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Conserved domains on  [gi|52076491|dbj|BAD45370|]
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putative dihydrolipoamide S-acetyltransferase [Oryza sativa Japonica Group]

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 ...
 59-472 3.38e-154

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


The actual alignment was detected with superfamily member TIGR01349:

Pssm-ID: 273567 [Multi-domain]  Cd Length: 436  Bit Score: 445.78  E-value: 3.38e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491    59 VVGMPALSPTMNQGNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSKDVQVGQPIAVTVEDLED 138
Cdd:TIGR01349   1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491   139 I----KNIPADASFGGEQKEQSIASEAQkvETDAAKESSII------------------TRI--SPAAKLLIKEHRLDQS 194
Cdd:TIGR01349  81 VadafKNYKLESSASPAPKPSEIAPTAP--PSAPKPSPAPQkqspepsspaplsdkesgDRIfaSPLAKKLAKEKGIDLS 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491   195 VLNASGPRGTLLKGDVLAAL--KLGASSSSTKQKNAPAAPssqpthdfqaqsVTIPQQNDAYEDIPNSQIRKVIAKRLLE 272
Cdd:TIGR01349 159 AVAGSGPNGRIVKKDIESFVpqSPASANQQAAATTPATYP------------AAAPVSTGSYEDVPLSNIRKIIAKRLLE 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491   273 SKQTTPHLYLSQDVILDPLLAFRNELKEQHG--VKVSVNDIVIKAVALALRNVPEANAYWNNDKEQAQKcvSVDISIAVA 350
Cdd:TIGR01349 227 SKQTIPHYYVSIECNVDKLLALRKELNAMASevYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYK--NVDISVAVA 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491   351 TEKGLMTPIIRNADQKTISAISSEVKQLAEKARAGKLAPNEFQGGTFSISNLGMYPVDHFCAIINPPQSGILAVGRGNKI 430
Cdd:TIGR01349 305 TPDGLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDV 384

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 52076491   431 iePVVDSDGTEKATVVTKMSLTLSADHRVFDGQVGGKFFTEL 472
Cdd:TIGR01349 385 --AVVDNDEEKGFAVASIMSVTLSCDHRVIDGAVGAEFLKSF 424
 
Name Accession Description Interval E-value
PDHac_trf_mito TIGR01349
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 59-472 3.38e-154

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


Pssm-ID: 273567 [Multi-domain]  Cd Length: 436  Bit Score: 445.78  E-value: 3.38e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491    59 VVGMPALSPTMNQGNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSKDVQVGQPIAVTVEDLED 138
Cdd:TIGR01349   1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491   139 I----KNIPADASFGGEQKEQSIASEAQkvETDAAKESSII------------------TRI--SPAAKLLIKEHRLDQS 194
Cdd:TIGR01349  81 VadafKNYKLESSASPAPKPSEIAPTAP--PSAPKPSPAPQkqspepsspaplsdkesgDRIfaSPLAKKLAKEKGIDLS 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491   195 VLNASGPRGTLLKGDVLAAL--KLGASSSSTKQKNAPAAPssqpthdfqaqsVTIPQQNDAYEDIPNSQIRKVIAKRLLE 272
Cdd:TIGR01349 159 AVAGSGPNGRIVKKDIESFVpqSPASANQQAAATTPATYP------------AAAPVSTGSYEDVPLSNIRKIIAKRLLE 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491   273 SKQTTPHLYLSQDVILDPLLAFRNELKEQHG--VKVSVNDIVIKAVALALRNVPEANAYWNNDKEQAQKcvSVDISIAVA 350
Cdd:TIGR01349 227 SKQTIPHYYVSIECNVDKLLALRKELNAMASevYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYK--NVDISVAVA 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491   351 TEKGLMTPIIRNADQKTISAISSEVKQLAEKARAGKLAPNEFQGGTFSISNLGMYPVDHFCAIINPPQSGILAVGRGNKI 430
Cdd:TIGR01349 305 TPDGLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDV 384

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 52076491   431 iePVVDSDGTEKATVVTKMSLTLSADHRVFDGQVGGKFFTEL 472
Cdd:TIGR01349 385 --AVVDNDEEKGFAVASIMSVTLSCDHRVIDGAVGAEFLKSF 424
PLN02744 PLN02744
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
 50-468 9.34e-140

dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex


Pssm-ID: 215397 [Multi-domain]  Cd Length: 539  Bit Score: 412.71  E-value: 9.34e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491   50 SSTGFPPHLVVGMPALSPTMNQGNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSKDVQVGQPI 129
Cdd:PLN02744 105 SSSDLPPHQEIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKEIKVGEVI 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491  130 AVTVEDLEDI---KNIPADASFGG---------------EQKEQSIASEAQKVETDAAKESSIITRISPAAKLLIKEHRL 191
Cdd:PLN02744 185 AITVEEEEDIgkfKDYKPSSSAAPaapkakpsppppkeeEVEKPASSPEPKASKPSAPPSSGDRIFASPLARKLAEDNNV 264

