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Conserved domains on  [gi|28201978|ref|NP_780303|]
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pyruvate dehydrogenase protein X component, mitochondrial [Mus musculus]

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 5.42e-138

pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model represents one of several closely related clades of the dihydrolipoamide acetyltransferase subunit of the pyruvate dehydrogenase complex. It includes sequences from mitochondria and from alpha and beta branches of the proteobacteria, as well as from some other bacteria. Sequences from Gram-positive bacteria are not included. The non-enzymatic homolog protein X, which serves as an E3 component binding protein, falls within the clade phylogenetically but is rejected by its low score. [Energy metabolism, Pyruvate dehydrogenase]


The actual alignment was detected with superfamily member TIGR01349:

Pssm-ID: 273567 [Multi-domain]  Cd Length: 436  Bit Score: 404.95  E-value: 5.42e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978    58 KVLMPSLSPTMEQGNIVKWLRKEGEAVSAGDSLCEIETDKAVVTLDANDDGILAKIVVEEGAKNIQLGSLIALMVEEGED 137
Cdd:TIGR01349   1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978   138 -----------WKQVEIPKDVSAPPPVSKPPAPTQPSPQPQIPCPA----RKEHKGTARFRLSPAARNILEKHSLDASQG 202
Cdd:TIGR01349  81 vadafknykleSSASPAPKPSEIAPTAPPSAPKPSPAPQKQSPEPSspapLSDKESGDRIFASPLAKKLAKEKGIDLSAV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978   203 TATGPRGIFTKEDALKLVELKqmgkitesrPASAPPPSLSAsvppqatagpsyprpmTPPVSIPGQPNAAGTFTEIPASN 282
Cdd:TIGR01349 161 AGSGPNGRIVKKDIESFVPQS---------PASANQQAAAT----------------TPATYPAAAPVSTGSYEDVPLSN 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978   283 IRRVIAKRLTESKSTVPHAYATADCDLGAVLKVRRDLVK---DDIKVSVNDFIIRAAAVTLKQMPGVNVTWDGEGPKQLP 359
Cdd:TIGR01349 216 IRKIIAKRLLESKQTIPHYYVSIECNVDKLLALRKELNAmasEVYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYK 295

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978   360 SVDISVAVATDKGLITPIIKDAAAKGIQEIADSVKVLSKKARDGKLMPEEYQGGSFSISNLGMFGIDEFAAVINPPQACI 439
Cdd:TIGR01349 296 NVDISVAVATPDGLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACI 375

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28201978   440 LAVG--RFRPVLKLTEDEegnpQLQQHQLITVTMSSDSRVVDDELATRFLETFKANLENPMRL 500
Cdd:TIGR01349 376 LAVGavEDVAVVDNDEEK----GFAVASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEM 434
 
Name Accession Description Interval E-value
PDHac_trf_mito TIGR01349
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 58-500 5.42e-138

pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model represents one of several closely related clades of the dihydrolipoamide acetyltransferase subunit of the pyruvate dehydrogenase complex. It includes sequences from mitochondria and from alpha and beta branches of the proteobacteria, as well as from some other bacteria. Sequences from Gram-positive bacteria are not included. The non-enzymatic homolog protein X, which serves as an E3 component binding protein, falls within the clade phylogenetically but is rejected by its low score. [Energy metabolism, Pyruvate dehydrogenase]


Pssm-ID: 273567 [Multi-domain]  Cd Length: 436  Bit Score: 404.95  E-value: 5.42e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978    58 KVLMPSLSPTMEQGNIVKWLRKEGEAVSAGDSLCEIETDKAVVTLDANDDGILAKIVVEEGAKNIQLGSLIALMVEEGED 137
Cdd:TIGR01349   1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978   138 -----------WKQVEIPKDVSAPPPVSKPPAPTQPSPQPQIPCPA----RKEHKGTARFRLSPAARNILEKHSLDASQG 202
Cdd:TIGR01349  81 vadafknykleSSASPAPKPSEIAPTAPPSAPKPSPAPQKQSPEPSspapLSDKESGDRIFASPLAKKLAKEKGIDLSAV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978   203 TATGPRGIFTKEDALKLVELKqmgkitesrPASAPPPSLSAsvppqatagpsyprpmTPPVSIPGQPNAAGTFTEIPASN 282
Cdd:TIGR01349 161 AGSGPNGRIVKKDIESFVPQS---------PASANQQAAAT----------------TPATYPAAAPVSTGSYEDVPLSN 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978   283 IRRVIAKRLTESKSTVPHAYATADCDLGAVLKVRRDLVK---DDIKVSVNDFIIRAAAVTLKQMPGVNVTWDGEGPKQLP 359
Cdd:TIGR01349 216 IRKIIAKRLLESKQTIPHYYVSIECNVDKLLALRKELNAmasEVYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYK 295

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978   360 SVDISVAVATDKGLITPIIKDAAAKGIQEIADSVKVLSKKARDGKLMPEEYQGGSFSISNLGMFGIDEFAAVINPPQACI 439
Cdd:TIGR01349 296 NVDISVAVATPDGLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACI 375

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28201978   440 LAVG--RFRPVLKLTEDEegnpQLQQHQLITVTMSSDSRVVDDELATRFLETFKANLENPMRL 500
Cdd:TIGR01349 376 LAVGavEDVAVVDNDEEK----GFAVASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEM 434
PRK11856 PRK11856
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
 56-500 1.83e-129

