Cdd:PRK11892    2 AIEILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEGVKVNTPIAVLLEEG 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1743165004 136 EDwkhVEIPKDVGPPPPVSKPSESRPSPEPQISIPVKKEHIP 177
Cdd:PRK11892   82 ES---ASDAGAAPAAAAEAAAAAPAAAAAAAAKKAAPAPAAP 120
PRK11857 PRK11857
dihydrolipoamide acetyltransferase; Reviewed
 185-497 3.64e-31

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237002 [Multi-domain]  Cd Length: 306  Bit Score: 122.21  E-value: 3.64e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 185 SPAARSILEKHSLDASQGTATGPRGIFTKEDALKLVqlkqtgkitESRPTPAPAATPTAPSPLQATAgpSYPRPVIPPVS 264
Cdd:PRK11857    5 TPIARALAKKLGIDISLLKGSGRDGKILAEDVENFI---------KSLKSAPTPAEAASVSSAQQAA--KTAAPAAAPPK 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 265 TPGQPNAVGTfteipasnIRRVIAKRLTESKSTVPHAYATADCDLGAVLKVRQDLVKD-----DIKVSVNDFIIKAAAVT 339
Cdd:PRK11857   74 LEGKREKVAP--------IRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPvlkteGVKLTFLPFIAKAILIA 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 340 LKQMPDVNVSWDgEGPKQLPF---IDISVAVATDKGLLTPIIKDAAAKGIQEIADSVKALSKKARDGKLLPEEYQGGSFS 416
Cdd:PRK11857  146 LKEFPIFAAKYD-EATSELVYpdtLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFT 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004 417 ISNLGMFGIDEFTAVINPPQACILAVGRF--RPVLKltedeegNAKLQQHQLITVTMSSDSRVVDDELATRFLKSFKANL 494
Cdd:PRK11857  225 ITNYGSVGSLYGVPVINYPELAIAGVGAIidKAIVK-------NGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELL 297


                  ...
gi 1743165004 495 ENP 497
Cdd:PRK11857  298 EKP 300
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 57-131 3.56e-28

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: 106.72  E-value: 3.56e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1743165004  57 IKILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnIRLGSLIGLI 131
Cdd:cd06849     1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAVI 74
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 56-132 1.89e-25

Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 440274 [Multi-domain]  Cd Length: 77  Bit Score: 99.37  E-value: 1.89e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1743165004  56 PIKILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnIRLGSLIGLIV 132
Cdd:COG0508     2 AIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDT-VPVGAVIAVIA 77
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 58-135 1.11e-17

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 84.61  E-value: 1.11e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1743165004  58 KILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSkNIRLGSLIGLIVEEG 135
Cdd:PRK14875    4 PITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGE-TLPVGALLAVVADAE 80
Biotinyl_lipoyl_domains cd06663
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ...
 59-120 2.88e-15

Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases, and the H-protein of the glycine cleavage system (GCS). These domains transport CO2, acyl, or methylamine, respectively, between components of the complex/protein via a biotinyl or lipoyl group, which is covalently attached to a highly conserved lysine residue.


Pssm-ID: 133456 [Multi-domain]  Cd Length: 73  Bit Score: 70.55  E-value: 2.88e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1743165004  59 ILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSK 120
Cdd:cd06663     2 ILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTK 63
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 59-131 3.83e-15

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: 69.94  E-value: 3.83e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1743165004  59 ILMPSLSPTMEEGnIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKnIRLGSLIGLI 131
Cdd:pfam00364   3 IKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDT-VEVGDPLAKI 73
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 71-119 6.53e-09

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: 52.03  E-value: 6.53e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1743165004  71 GNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGS 119
Cdd:cd06850     8 GTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGD 56
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
 245-488 2.24e-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: 2.24e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004  245 SPLQATAGPSYPRPVIPPVSTPGQPNAVGTFTEIPASNIR---RVIAKRLTESKStVPhaYATAdcdlgavlkVRQDLVK 321
Cdd:PRK12270    82 APPKPAAAAAAAAAPAAPPAAAAAAAPAAAAVEDEVTPLRgaaAAVAKNMDASLE-VP--TATS---------VRAVPAK 149

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004  322 --DDIKVSVNDF-------------IIKAAAV-TLKQMPDVNVSWDGEGPKqlPFI----DISVAVATD-------KGLL 374
Cdd:PRK12270   150 llIDNRIVINNHlkrtrggkvsfthLIGYALVqALKAFPNMNRHYAEVDGK--PTLvtpaHVNLGLAIDlpkkdgsRQLV 227

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743165004  375 TPIIKDAAAKGIQEIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGRFR-PVLKLTE 453
Cdd:PRK12270   228 VPAIKGAETMDFAQFWAAYEDIVRRARDGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAMEyPAEFQGA 307

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1743165004  454 DEEGNAKLQQHQLITVTMSSDSRVVDDELATRFLK 488
Cdd:PRK12270   308 SEERLAELGISKVMTLTSTYDHRIIQGAESGEFLR 342
E3_binding pfam02817
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ...
 183-217 1.94e-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: 1.94e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1743165004 183 RLSPAARSILEKHSLDASQGTATGPRGIFTKEDAL 217
Cdd:pfam02817   2 LASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
 71-120 1.43e-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: 41.60  E-value: 1.43e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1743165004   71 GNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSK 120
Cdd:COG1038   1085 GTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQ 1134
PRK09282 PRK09282
pyruvate carboxylase subunit B; Validated
 71-118 2.49e-03

pyruvate carboxylase subunit B; Validated


Pssm-ID: 236449 [Multi-domain]  Cd Length: 592  Bit Score: 40.60  E-value: 2.49e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1743165004  71 GNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEG 118
Cdd:PRK09282  531 GTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEG 578
AccB COG0511
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ...
 79-119 8.49e-03

Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440277 [Multi-domain]  Cd Length: 136  Bit Score: 36.80  E-value: 8.49e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1743165004  79 KEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGS 119
Cdd:COG0511    84 KVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQ 124
 
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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