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491  192 DQSVLNASGPRGTLLKGDVLAALKLGASSSSTKQKNAPAAPSSqpthdfqaqsvtipqqndAYEDIPNSQIRKVIAKRLL 271
Cdd:PLN02744 265 PLSSIKGTGPDGRIVKADIEDYLASGGKGATAPPSTDSKAPAL------------------DYTDIPNTQIRKVTASRLL 326

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491  272 ESKQTTPHLYLSQDVILDPLLAFRNEL----KEQHGVKVSVNDIVIKAVALALRNVPEANAYWNNDKEQAQKcvSVDISI 347
Cdd:PLN02744 327 QSKQTIPHYYLTVDTRVDKLMALRSQLnslqEASGGKKISVNDLVIKAAALALRKVPQCNSSWTDDYIRQYH--NVNINV 404

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491  348 AVATEKGLMTPIIRNADQKTISAISSEVKQLAEKARAGKLAPNEFQGGTFSISNL-GMYPVDHFCAIINPPQSGILAVGR 426
Cdd:PLN02744 405 AVQTENGLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLgGPFGIKQFCAIINPPQSAILAVGS 484

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 52076491  427 GNKiiePVVDSDGTEKATVVTKMSLTLSADHRVFDGQVGGKF 468
Cdd:PLN02744 485 AEK---RVIPGSGPDQYNFASFMSVTLSCDHRVIDGAIGAEW 523
2-oxoacid_dh pfam00198
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ...
 270-472 8.05e-84

2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to three copies of a lipoyl binding domain followed by the catalytic domain.


Pssm-ID: 425518 [Multi-domain]  Cd Length: 212  Bit Score: 257.47  E-value: 8.05e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491   270 LLESKQTTPHLYLSQDVILDPLLAFRNELKEQH---GVKVSVNDIVIKAVALALRNVPEANAYWNNDKEQAQKCVSVDIS 346
Cdd:pfam00198   1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAadeETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491   347 IAVATEKGLMTPIIRNADQKTISAISSEVKQLAEKARAGKLAPNEFQGGTFSISNLGMYPVDHFCAIINPPQSGILAVGR 426
Cdd:pfam00198  81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 52076491   427 GNKiiEPVVDSDGTEKATVvtkMSLTLSADHRVFDGQVGGKFFTEL 472
Cdd:pfam00198 161 IRK--RPVVVDGEIVVRKV---MPLSLSFDHRVIDGAEAARFLNTL 201
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 62-131 1.27e-27

Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.


Pssm-ID: 133458 [Multi-domain]  Cd Length: 74  Bit Score: 105.18  E-value: 1.27e-27
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491  62 MPALSPTMNQGNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSKdVQVGQPIAV 131
Cdd:cd06849   5 MPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAV 73
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 62-131 2.85e-25

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


Pssm-ID: 440274 [Multi-domain]  Cd Length: 77  Bit Score: 98.60  E-value: 2.85e-25
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491  62 MPALSPTMNQGNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSKdVQVGQPIAV 131
Cdd:COG0508   7 MPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDT-VPVGAVIAV 75
 
Name Accession Description Interval E-value
PDHac_trf_mito TIGR01349
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 59-472 3.38e-154

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


Pssm-ID: 273567 [Multi-domain]  Cd Length: 436  Bit Score: 445.78  E-value: 3.38e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491    59 VVGMPALSPTMNQGNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSKDVQVGQPIAVTVEDLED 138
Cdd:TIGR01349   1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491   139 I----KNIPADASFGGEQKEQSIASEAQkvETDAAKESSII------------------TRI--SPAAKLLIKEHRLDQS 194
Cdd:TIGR01349  81 VadafKNYKLESSASPAPKPSEIAPTAP--PSAPKPSPAPQkqspepsspaplsdkesgDRIfaSPLAKKLAKEKGIDLS 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491   195 VLNASGPRGTLLKGDVLAAL--KLGASSSSTKQKNAPAAPssqpthdfqaqsVTIPQQNDAYEDIPNSQIRKVIAKRLLE 272
Cdd:TIGR01349 159 AVAGSGPNGRIVKKDIESFVpqSPASANQQAAATTPATYP------------AAAPVSTGSYEDVPLSNIRKIIAKRLLE 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491   273 SKQTTPHLYLSQDVILDPLLAFRNELKEQHG--VKVSVNDIVIKAVALALRNVPEANAYWNNDKEQAQKcvSVDISIAVA 350
Cdd:TIGR01349 227 SKQTIPHYYVSIECNVDKLLALRKELNAMASevYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYK--NVDISVAVA 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491   351 TEKGLMTPIIRNADQKTISAISSEVKQLAEKARAGKLAPNEFQGGTFSISNLGMYPVDHFCAIINPPQSGILAVGRGNKI 430
Cdd:TIGR01349 305 TPDGLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDV 384