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


Pssm-ID: 237001 [Multi-domain]  Cd Length: 411  Bit Score: 382.22  E-value: 1.83e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978   56 PIKVLMPSLSPTMEQGNIVKWLRKEGEAVSAGDSLCEIETDKAVVTLDANDDGILAKIVVEEGAKnIQLGSLIALMVEEG 135
Cdd:PRK11856   2 MFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDV-VPVGSVIAVIEEEG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978  136 EdwKQVEIPKDVSAPPPVSKPPAPTQPSPQPQIPCPARKEHKGTARFRLSPAARNILEKHSLDASQGTATGPRGIFTKED 215
Cdd:PRK11856  81 E--AEAAAAAEAAPEAPAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKED 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978  216 alklVElkqmgKITESRPASAPPPSLSASVPPQATAGPSyprpmtppvsipgqpnaagtfTEIPASNIRRVIAKRLTESK 295
Cdd:PRK11856 159 ----VE-----AAAAAAAPAAAAAAAAAAAPPAAAAEGE---------------------ERVPLSGMRKAIAKRMVESK 208

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978  296 STVPHAYATADCDLGAVLKVRRDLVKDDIKVSVNDFIIRAAAVTLKQMPGVNVTWDGEGPKQLPSVDISVAVATDKGLIT 375
Cdd:PRK11856 209 REIPHFTLTDEVDVTALLALRKQLKAIGVKLTVTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVATDGGLIV 288

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978  376 PIIKDAAAKGIQEIADSVKVLSKKARDGKLMPEEYQGGSFSISNLGMFGIDEFAAVINPPQACILAVGRF--RPVLKlte 453
Cdd:PRK11856 289 PVIRDADKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIveRPVVV--- 365

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 28201978  454 deegNPQLQQHQLITVTMSSDSRVVDDELATRFLETFKANLENPMRL 500
Cdd:PRK11856 366 ----DGEIVVRKVMPLSLSFDHRVIDGADAARFLKALKELLENPALL 408
2-oxoacid_dh pfam00198
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ...
 291-500 3.90e-80

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: 248.61  E-value: 3.90e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978   291 LTESKSTVPHAYATADCDLGAVLKVRRDL----VKDDIKVSVNDFIIRAAAVTLKQMPGVNVTWDGEGPK--QLPSVDIS 364
Cdd:pfam00198   1 MTESKQTIPHFTLTDEVDVTELLALREELkedaADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEivYKKYVNIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978   365 VAVATDKGLITPIIKDAAAKGIQEIADSVKVLSKKARDGKLMPEEYQGGSFSISNLGMFGIDEFAAVINPPQACILAVGR 444
Cdd:pfam00198  81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 28201978   445 --FRPVLKltedeegNPQLQQHQLITVTMSSDSRVVDDELATRFLETFKANLENPMRL 500
Cdd:pfam00198 161 irKRPVVV-------DGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELL 211
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 57-131 1.46e-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: 102.10  E-value: 1.46e-26
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28201978  57 IKVLMPSLSPTMEQGNIVKWLRKEGEAVSAGDSLCEIETDKAVVTLDANDDGILAKIVVEEGAKnIQLGSLIALM 131
Cdd:cd06849   1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAVI 74
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 56-132 4.10e-23

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


Pssm-ID: 440274 [Multi-domain]  Cd Length: 77  Bit Score: 92.82  E-value: 4.10e-23
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28201978  56 PIKVLMPSLSPTMEQGNIVKWLRKEGEAVSAGDSLCEIETDKAVVTLDANDDGILAKIVVEEGAKnIQLGSLIALMV 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 5.42e-138

pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model represents one of several closely related clades of the dihydrolipoamide acetyltransferase subunit of the pyruvate dehydrogenase complex. It includes sequences from mitochondria and from alpha and beta branches of the proteobacteria, as well as from some other bacteria. Sequences from Gram-positive bacteria are not included. The non-enzymatic homolog protein X, which serves as an E3 component binding protein, falls within the clade phylogenetically but is rejected by its low score. [Energy metabolism, Pyruvate dehydrogenase]


Pssm-ID: 273567 [Multi-domain]  Cd Length: 436  Bit Score: 404.95  E-value: 5.42e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978    58 KVLMPSLSPTMEQGNIVKWLRKEGEAVSAGDSLCEIETDKAVVTLDANDDGILAKIVVEEGAKNIQLGSLIALMVEEGED 137
Cdd:TIGR01349   1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978   138 -----------WKQVEIPKDVSAPPPVSKPPAPTQPSPQPQIPCPA----RKEHKGTARFRLSPAARNILEKHSLDASQG 202
Cdd:TIGR01349  81 vadafknykleSSASPAPKPSEIAPTAPPSAPKPSPAPQKQSPEPSspapLSDKESGDRIFASPLAKKLAKEKGIDLSAV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978   203 TATGPRGIFTKEDALKLVELKqmgkitesrPASAPPPSLSAsvppqatagpsyprpmTPPVSIPGQPNAAGTFTEIPASN 282
Cdd:TIGR01349 161 AGSGPNGRIVKKDIESFVPQS---------PASANQQAAAT----------------TPATYPAAAPVSTGSYEDVPLSN 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978   283 IRRVIAKRLTESKSTVPHAYATADCDLGAVLKVRRDLVK---DDIKVSVNDFIIRAAAVTLKQMPGVNVTWDGEGPKQLP 359
Cdd:TIGR01349 216 IRKIIAKRLLESKQTIPHYYVSIECNVDKLLALRKELNAmasEVYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYK 295

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978   360 SVDISVAVATDKGLITPIIKDAAAKGIQEIADSVKVLSKKARDGKLMPEEYQGGSFSISNLGMFGIDEFAAVINPPQACI 439
Cdd:TIGR01349 296 NVDISVAVATPDGLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACI 375

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28201978   440 LAVG--RFRPVLKLTEDEegnpQLQQHQLITVTMSSDSRVVDDELATRFLETFKANLENPMRL 500
Cdd:TIGR01349 376 LAVGavEDVAVVDNDEEK----GFAVASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEM 434
PRK11856 PRK11856
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
 56-500 1.83e-129

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


Pssm-ID: 237001 [Multi-domain]  Cd Length: 411  Bit Score: 382.22  E-value: 1.83e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978   56 PIKVLMPSLSPTMEQGNIVKWLRKEGEAVSAGDSLCEIETDKAVVTLDANDDGILAKIVVEEGAKnIQLGSLIALMVEEG 135
Cdd:PRK11856   2 MFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDV-VPVGSVIAVIEEEG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978  136 EdwKQVEIPKDVSAPPPVSKPPAPTQPSPQPQIPCPARKEHKGTARFRLSPAARNILEKHSLDASQGTATGPRGIFTKED 215
Cdd:PRK11856  81 E--AEAAAAAEAAPEAPAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKED 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978  216 alklVElkqmgKITESRPASAPPPSLSASVPPQATAGPSyprpmtppvsipgqpnaagtfTEIPASNIRRVIAKRLTESK 295
Cdd:PRK11856 159 ----VE-----AAAAAAAPAAAAAAAAAAAPPAAAAEGE---------------------ERVPLSGMRKAIAKRMVESK 208

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978  296 STVPHAYATADCDLGAVLKVRRDLVKDDIKVSVNDFIIRAAAVTLKQMPGVNVTWDGEGPKQLPSVDISVAVATDKGLIT 375
Cdd:PRK11856 209 REIPHFTLTDEVDVTALLALRKQLKAIGVKLTVTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVATDGGLIV 288

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978  376 PIIKDAAAKGIQEIADSVKVLSKKARDGKLMPEEYQGGSFSISNLGMFGIDEFAAVINPPQACILAVGRF--RPVLKlte 453
Cdd:PRK11856 289 PVIRDADKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIveRPVVV--- 365

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 28201978  454 deegNPQLQQHQLITVTMSSDSRVVDDELATRFLETFKANLENPMRL 500
Cdd:PRK11856 366 ----DGEIVVRKVMPLSLSFDHRVIDGADAARFLKALKELLENPALL 408
PLN02744 PLN02744
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
 61-500 4.17e-111

dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex


Pssm-ID: 215397 [Multi-domain]  Cd Length: 539  Bit Score: 339.91  E-value: 4.17e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978   61 MPSLSPTMEQGNIVKWLRKEGEAVSAGDSLCEIETDKAVVTLDANDDGILAKIVVEEGAKNIQLGSLIALMVEEGEDWKQ 140
Cdd:PLN02744 117 MPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKEIKVGEVIAITVEEEEDIGK 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978  141 VeipKDVSAPPPVSKPPAPTQPSPQP--------QIPCPARKEHKGTA------RFRLSPAARNILEKHSLDASQGTATG 206
Cdd:PLN02744 197 F---KDYKPSSSAAPAAPKAKPSPPPpkeeevekPASSPEPKASKPSAppssgdRIFASPLARKLAEDNNVPLSSIKGTG 273

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978  207 PRGIFTKEDALKLveLKQMGK-ITESRPASAPPPSLSasvppqatagpsyprpmtppvsipgqpnaagtFTEIPASNIRR 285
Cdd:PLN02744 274 PDGRIVKADIEDY--LASGGKgATAPPSTDSKAPALD--------------------------------YTDIPNTQIRK 319

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978  286 VIAKRLTESKSTVPHAYATADCDLGAVLKVRRDL-----VKDDIKVSVNDFIIRAAAVTLKQMPGVNVTWDGEGPKQLPS 360
Cdd:PLN02744 320 VTASRLLQSKQTIPHYYLTVDTRVDKLMALRSQLnslqeASGGKKISVNDLVIKAAALALRKVPQCNSSWTDDYIRQYHN 399

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978  361 VDISVAVATDKGLITPIIKDAAAKGIQEIADSVKVLSKKARDGKLMPEEYQGGSFSISNL-GMFGIDEFAAVINPPQACI 439
Cdd:PLN02744 400 VNINVAVQTENGLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLgGPFGIKQFCAIINPPQSAI 479

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28201978  440 LAVG----RFRPvlkltedEEGNPQLQQHQLITVTMSSDSRVVDDELATRFLETFKANLENPMRL 500
Cdd:PLN02744 480 LAVGsaekRVIP-------GSGPDQYNFASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESM 537
2-oxoacid_dh pfam00198
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ...
 291-500 3.90e-80

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: 248.61  E-value: 3.90e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978   291 LTESKSTVPHAYATADCDLGAVLKVRRDL----VKDDIKVSVNDFIIRAAAVTLKQMPGVNVTWDGEGPK--QLPSVDIS 364
Cdd:pfam00198   1 MTESKQTIPHFTLTDEVDVTELLALREELkedaADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEivYKKYVNIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978   365 VAVATDKGLITPIIKDAAAKGIQEIADSVKVLSKKARDGKLMPEEYQGGSFSISNLGMFGIDEFAAVINPPQACILAVGR 444
Cdd:pfam00198  81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 28201978   445 --FRPVLKltedeegNPQLQQHQLITVTMSSDSRVVDDELATRFLETFKANLENPMRL 500
Cdd:pfam00198 161 irKRPVVV-------DGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELL 211
sucB TIGR01347
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ...
 57-500 9.36e-69

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: 225.77  E-value: 9.36e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978    57 IKVLMPSLSPTMEQGNIVKWLRKEGEAVSAGDSLCEIETDKAVVTLDANDDGILAKIVVEEGAKniqlgslialmVEEGE 136
Cdd:TIGR01347   1 IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDT-----------VESGQ 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978   137 DWKQVEIPKDVSAPPPVSKPPAPTQPSPQPQIPCPARKEhkgtARFRLSPAARNILEKHSLDASQGTATGPRGIFTKEDA 216
Cdd:TIGR01347  70 VLAILEEGNDATAAPPAKSGEEKEETPAASAAAAPTAAA----NRPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDI 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978   217 LKLvelkqmgkiTESRPASAPPPSLSASVPPQAtagpsYPRPMTppvsipgqpnaagtftEIPASNIRRVIAKRLTESKS 296
Cdd:TIGR01347 146 IKK---------TEAPASAQPPAAAAAAAAPAA-----ATRPEE----------------RVKMTRLRQRIAERLKEAQN 195