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 52076491   431 iePVVDSDGTEKATVVTKMSLTLSADHRVFDGQVGGKFFTEL 472
Cdd:TIGR01349 385 --AVVDNDEEKGFAVASIMSVTLSCDHRVIDGAVGAEFLKSF 424
PLN02744 PLN02744
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
 50-468 9.34e-140

dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex


Pssm-ID: 215397 [Multi-domain]  Cd Length: 539  Bit Score: 412.71  E-value: 9.34e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491   50 SSTGFPPHLVVGMPALSPTMNQGNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSKDVQVGQPI 129
Cdd:PLN02744 105 SSSDLPPHQEIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKEIKVGEVI 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491  130 AVTVEDLEDI---KNIPADASFGG---------------EQKEQSIASEAQKVETDAAKESSIITRISPAAKLLIKEHRL 191
Cdd:PLN02744 185 AITVEEEEDIgkfKDYKPSSSAAPaapkakpsppppkeeEVEKPASSPEPKASKPSAPPSSGDRIFASPLARKLAEDNNV 264

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491  192 DQSVLNASGPRGTLLKGDVLAALKLGASSSSTKQKNAPAAPSSqpthdfqaqsvtipqqndAYEDIPNSQIRKVIAKRLL 271
Cdd:PLN02744 265 PLSSIKGTGPDGRIVKADIEDYLASGGKGATAPPSTDSKAPAL------------------DYTDIPNTQIRKVTASRLL 326

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491  272 ESKQTTPHLYLSQDVILDPLLAFRNEL----KEQHGVKVSVNDIVIKAVALALRNVPEANAYWNNDKEQAQKcvSVDISI 347
Cdd:PLN02744 327 QSKQTIPHYYLTVDTRVDKLMALRSQLnslqEASGGKKISVNDLVIKAAALALRKVPQCNSSWTDDYIRQYH--NVNINV 404

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491  348 AVATEKGLMTPIIRNADQKTISAISSEVKQLAEKARAGKLAPNEFQGGTFSISNL-GMYPVDHFCAIINPPQSGILAVGR 426
Cdd:PLN02744 405 AVQTENGLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLgGPFGIKQFCAIINPPQSAILAVGS 484

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 52076491  427 GNKiiePVVDSDGTEKATVVTKMSLTLSADHRVFDGQVGGKF 468
Cdd:PLN02744 485 AEK---RVIPGSGPDQYNFASFMSVTLSCDHRVIDGAIGAEW 523
PRK11856 PRK11856
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
 62-472 3.89e-137

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


Pssm-ID: 237001 [Multi-domain]  Cd Length: 411  Bit Score: 401.09  E-value: 3.89e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491   62 MPALSPTMNQGNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSKdVQVGQPIAvTVEDLEDIKN 141
Cdd:PRK11856   7 MPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDV-VPVGSVIA-VIEEEGEAEA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491  142 IPADASFGGEQKEQSIASEAQKVETDAA------KESSIITRISPAAKLLIKEHRLDQSVLNASGPRGTLLKGDVLAALK 215
Cdd:PRK11856  85 AAAAEAAPEAPAPEPAPAAAAAAAAAPAaaaapaAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEAAAA 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491  216 LGASSSSTKQKNAPAAPSSQPthdfqaqsvtipqqnDAYEDIPNSQIRKVIAKRLLESKQTTPHLYLSQDVILDPLLAFR 295
Cdd:PRK11856 165 AAAPAAAAAAAAAAAPPAAAA---------------EGEERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLALR 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491  296 NELKEQhGVKVSVNDIVIKAVALALRNVPEANAYWNNDKEQAQKcvSVDISIAVATEKGLMTPIIRNADQKTISAISSEV 375
Cdd:PRK11856 230 KQLKAI-GVKLTVTDFLIKAVALALKKFPELNASWDDDAIVLKK--YVNIGIAVATDGGLIVPVIRDADKKSLFELAREI 306

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491  376 KQLAEKARAGKLAPNEFQGGTFSISNLGMYPVDHFCAIINPPQSGILAVGRgnkIIEPVVDSDGteKATVVTKMSLTLSA 455
Cdd:PRK11856 307 KDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGA---IVERPVVVDG--EIVVRKVMPLSLSF 381

                        410
                 ....*....|....*..
gi 52076491  456 DHRVFDGQVGGKFFTEL 472
Cdd:PRK11856 382 DHRVIDGADAARFLKAL 398
2-oxoacid_dh pfam00198
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ...
 270-472 8.05e-84

2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to three copies of a lipoyl binding domain followed by the catalytic domain.


Pssm-ID: 425518 [Multi-domain]  Cd Length: 212  Bit Score: 257.47  E-value: 8.05e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491   270 LLESKQTTPHLYLSQDVILDPLLAFRNELKEQH---GVKVSVNDIVIKAVALALRNVPEANAYWNNDKEQAQKCVSVDIS 346
Cdd:pfam00198   1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAadeETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491   347 IAVATEKGLMTPIIRNADQKTISAISSEVKQLAEKARAGKLAPNEFQGGTFSISNLGMYPVDHFCAIINPPQSGILAVGR 426
Cdd:pfam00198  81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 52076491   427 GNKiiEPVVDSDGTEKATVvtkMSLTLSADHRVFDGQVGGKFFTEL 472
Cdd:pfam00198 161 IRK--RPVVVDGEIVVRKV---MPLSLSFDHRVIDGAEAARFLNTL 201
PRK05704 PRK05704
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
63-484 1.93e-82

2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;


Pssm-ID: 235571 [Multi-domain]  Cd Length: 407  Bit Score: 260.92  E-value: 1.93e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491   63 PALSPTMNQGNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSkDVQVGQPIAVTVEDLEDIKNI 142
Cdd:PRK05704   8 PTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGD-TVTVGQVLGRIDEGAAAGAAA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491  143 PADASfggeqKEQSIASEAQKVETDAAKESSIItrISPAAKLLIKEHRLDQSVLNASGPRGTLLKGDVLAALklgASSSS 222
Cdd:PRK05704  87 AAAAA-----AAAAAAAPAQAQAAAAAEQSNDA--LSPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAAL---AAAAA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491  223 TKQKNAPAAPSSQPTHDFqAQSVtipqqndayEDIPNSQIRKVIAKRLLESKQTTPHLYLSQDVILDPLLAFRNELKEQ- 301
Cdd:PRK05704 157 APAAPAAAAPAAAPAPLG-ARPE---------ERVPMTRLRKTIAERLLEAQNTTAMLTTFNEVDMTPVMDLRKQYKDAf 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491  302 ---HGVKVSVNDIVIKAVALALRNVPEANAYWNND----KEQaqkcvsVDISIAVATEKGLMTPIIRNADQKTISAISSE 374
Cdd:PRK05704 227 ekkHGVKLGFMSFFVKAVVEALKRYPEVNASIDGDdivyHNY------YDIGIAVGTPRGLVVPVLRDADQLSFAEIEKK 300

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491  375 VKQLAEKARAGKLAPNEFQGGTFSISNLGMY------PvdhfcaIINPPQSGILAVgrgNKIIE-PVVdsdgtEKATVVT 447
Cdd:PRK05704 301 IAELAKKARDGKLSIEELTGGTFTITNGGVFgslmstP------IINPPQSAILGM---HKIKErPVA-----VNGQIVI 366

                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 52076491  448 K--MSLTLSADHRVFDGQVGGKFFTELSQNFGDIRRLLL 484
Cdd:PRK05704 367 RpmMYLALSYDHRIIDGKEAVGFLVTIKELLEDPERLLL 405
sucB TIGR01347
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ...
 60-484 5.66e-82

2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This model describes the TCA cycle 2-oxoglutarate system E2 component, dihydrolipoamide succinyltransferase. It is closely related to the pyruvate dehydrogenase E2 component, dihydrolipoamide acetyltransferase. The seed for this model includes mitochondrial and Gram-negative bacterial forms. Mycobacterial candidates are highly derived, differ in having and extra copy of the lipoyl-binding domain at the N-terminus. They score below the trusted cutoff, but above the noise cutoff and above all examples of dihydrolipoamide acetyltransferase. [Energy metabolism, TCA cycle]


Pssm-ID: 273565 [Multi-domain]  Cd Length: 403  Bit Score: 259.67  E-value: 5.66e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491    60 VGMPALSPTMNQGNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSKdVQVGQPIAVtVEDLEDI 139
Cdd:TIGR01347   3 IKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDT-VESGQVLAI-LEEGNDA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491   140 KNIPADASfgGEQKEQSIASEAQKVETDAAKESSIitriSPAAKLLIKEHRLDQSVLNASGPRGTLLKGDVLAALKLGAS 219
Cdd:TIGR01347  81 TAAPPAKS--GEEKEETPAASAAAAPTAAANRPSL----SPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKTEAPAS 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491   220 SSstkqknAPAAPSSQPTHDFQAQSVtipqqndayEDIPNSQIRKVIAKRLLESKQTTPHLYLSQDVILDPLLAFRNELK 299
Cdd:TIGR01347 155 AQ------PPAAAAAAAAPAAATRPE---------ERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYK 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491   300 EQ----HGVKVSVNDIVIKAVALALRNVPEANAYWNNDKEQAQKcvSVDISIAVATEKGLMTPIIRNADQKTISAISSEV 375
Cdd:TIGR01347 220 EEfekkHGVKLGFMSFFVKAVVAALKRFPEVNAEIDGDDIVYKD--YYDISVAVSTDRGLVVPVVRNADRMSFADIEKEI 297

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491   376 KQLAEKARAGKLAPNEFQGGTFSISNLGMYPVDHFCAIINPPQSGILAVgrgNKIIE-PVVDSDGTEkatVVTKMSLTLS 454
Cdd:TIGR01347 298 ADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGM---HGIKErPVAVNGQIE---IRPMMYLALS 371

                         410       420       430
                  ....*....|....*....|....*....|
gi 52076491   455 ADHRVFDGQVGGKFFTELSQNFGDIRRLLL 484
Cdd:TIGR01347 372 YDHRLIDGKEAVTFLVTIKELLEDPRRLLL 401
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 72-484 3.08e-78