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978   297 TVPHAYATADCDLGAVLKVRRD-----LVKDDIKVSVNDFIIRAAAVTLKQMPGVNVTWDGEGPKQLPSVDISVAVATDK 371
Cdd:TIGR01347 196 STAMLTTFNEVDMSAVMELRKRykeefEKKHGVKLGFMSFFVKAVVAALKRFPEVNAEIDGDDIVYKDYYDISVAVSTDR 275

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978   372 GLITPIIKDAAAKGIQEIADSVKVLSKKARDGKLMPEEYQGGSFSISNLGMFGIDEFAAVINPPQACILAVGRF--RPVL 449
Cdd:TIGR01347 276 GLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIkeRPVA 355

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 28201978   450 KltedeegNPQLQQHQLITVTMSSDSRVVDDELATRFLETFKANLENPMRL 500
Cdd:TIGR01347 356 V-------NGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRRL 399
PRK05704 PRK05704
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
57-500 1.12e-65

2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;


Pssm-ID: 235571 [Multi-domain]  Cd Length: 407  Bit Score: 217.78  E-value: 1.12e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978   57 IKVLMPSLSPTMEQGNIVKWLRKEGEAVSAGDSLCEIETDKAVVTLDANDDGILAKIVVEEGAkNIQLGSLIALMVEEGE 136
Cdd:PRK05704   3 VEIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGD-TVTVGQVLGRIDEGAA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978  137 DWKQVEIPKDVSAPPPVSKPPAPTQPSPQPQIPcparkehkgtarfrLSPAARNILEKHSLDASQGTATGPRGIFTKEDA 216
Cdd:PRK05704  82 AGAAAAAAAAAAAAAAAPAQAQAAAAAEQSNDA--------------LSPAARKLAAENGLDASAVKGTGKGGRVTKEDV 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978  217 LKLVElkqmgkiTESRPASAPPPSLSASVPPQATAGPSYPRPMTppvsipgqpnaagtfteipasNIRRVIAKRLTESKS 296
Cdd:PRK05704 148 LAALA-------AAAAAPAAPAAAAPAAAPAPLGARPEERVPMT---------------------RLRKTIAERLLEAQN 199

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978  297 TvphayaTA------DCDLGAVLKVRRDLvKD------DIKVSVNDFIIRAAAVTLKQMPGVNVTWDGEGP--KQLpsVD 362
Cdd:PRK05704 200 T------TAmlttfnEVDMTPVMDLRKQY-KDafekkhGVKLGFMSFFVKAVVEALKRYPEVNASIDGDDIvyHNY--YD 270

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978  363 ISVAVATDKGLITPIIKDAAAKGIQEIADSVKVLSKKARDGKLMPEEYQGGSFSISNLGMFGIDEFAAVINPPQACILAV 442
Cdd:PRK05704 271 IGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELAKKARDGKLSIEELTGGTFTITNGGVFGSLMSTPIINPPQSAILGM 350

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978  443 GRF--RPVLKltedeegNPQLQQHQLITVTMSSDSRVVDDELATRFLETFKANLENPMRL 500
Cdd:PRK05704 351 HKIkeRPVAV-------NGQIVIRPMMYLALSYDHRIIDGKEAVGFLVTIKELLEDPERL 403
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 59-500 3.18e-64

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 217.77  E-value: 3.18e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978   59 VLMPSLSPTMEqGNIVKWLRKEGEAVSAGDSLCEIETDKAVVTLDANDDGILAKIVVEEGAKnIQLGSLIALM-VEEGED 137
Cdd:PRK11855 122 VKVPDIGEITE-VEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDK-VSVGSLLVVIeVAAAAP 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978  138 WKQVEIPKDVSAPPPVSKPPAPTQPSPQPQIPCPARKEHKGTARFrLSPAARNILEKHSLDASQGTATGPRGIFTKEDAL 217
Cdd:PRK11855 200 AAAAAPAAAAPAAAAAAAPAPAPAAAAAPAAAAPAAAAAPGKAPH-ASPAVRRLARELGVDLSQVKGTGKKGRITKEDVQ 278

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978  218 KLVElkqmgkitesrpASAPPPSLSASVPPQATAGPSyprpmtppvSIPGQPNAA----GTFTEIPASNIRRVIAKRLTE 293
Cdd:PRK11855 279 AFVK------------GAMSAAAAAAAAAAAAGGGGL---------GLLPWPKVDfskfGEIETKPLSRIKKISAANLHR 337

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978  294 SKSTVPHAYATADCDLGAVLKVRRDL----VKDDIKVSVNDFIIRAAAVTLKQMPGVNVTWDGEGpKQL---PSVDISVA 366
Cdd:PRK11855 338 SWVTIPHVTQFDEADITDLEALRKQLkkeaEKAGVKLTMLPFFIKAVVAALKEFPVFNASLDEDG-DELtykKYFNIGFA 416

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978  367 VATDKGLITPIIKDAAAKGIQEIADSVKVLSKKARDGKLMPEEYQGGSFSISNLGMFGIDEFAAVINPPQACILAVGRF- 445
Cdd:PRK11855 417 VDTPNGLVVPVIKDVDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSq 496