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 253.98  E-value: 3.08e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491   72 GNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSKdVQVGQPIAVtVEDLEDIKNIPADASFGGE 151
Cdd:PRK11855 133 VEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDK-VSVGSLLVV-IEVAAAAPAAAAAPAAAAP 210

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491  152 QKEQSIASEA--------QKVETDAAKESSIITRISPAAKLLIKEHRLDQSVLNASGPRGTLLKGDVLAALKLGASSSST 223
Cdd:PRK11855 211 AAAAAAAPAPapaaaaapAAAAPAAAAAPGKAPHASPAVRRLARELGVDLSQVKGTGKKGRITKEDVQAFVKGAMSAAAA 290

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491  224 KQKNAPAAPS------SQPTHDFqAQSVTIpqqndayEDIPNSQIRKVIAKRLLESKQTTPHLYLSQDVILDPLLAFRNE 297
Cdd:PRK11855 291 AAAAAAAAGGgglgllPWPKVDF-SKFGEI-------ETKPLSRIKKISAANLHRSWVTIPHVTQFDEADITDLEALRKQ 362

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491  298 LKEQH---GVKVSVNDIVIKAVALALRNVPEANAYWNND-KEQAQKcVSVDISIAVATEKGLMTPIIRNADQKTISAISS 373
Cdd:PRK11855 363 LKKEAekaGVKLTMLPFFIKAVVAALKEFPVFNASLDEDgDELTYK-KYFNIGFAVDTPNGLVVPVIKDVDKKSLLEIAR 441

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491  374 EVKQLAEKARAGKLAPNEFQGGTFSISNLGMYPVDHFCAIINPPQSGILAVGRGnkIIEPVvdSDGTEkatVVTK--MSL 451
Cdd:PRK11855 442 EIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKS--QMKPV--WDGKE---FVPRlmLPL 514

                        410       420       430
                 ....*....|....*....|....*....|...
gi 52076491  452 TLSADHRVFDGQVGGKFFTELSQNFGDIRRLLL 484
Cdd:PRK11855 515 SLSYDHRVIDGATAARFTNYLKQLLADPRRMLL 547
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 60-484 2.08e-65

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 222.19  E-value: 2.08e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491   60 VGMPALSPTmnQGNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSKdVQVGQPIAVtvedLEDI 139
Cdd:PRK11854 209 VNVPDIGGD--EVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDK-VKTGSLIMR----FEVE 281

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491  140 KNIPADASfGGEQKEQSIASEAQKVETDAA-----------KESSIITRISPAAKLLIKEHRLDQSVLNASGPRGTLLKG 208
Cdd:PRK11854 282 GAAPAAAP-AKQEAAAPAPAAAKAEAPAAApaakaegksefAENDAYVHATPLVRRLAREFGVNLAKVKGTGRKGRILKE 360

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491  209 DVLAALKlgasSSSTKQKNAPAAPSSQ---------PTHDFQAQSVTipqqndayEDIPNSQIRKVIAKRLLESKQTTPH 279
Cdd:PRK11854 361 DVQAYVK----DAVKRAEAAPAAAAAGgggpgllpwPKVDFSKFGEI--------EEVELGRIQKISGANLHRNWVMIPH 428

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491  280 LYLSQDVILDPLLAFRNE-----LKEQHGVKVSVNDIVIKAVALALRNVPEANAYWNNDKEQAQKCVSVDISIAVATEKG 354
Cdd:PRK11854 429 VTQFDKADITELEAFRKQqnaeaEKRKLGVKITPLVFIMKAVAAALEQMPRFNSSLSEDGQRLTLKKYVNIGIAVDTPNG 508

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491  355 LMTPIIRNADQKTISAISSEVKQLAEKARAGKLAPNEFQGGTFSISNLGMYPVDHFCAIINPPQSGILAVGRGNKiiEPV 434
Cdd:PRK11854 509 LVVPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKSAM--EPV 586

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 52076491  435 vdsDGTEKATVVTKMSLTLSADHRVFDGQVGGKFFTELSQNFGDIRRLLL 484
Cdd:PRK11854 587 ---WNGKEFAPRLMLPLSLSYDHRVIDGADGARFITIINDRLSDIRRLVL 633
PTZ00144 PTZ00144
dihydrolipoamide succinyltransferase; Provisional
 58-484 3.11e-59

dihydrolipoamide succinyltransferase; Provisional


Pssm-ID: 240289 [Multi-domain]  Cd Length: 418  Bit Score: 200.68  E-value: 3.11e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491   58 LVVGMPALSPTMNQGNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSkDVQVGQPIAVtvedle 137
Cdd:PTZ00144  45 KVIKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGD-TVEVGAPLSE------ 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491  138 dIKNIPADASFGGEQKEQSIASEAQKVETDAAKESSiitrisPAAKllikehrldqsvlnasgprgtllkgdvlaalklg 217
Cdd:PTZ00144 118 -IDTGGAPPAAAPAAAAAAKAEKTTPEKPKAAAPTP------EPPA---------------------------------- 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491  218 ASSSSTKQKNAPAAPSSQPTHDFQAQSVTIPQQndayEDIPNSQIRKVIAKRLLESKQTTPHLYLSQDVILDPLLAFRNE 297
Cdd:PTZ00144 157 ASKPTPPAAAKPPEPAPAAKPPPTPVARADPRE----TRVPMSRMRQRIAERLKASQNTCAMLTTFNECDMSALMELRKE 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491  298 LKEQ----HGVKVSVNDIVIKAVALALRNVPEANAYWNNDkeqaqkCVS----VDISIAVATEKGLMTPIIRNADQKTIS 369
Cdd:PTZ00144 233 YKDDfqkkHGVKLGFMSAFVKASTIALKKMPIVNAYIDGD------EIVyrnyVDISVAVATPTGLVVPVIRNCENKSFA 306

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491  370 AISSEVKQLAEKARAGKLAPNEFQGGTFSISNLGMYPVDHFCAIINPPQSGIL--------AVGRGNKI-IEPVvdsdgt 440
Cdd:PTZ00144 307 EIEKELADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILgmhaikkrPVVVGNEIvIRPI------ 380

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 52076491  441 ekatvvtkMSLTLSADHRVFDGQVGGKFFTELSQNFGDIRRLLL 484
Cdd:PTZ00144 381 --------MYLALTYDHRLIDGRDAVTFLKKIKDLIEDPARMLL 416
PRK14843 PRK14843
dihydrolipoamide acetyltransferase; Provisional
 138-474 8.80e-53

dihydrolipoamide acetyltransferase; Provisional


Pssm-ID: 184847 [Multi-domain]  Cd Length: 347  Bit Score: 181.64  E-value: 8.80e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491  138 DIKNIPADASFGGEQKEQsiaseaqkVETdaAKESSIItRISPAAKLLIKEHRLDQSVLNASGPRGTLLKGDVLAALklg 217
Cdd:PRK14843  22 NLYDVSGSGANGRVHKED--------VET--YKDTNVV-RISPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALL--- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491  218 asssSTKQKNAPAAPSSQPTHDFQAQSVTIPQQNdaYEDIPNSQIRKVIAKRLLESKQTTPHLYLSQDVILDPLLAFRNE 297
Cdd:PRK14843  88 ----PENIENDSIKSPAQIEKVEEVPDNVTPYGE--IERIPMTPMRKVIAQRMVESYLTAPTFTLNYEVDMTEMLALRKK 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491  298 L----KEQHGVKVSVNDIVIKAVALALRNVPEANAYWNNDKEQAQKCVSVDISIAVATEKGLMTPIIRNADQKTISAISS 373
Cdd:PRK14843 162 VlepiMEATGKKTTVTDLLSLAVVKTLMKHPYINASLTEDGKTIITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVV 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491  374 EVKQLAEKARAGKLAPNEFQGGTFSISNLGMYPVDHFCAIINPPQSGILAVgrGNKIIEPVVDSDgteKATVVTKMSLTL 453
Cdd:PRK14843 242 AFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQPNSAILGV--SSTIEKPVVVNG---EIVIRPIMSLGL 316

                        330       340
                 ....*....|....*....|.
gi 52076491  454 SADHRVFDGQVGGKFFTELSQ 474
Cdd:PRK14843 317 TIDHRVVDGMAGAKFMKDLKE 337
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 82-484 9.83e-53

pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]


Pssm-ID: 273566 [Multi-domain]  Cd Length: 546  Bit Score: 186.62  E-value: 9.83e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491    82 GEKIEVGDVICEIETDKATLEF----------------ESLEEGYLAKILAPEGSKDVQVGQPIAVTvedledikniPAD 145
Cdd:TIGR01348 140 GDTVSADQSLITLESDKASMEVpapasgvvksvkvkvgDSVPTGDLILTLSVAGSTPATAPAPASAQ----------PAA 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491   146 ASFGGEQKEQSIASEAQKVETDAAKES-----SIITRISPAAKLLIKEHRLDQSVLNASGPRGTLLKGDVLAALKlgass 220
Cdd:TIGR01348 210 QSPAATQPEPAAAPAAAKAQAPAPQQAgtqnpAKVDHAAPAVRRLAREFGVDLSAVKGTGIKGRILREDVQRFVK----- 284

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491   221 ssTKQKNAPAAPSSqpTHDFQAQSVTIPQQN----DAYEDIPNSQIRKVIAKRLLESKQTTPHLYLSQDVILDPLLAFR- 295
Cdd:TIGR01348 285 --EPSVRAQAAAAS--AAGGAPGALPWPNVDfskfGEVEEVDMSRIRKISGANLTRNWTMIPHVTHFDKADITEMEAFRk 360

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491   296 --NELKEQHGVKVSVNDIVIKAVALALRNVPEANAYWNNDKEQAQKCVSVDISIAVATEKGLMTPIIRNADQKTISAISS 373
Cdd:TIGR01348 361 qqNAAVEKEGVKLTVLHILMKAVAAALKKFPKFNASLDLGGEQLILKKYVNIGVAVDTPNGLLVPVIKDVDRKGITELAL 440