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 28201978  446 -RPVlklTEDEEGNPQLqqhqLITVTMSSDSRVVDDELATRFLETFKANLENPMRL 500
Cdd:PRK11855 497 mKPV---WDGKEFVPRL----MLPLSLSYDHRVIDGATAARFTNYLKQLLADPRRM 545
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 59-500 1.17e-53

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 190.98  E-value: 1.17e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978   59 VLMPSLSPTmeQGNIVKWLRKEGEAVSAGDSLCEIETDKAVVTLDANDDGILAKIVVEEGAKnIQLGSLIALMVEEGEDW 138
Cdd:PRK11854 209 VNVPDIGGD--EVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDK-VKTGSLIMRFEVEGAAP 285

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978  139 KQVEIPKDVSAPPPVSKPPAPTQPSPqPQIPCPARKEHKGTARFRLSPAARNILEKHSLDASQGTATGPRGIFTKEDALK 218
Cdd:PRK11854 286 AAAPAKQEAAAPAPAAAKAEAPAAAP-AAKAEGKSEFAENDAYVHATPLVRRLAREFGVNLAKVKGTGRKGRILKEDVQA 364

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978  219 LVelKQMGKITESRPASApppslsasvppqATAGPSYPRPMTPPVSipgqPNAAGTFTEIPASNIRRVIAKRLTESKSTV 298
Cdd:PRK11854 365 YV--KDAVKRAEAAPAAA------------AAGGGGPGLLPWPKVD----FSKFGEIEEVELGRIQKISGANLHRNWVMI 426

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978  299 PHA--YATAD-CDLGAVLKVRRDLV---KDDIKVSVNDFIIRAAAVTLKQMPGVNVTWDGEGpKQL---PSVDISVAVAT 369
Cdd:PRK11854 427 PHVtqFDKADiTELEAFRKQQNAEAekrKLGVKITPLVFIMKAVAAALEQMPRFNSSLSEDG-QRLtlkKYVNIGIAVDT 505

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978  370 DKGLITPIIKDAAAKGIQEIADSVKVLSKKARDGKLMPEEYQGGSFSISNLGMFGIDEFAAVINPPQACILAVGR--FRP 447
Cdd:PRK11854 506 PNGLVVPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKsaMEP 585

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 28201978  448 VlkltedeEGNPQLQQHQLITVTMSSDSRVVDDELATRFLETFKANLENPMRL 500
Cdd:PRK11854 586 V-------WNGKEFAPRLMLPLSLSYDHRVIDGADGARFITIINDRLSDIRRL 631
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 69-500 6.51e-49

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: 176.60  E-value: 6.51e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978    69 EQGNIVKWLRKEGEAVSAGDSLCEIETDKAVVTLDANDDGILAKIVVEEGAKnIQLGSLIALMVEEGEDWKQVEIPKdvs 148
Cdd:TIGR01348 128 EKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDS-VPTGDLILTLSVAGSTPATAPAPA--- 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978   149 APPPVSKPPAPTQPSPqPQIPCPARKEHKGT--------ARFR-LSPAARNILEKHSLDASQGTATGPRGIFTKEDALKL 219
Cdd:TIGR01348 204 SAQPAAQSPAATQPEP-AAAPAAAKAQAPAPqqagtqnpAKVDhAAPAVRRLAREFGVDLSAVKGTGIKGRILREDVQRF 282

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978   220 VElkqmgkitesrpasapPPSLSASVPPQATAGPSyprPMTPPVsipgqPNAA----GTFTEIPASNIRRVIAKRLTESK 295
Cdd:TIGR01348 283 VK----------------EPSVRAQAAAASAAGGA---PGALPW-----PNVDfskfGEVEEVDMSRIRKISGANLTRNW 338

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978   296 STVPHAYATADCDLGAVLKVRRDL----VKDDIKVSVNDFIIRAAAVTLKQMPGVNVTWDgEGPKQL---PSVDISVAVA 368
Cdd:TIGR01348 339 TMIPHVTHFDKADITEMEAFRKQQnaavEKEGVKLTVLHILMKAVAAALKKFPKFNASLD-LGGEQLilkKYVNIGVAVD 417

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978   369 TDKGLITPIIKDAAAKGIQEIADSVKVLSKKARDGKLMPEEYQGGSFSISNLGMFGIDEFAAVINPPQACILAVGR--FR 446
Cdd:TIGR01348 418 TPNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKsgME 497

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 28201978   447 PVLKLTEDEegnPQLqqhqLITVTMSSDSRVVDDELATRFLETFKANLENPMRL 500
Cdd:TIGR01348 498 PVWNGKEFE---PRL----MLPLSLSYDHRVIDGADAARFTTYICESLADIRRL 544
PTZ00144 PTZ00144
dihydrolipoamide succinyltransferase; Provisional
 57-500 2.43e-47

dihydrolipoamide succinyltransferase; Provisional


Pssm-ID: 240289 [Multi-domain]  Cd Length: 418  Bit Score: 169.48  E-value: 2.43e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978   57 IKVlmPSLSPTMEQGNIVKWLRKEGEAVSAGDSLCEIETDKAVVTLDANDDGILAKIVVEEGAKniqlgslialmVEEGE 136
Cdd:PTZ00144  47 IKV--PTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDT-----------VEVGA 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978  137 DWkqVEIPKDVsapppvskppaptQPSPQPqipCPARKEHKGTARFRLSPAARNIlekhsldasqgtatgprgiftkeda 216
Cdd:PTZ00144 114 PL--SEIDTGG-------------APPAAA---PAAAAAAKAEKTTPEKPKAAAP------------------------- 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978  217 lklvelkqmgkitESRPASAPPPSLSASVPPQATagPSYPRPMTPPVSIPGQPNaagtfTEIPASNIRRVIAKRLTESKS 296
Cdd:PTZ00144 151 -------------TPEPPAASKPTPPAAAKPPEP--APAAKPPPTPVARADPRE-----TRVPMSRMRQRIAERLKASQN 210

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978  297 TVPHAYATADCDLGAVLKVRRDL-----VKDDIKVSVNDFIIRAAAVTLKQMPGVNVTWDGEGPKQLPSVDISVAVATDK 371
Cdd:PTZ00144 211 TCAMLTTFNECDMSALMELRKEYkddfqKKHGVKLGFMSAFVKASTIALKKMPIVNAYIDGDEIVYRNYVDISVAVATPT 290

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978  372 GLITPIIKDAAAKGIQEIADSVKVLSKKARDGKLMPEEYQGGSFSISNLGMFGIDEFAAVINPPQACIL---AVGRfRPV 448
Cdd:PTZ00144 291 GLVVPVIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILgmhAIKK-RPV 369

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 28201978  449 LKltedeegNPQLQQHQLITVTMSSDSRVVDDELATRFLETFKANLENPMRL 500
Cdd:PTZ00144 370 VV-------GNEIVIRPIMYLALTYDHRLIDGRDAVTFLKKIKDLIEDPARM 414
PLN02528 PLN02528
2-oxoisovalerate dehydrogenase E2 component
 73-500 4.00e-47

2-oxoisovalerate dehydrogenase E2 component


Pssm-ID: 215289 [Multi-domain]  Cd Length: 416  Bit Score: 168.74  E-value: 4.00e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978   73 IVKWLRKEGEAVSAGDSLCEIETDKAVVTLDANDDGILAKIVVEEGAKnIQLG-SLIALMVEEGEDwkqveipkdvsapp 151
Cdd:PLN02528  15 LLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDI-VKVGeTLLKIMVEDSQH-------------- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978  152 PVSKPPAPTQPSPQPQIPCPARKEHKGTARFRLSPAARNILEKHSLDASQGTATGPRGIFTKEDALKLveLKQMGKITES 231
Cdd:PLN02528  80 LRSDSLLLPTDSSNIVSLAESDERGSNLSGVLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKY--AAQKGVVKDS 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978  232 RPASA--PPPSLSASVPPQATAGPSYPRpmtppvsipgqpnaagtfTEIPASNIRRVIAKRLTESKStVPHAYATADCDL 309
Cdd:PLN02528 158 SSAEEatIAEQEEFSTSVSTPTEQSYED------------------KTIPLRGFQRAMVKTMTAAAK-VPHFHYVEEINV 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978  310 GAVLKVRRDL----VKDDIKVSVNDFIIRAAAVTLKQMPGVNVTWDGEGPK--QLPSVDISVAVATDKGLITPIIKDAAA 383
Cdd:PLN02528 219 DALVELKASFqennTDPTVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEirLKGSHNIGVAMATEHGLVVPNIKNVQS 298

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978  384 KGIQEIADSVKVLSKKARDGKLMPEEYQGGSFSISNLGMFGIDEFAAVINPPQACILAVGRFRPVLKLTEDEEGNPQlqq 463
Cdd:PLN02528 299 LSLLEITKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPRFVDDGNVYPA--- 375

                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 28201978  464 hQLITVTMSSDSRVVDDELATRFLETFKANLENPMRL 500
Cdd:PLN02528 376 -SIMTVTIGADHRVLDGATVARFCNEWKSYVEKPELL 411
SucB_Actino TIGR02927
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ...
 59-495 6.35e-46

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: 169.04  E-value: 6.35e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978    59 VLMPSLSPTMEQGNIVKWLRKEGEAVSAGDSLCEIETDKAVVTLDANDDGILAKIVVEEGaKNIQLGSLIALMVEEGEDW 138
Cdd:TIGR02927 129 VKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPED-DTVEVGTVLAIIGDANAAP 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978   139 KQVEIPKDVSAPPPVSKPPAPTQPSPQ---PQIPCPARKEHKGTARFRLSPAA------------RNILEKHSLDASQGT 203
Cdd:TIGR02927 208 AEPAEEEAPAPSEAGSEPAPDPAARAPhaaPDPPAPAPAPAKTAAPAAAAPVSsgdsgpyvtplvRKLAKDKGVDLSTVK 287

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978   204 ATGPRGIFTKEDALKLVELKQMGKitesRPASAPPPSLSASVPPQATAGPSyprpmtppvsiPGQPNAAGTFTEipASNI 283
Cdd:TIGR02927 288 GTGVGGRIRKQDVLAAAKAAEEAR----AAAAAPAAAAAPAAPAAAAKPAE-----------PDTAKLRGTTQK--MNRI 350

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978   284 RRVIAKRLTESKSTVPHAYATADCDLGAVLKVRRD-----LVKDDIKVSVNDFIIRAAAVTLKQMPGVNVTWDGEGPKQL 358
Cdd:TIGR02927 351 RQITADKTIESLQTSAQLTQVHEVDMTRVAALRARakndfLEKNGVNLTFLPFFVQAVTEALKAHPNVNASYNAETKEVT 430

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978   359 --PSVDISVAVATDKGLITPIIKDAAAKGIQEIADSVKVLSKKARDGKLMPEEYQGGSFSISNLGMFGIDEFAAVINPPQ 436
Cdd:TIGR02927 431 yhDVEHVGIAVDTPRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDTPILNPPQ 510