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491   374 EVKQLAEKARAGKLAPNEFQGGTFSISNLGMYPVDHFCAIINPPQSGILAVGRGnkIIEPVvdSDGTEKATVVTkMSLTL 453
Cdd:TIGR01348 441 ELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKS--GMEPV--WNGKEFEPRLM-LPLSL 515

                         410       420       430
                  ....*....|....*....|....*....|.
gi 52076491   454 SADHRVFDGQVGGKFFTELSQNFGDIRRLLL 484
Cdd:TIGR01348 516 SYDHRVIDGADAARFTTYICESLADIRRLLL 546
PLN02528 PLN02528
2-oxoisovalerate dehydrogenase E2 component
 76-484 1.42e-47

2-oxoisovalerate dehydrogenase E2 component


Pssm-ID: 215289 [Multi-domain]  Cd Length: 416  Bit Score: 169.51  E-value: 1.42e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491   76 KWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSKdVQVGQP-IAVTVEDLEDIKNIPADASFGGEqKE 154
Cdd:PLN02528  17 RWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDI-VKVGETlLKIMVEDSQHLRSDSLLLPTDSS-NI 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491  155 QSIASEAQKVETdaakESSIITriSPAAKLLIKEHRLDQSVLNASGPRGTLLKGDVL--AALKLGASSSSTKQKNAPAAP 232
Cdd:PLN02528  95 VSLAESDERGSN----LSGVLS--TPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLkyAAQKGVVKDSSSAEEATIAEQ 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491  233 SSQPTHdfqaqSVTIPQQNDAYEDIPNSQIRKVIAKRLLESKQTtPHLYLSQDVILDPLLAFR---NELKEQHGVKVSVN 309
Cdd:PLN02528 169 EEFSTS-----VSTPTEQSYEDKTIPLRGFQRAMVKTMTAAAKV-PHFHYVEEINVDALVELKasfQENNTDPTVKHTFL 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491  310 DIVIKAVALALRNVPEANAYWNNDKEQAQKCVSVDISIAVATEKGLMTPIIRNADQKTISAISSEVKQLAEKARAGKLAP 389
Cdd:PLN02528 243 PFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAAENKLNP 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491  390 NEFQGGTFSISNLGMYPVDHFCAIINPPQSGILAVGRGNKIiePVVDSDGTEKATVVtkMSLTLSADHRVFDGQVGGKFF 469
Cdd:PLN02528 323 EDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKV--PRFVDDGNVYPASI--MTVTIGADHRVLDGATVARFC 398

                        410
                 ....*....|....*
gi 52076491  470 TELSQNFGDIRRLLL 484
Cdd:PLN02528 399 NEWKSYVEKPELLML 413
SucB_Actino TIGR02927
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ...
 60-470 4.21e-42

2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model represents an Actinobacterial clade of E2 enzyme, a component of the 2-oxoglutarate dehydrogenase complex involved in the TCA cycle. These proteins have multiple domains including the catalytic domain (pfam00198), one or two biotin domains (pfam00364) and an E3-component binding domain (pfam02817).


Pssm-ID: 200219 [Multi-domain]  Cd Length: 579  Bit Score: 157.87  E-value: 4.21e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491    60 VGMPALSPTMNQGNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEgSKDVQVGQPIAVTVEDLED- 138
Cdd:TIGR02927   5 VKMPALGESVTEGTVTSWLKAVGDTVEADEPLLEVSTDKVDTEIPSPAAGVLLEIRAPE-DDTVEVGGVLAIIGEPGEAg 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491   139 ---------------------------------------------------------------IKNI------------- 142
Cdd:TIGR02927  84 sepapaapepeaapepeapapaptpaaeapapaapqaggsgeatevkmpelgesvtegtvtswLKAVgdtvevdepllev 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491   143 ----------------------------------------------------PADASFGGEQKEQSIASEAQKVETDAAK 170
Cdd:TIGR02927 164 stdkvdteipspvagtlleirapeddtvevgtvlaiigdanaapaepaeeeaPAPSEAGSEPAPDPAARAPHAAPDPPAP 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491   171 -----------------ESSIITRISPAAKLLIKEHRLDQSVLNASGPRGTLLKGDVLAALKLGASSSSTKQKNAPAAPS 233
Cdd:TIGR02927 244 apapaktaapaaaapvsSGDSGPYVTPLVRKLAKDKGVDLSTVKGTGVGGRIRKQDVLAAAKAAEEARAAAAAPAAAAAP 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491   234 SQPTHDFQAQSVTIPQQNDAYEDIpnSQIRKVIAKRLLESKQTTPHLYLSQDVILDPLLAFR----NELKEQHGVKVSVN 309
Cdd:TIGR02927 324 AAPAAAAKPAEPDTAKLRGTTQKM--NRIRQITADKTIESLQTSAQLTQVHEVDMTRVAALRarakNDFLEKNGVNLTFL 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491   310 DIVIKAVALALRNVPEANAYWNNDKEQAQKCVSVDISIAVATEKGLMTPIIRNADQKTISAISSEVKQLAEKARAGKLAP 389
Cdd:TIGR02927 402 PFFVQAVTEALKAHPNVNASYNAETKEVTYHDVEHVGIAVDTPRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKP 481