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 28201978   437 ACILAVGRFRPVLKLTEDEEGNPQLQQHQLITVTMSSDSRVVDDELATRFLETFKANLE 495
Cdd:TIGR02927 511 AAILGTGAIVKRPRVIKDEDGGESIAIRSVCYLPLTYDHRLVDGADAGRFLTTIKKRLE 569
PRK14843 PRK14843
dihydrolipoamide acetyltransferase; Provisional
 176-500 4.99e-43

dihydrolipoamide acetyltransferase; Provisional


Pssm-ID: 184847 [Multi-domain]  Cd Length: 347  Bit Score: 155.83  E-value: 4.99e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978  176 HKGTARFRLSPAARNILEKHSLDASQGTATGPRGIFTKEDALKLVelkqmgkitesrpasaPPPSLSASVPPqatagpsy 255
Cdd:PRK14843  43 YKDTNVVRISPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALL----------------PENIENDSIKS-------- 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978  256 PRPMTPPVSIPGQPNAAGTFTEIPASNIRRVIAKRLTESKSTVPHAYATADCDLGAVLKVRRDLVkDDI------KVSVN 329
Cdd:PRK14843  99 PAQIEKVEEVPDNVTPYGEIERIPMTPMRKVIAQRMVESYLTAPTFTLNYEVDMTEMLALRKKVL-EPImeatgkKTTVT 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978  330 DFIIRAAAVTLKQMPGVNVTWDGEGPKQLPS--VDISVAVATDKGLITPIIKDAAAKGIQEIADSVKVLSKKARDGKLMP 407
Cdd:PRK14843 178 DLLSLAVVKTLMKHPYINASLTEDGKTIITHnyVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAP 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978  408 EEYQGGSFSISNLGMFGIDEFAAVINPPQACILAVGRF--RPVLKltedeegNPQLQQHQLITVTMSSDSRVVDDELATR 485
Cdd:PRK14843 258 SELQNSTFTISNLGMFGVQSFGPIINQPNSAILGVSSTieKPVVV-------NGEIVIRPIMSLGLTIDHRVVDGMAGAK 330

                        330
                 ....*....|....*
gi 28201978  486 FLETFKANLENPMRL 500
Cdd:PRK14843 331 FMKDLKELIETPISM 345
PLN02226 PLN02226
2-oxoglutarate dehydrogenase E2 component
 44-500 2.03e-36

2-oxoglutarate dehydrogenase E2 component


Pssm-ID: 177871 [Multi-domain]  Cd Length: 463  Bit Score: 140.28  E-value: 2.03e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978   44 RWFHSTQLLQADPIKVLMPSLSPTMEQGNIVKWLRKEGEAVSAGDSLCEIETDKAVVTLDANDDGILAKIVVEEGaKNIQ 123
Cdd:PLN02226  79 RWVRPFSSESGDTVEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEG-DTVE 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978  124 LGSLIALMVEEGEDWKQVEIPKDVSAPppvskppapTQPSPQPqipcPARKEHKgtarfrlspaarnilekhsldasqgt 203
Cdd:PLN02226 158 PGTKVAIISKSEDAASQVTPSQKIPET---------TDPKPSP----PAEDKQK-------------------------- 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978  204 atgPRgiftkedalklvelKQMGKITESRPASAPPPslsasvPPQATAgpsyPRPMTPPVSIPgqpnaagtfTEIPASNI 283
Cdd:PLN02226 199 ---PK--------------VESAPVAEKPKAPSSPP------PPKQSA----KEPQLPPKERE---------RRVPMTRL 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978  284 RRVIAKRLTESKSTVPHAYATADCDLGAVLKVRRD-----LVKDDIKVSVNDFIIRAAAVTLKQMPGVNVTWDGEGPKQL 358
Cdd:PLN02226 243 RKRVATRLKDSQNTFALLTTFNEVDMTNLMKLRSQykdafYEKHGVKLGLMSGFIKAAVSALQHQPVVNAVIDGDDIIYR 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978  359 PSVDISVAVATDKGLITPIIKDAAAKGIQEIADSVKVLSKKARDGKLMPEEYQGGSFSISNLGMFGIDEFAAVINPPQAC 438
Cdd:PLN02226 323 DYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSA 402

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28201978  439 ILAVGRF--RPVLKltedeegNPQLQQHQLITVTMSSDSRVVDDELATRFLETFKANLENPMRL 500
Cdd:PLN02226 403 ILGMHSIvsRPMVV-------GGSVVPRPMMYVALTYDHRLIDGREAVYFLRRVKDVVEDPQRL 459
PRK11857 PRK11857
dihydrolipoamide acetyltransferase; Reviewed
 185-501 2.33e-34

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237002 [Multi-domain]  Cd Length: 306  Bit Score: 131.07  E-value: 2.33e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978  185 SPAARNILEKHSLDASQGTATGPRGIFTKEDALKLVElkqmgkitesRPASAPPPSLSASVPPQATAGPSyprpmTPPVS 264
Cdd:PRK11857   5 TPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIK----------SLKSAPTPAEAASVSSAQQAAKT-----AAPAA 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978  265 IPGQPNAAGTfteiPASNIRRVIAKRLTESKSTVPHAYATADCDLGAVLKVRRDLVKD-----DIKVSVNDFIIRAAAVT 339
Cdd:PRK11857  70 APPKLEGKRE----KVAPIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPvlkteGVKLTFLPFIAKAILIA 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978  340 LKQMPGVNVTWDgEGPKQL--PS-VDISVAVATDKGLITPIIKDAAAKGIQEIADSVKVLSKKARDGKLMPEEYQGGSFS 416
Cdd:PRK11857 146 LKEFPIFAAKYD-EATSELvyPDtLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFT 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978  417 ISNLGMFGIDEFAAVINPPQACILAVGRF--RPVLKltedeegNPQLQQHQLITVTMSSDSRVVDDELATRFLETFKANL 494
Cdd:PRK11857 225 ITNYGSVGSLYGVPVINYPELAIAGVGAIidKAIVK-------NGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELL 297


                 ....*..
gi 28201978  495 ENPMRLG 501
Cdd:PRK11857 298 EKPEILG 304
PRK11892 PRK11892
pyruvate dehydrogenase subunit beta; Provisional
 56-188 2.21e-30

pyruvate dehydrogenase subunit beta; Provisional


Pssm-ID: 237011 [Multi-domain]  Cd Length: 464  Bit Score: 123.10  E-value: 2.21e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978   56 PIKVLMPSLSPTMEQGNIVKWLRKEGEAVSAGDSLCEIETDKAVVTLDANDDGILAKIVVEEGAKNIQLGSLIALMVEEG 135
Cdd:PRK11892   2 AIEILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEGVKVNTPIAVLLEEG 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 28201978  136 EDwkqveipkdvsaPPPVSKPPAPTQPSPQPQIPCPARKEHKGTARFRLSPAA 188
Cdd:PRK11892  82 ES------------ASDAGAAPAAAAEAAAAAPAAAAAAAAKKAAPAPAAPAA 122
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 57-131 1.46e-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: 102.10  E-value: 1.46e-26
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28201978  57 IKVLMPSLSPTMEQGNIVKWLRKEGEAVSAGDSLCEIETDKAVVTLDANDDGILAKIVVEEGAKnIQLGSLIALM 131
Cdd:cd06849   1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAVI 74
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 56-132 4.10e-23

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


Pssm-ID: 440274 [Multi-domain]  Cd Length: 77  Bit Score: 92.82  E-value: 4.10e-23
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28201978  56 PIKVLMPSLSPTMEQGNIVKWLRKEGEAVSAGDSLCEIETDKAVVTLDANDDGILAKIVVEEGAKnIQLGSLIALMV 132
Cdd:COG0508   2 AIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDT-VPVGAVIAVIA 77
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 58-135 1.90e-15

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 77.68  E-value: 1.90e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28201978   58 KVLMPSLSPTMEQGNIVKWLRKEGEAVSAGDSLCEIETDKAVVTLDANDDGILAKIVVEEGaKNIQLGSLIALMVEEG 135
Cdd:PRK14875   4 PITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEG-ETLPVGALLAVVADAE 80
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 59-131 4.75e-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: 4.75e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28201978    59 VLMPSLSPTMEQGnIVKWLRKEGEAVSAGDSLCEIETDKAVVTLDANDDGILAKIVVEEGAKnIQLGSLIALM 131
Cdd:pfam00364   3 IKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDT-VEVGDPLAKI 73
Biotinyl_lipoyl_domains cd06663
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ...
 59-120 1.04e-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: 69.01  E-value: 1.04e-14
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28201978  59 VLMPSLSPTMEQGNIVKWLRKEGEAVSAGDSLCEIETDKAVVTLDANDDGILAKIVVEEGAK 120
Cdd:cd06663   2 ILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTK 63
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
 233-443 8.84e-11

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


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 64.53  E-value: 8.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978   233 PASAPPPSLSASVPPQATAGPSYPRPMTPPVSIPGQPNAAGTFTEIPASNIR---RVIAKRLTESKStVPhaYATADCDL 309
Cdd:PRK12270   70 PAPAPPAAAAPAAPPKPAAAAAAAAAPAAPPAAAAAAAPAAAAVEDEVTPLRgaaAAVAKNMDASLE-VP--TATSVRAV 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978   310 GAVLKVRRDLVKDD-------IKVSVNDFIIRAAAVTLKQMPGVNVTWDGEGPKqlPSV----DISVAVATD-------K 371
Cdd:PRK12270  147 PAKLLIDNRIVINNhlkrtrgGKVSFTHLIGYALVQALKAFPNMNRHYAEVDGK--PTLvtpaHVNLGLAIDlpkkdgsR 224

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28201978   372 GLITPIIKDAAAKGIQEIADSVKVLSKKARDGKLMPEEYQGGSFSISNLGMFGIDEFAAVINPPQACILAVG 443
Cdd:PRK12270  225 QLVVPAIKGAETMDFAQFWAAYEDIVRRARDGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVG 296
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 70-129 1.41e-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: 1.41e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201978  70 QGNIVKWLRKEGEAVSAGDSLCEIETDKAVVTLDANDDGILAKIVVEEGAkNIQLGSLIA 129
Cdd:cd06850   7 PGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGD-QVEAGQLLV 65
E3_binding pfam02817
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ...
 183-217 9.48e-05

e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid dehydrogenases responsible for the binding of the E3 subunit.


Pssm-ID: 460710 [Multi-domain]  Cd Length: 36  Bit Score: 39.59  E-value: 9.48e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 28201978   183 RLSPAARNILEKHSLDASQGTATGPRGIFTKEDAL 217
Cdd:pfam02817   2 LASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
 70-131 4.64e-04

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: 43.14  E-value: 4.64e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28201978   70 QGNIVKWLRKEGEAVSAGDSLCEIETDKAVVTLDANDDGILAKIVVEEGAKnIQLGSLIALM 131
Cdd:COG1038 1084 PGTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQ-VEAGDLLIEL 1144
PRK09282 PRK09282
pyruvate carboxylase subunit B; Validated
 64-118 1.97e-03

pyruvate carboxylase subunit B; Validated


Pssm-ID: 236449 [Multi-domain]  Cd Length: 592  Bit Score: 40.60  E-value: 1.97e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 28201978   64 LSPTMeQGNIVKWLRKEGEAVSAGDSLCEIETDKAVVTLDANDDGILAKIVVEEG 118
Cdd:PRK09282 525 VTSPM-PGTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEG 578
PRK12438 PRK12438
hypothetical protein; Provisional
 233-272 4.41e-03

hypothetical protein; Provisional


Pssm-ID: 171499 [Multi-domain]  Cd Length: 991  Bit Score: 39.84  E-value: 4.41e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 28201978  233 PASAPPPSLSASVPPQATAGPSYPRPMTPPVSIPGQPNAA 272
Cdd:PRK12438 910 AASAPPPGAGPPAPPQAVPPPRTTQPPAAPPRGPDVPPAA 949
 
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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