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491   390 NEFQGGTFSISNLGMYPVDHFCAIINPPQSGILAVGRGNKIIEPVVDSDGTEKATVVTKMSLTLSADHRVFDGQVGGKFF 469
Cdd:TIGR02927 482 DELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAIVKRPRVIKDEDGGESIAIRSVCYLPLTYDHRLVDGADAGRFL 561


                  .
gi 52076491   470 T 470
Cdd:TIGR02927 562 T 562
PLN02226 PLN02226
2-oxoglutarate dehydrogenase E2 component
 47-484 9.70e-42

2-oxoglutarate dehydrogenase E2 component


Pssm-ID: 177871 [Multi-domain]  Cd Length: 463  Bit Score: 154.91  E-value: 9.70e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491   47 RWL----SSTGFPPHLVVgmPALSPTMNQGNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSKd 122
Cdd:PLN02226  79 RWVrpfsSESGDTVEAVV--PHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDT- 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491  123 VQVGQPIAVTvedlediknipadasfggeqkeqsiaseaqkvetdaAKESSIITRISPAAKLlikehrldqsvlnasgPR 202
Cdd:PLN02226 156 VEPGTKVAII------------------------------------SKSEDAASQVTPSQKI----------------PE 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491  203 GTLLKGDVLAALKLGASSSSTKQKNAPAAPSSQPTHDFQAQSVTIPQQnDAYEDIPNSQIRKVIAKRLLESKQTTPHLYL 282
Cdd:PLN02226 184 TTDPKPSPPAEDKQKPKVESAPVAEKPKAPSSPPPPKQSAKEPQLPPK-ERERRVPMTRLRKRVATRLKDSQNTFALLTT 262

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491  283 SQDVILDPLLAFRNELK----EQHGVKVSVNDIVIKAVALALRNVPEANAYWNNDKEQAQKcvSVDISIAVATEKGLMTP 358
Cdd:PLN02226 263 FNEVDMTNLMKLRSQYKdafyEKHGVKLGLMSGFIKAAVSALQHQPVVNAVIDGDDIIYRD--YVDISIAVGTSKGLVVP 340

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491  359 IIRNADQKTISAISSEVKQLAEKARAGKLAPNEFQGGTFSISNLGMYPVDHFCAIINPPQSGILavGRGNKIIEPVVDSd 438
Cdd:PLN02226 341 VIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAIL--GMHSIVSRPMVVG- 417

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 52076491  439 gtekATVVTK--MSLTLSADHRVFDGQVGGKFFTELSQNFGDIRRLLL 484
Cdd:PLN02226 418 ----GSVVPRpmMYVALTYDHRLIDGREAVYFLRRVKDVVEDPQRLLL 461
PRK11857 PRK11857
dihydrolipoamide acetyltransferase; Reviewed
 178-474 9.80e-38

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237002 [Multi-domain]  Cd Length: 306  Bit Score: 139.93  E-value: 9.80e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491  178 ISPAAKLLIKEHRLDQSVLNASGPRGTLLKGDVLaalKLGASSSSTKQKNAPAAPSSQPTHDFQAQSVTIPQQNDAYEDi 257
Cdd:PRK11857   4 ATPIARALAKKLGIDISLLKGSGRDGKILAEDVE---NFIKSLKSAPTPAEAASVSSAQQAAKTAAPAAAPPKLEGKRE- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491  258 PNSQIRKVIAKRLLESKQTTPHLYLSQDVILDPLLAFRNELKEQ----HGVKVSVNDIVIKAVALALRNVPEANAYWNND 333
Cdd:PRK11857  80 KVAPIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPvlktEGVKLTFLPFIAKAILIALKEFPIFAAKYDEA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491  334 KEQAQKCVSVDISIAVATEKGLMTPIIRNADQKTISAISSEVKQLAEKARAGKLAPNEFQGGTFSISNLGMYPVDHFCAI 413
Cdd:PRK11857 160 TSELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLYGVPV 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 52076491  414 INPPQSGILAVGrgnKIIEPVVDSDGTEKATVVtkMSLTLSADHRVFDGQVGGKFFTELSQ 474
Cdd:PRK11857 240 INYPELAIAGVG---AIIDKAIVKNGQIVAGKV--MHLTVAADHRWIDGATIGRFASRVKE 295
PRK11892 PRK11892
pyruvate dehydrogenase subunit beta; Provisional
 62-174 1.57e-35

pyruvate dehydrogenase subunit beta; Provisional


Pssm-ID: 237011 [Multi-domain]  Cd Length: 464  Bit Score: 137.74  E-value: 1.57e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491   62 MPALSPTMNQGNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSKDVQVGQPIAVTVEDLEDIKN 141
Cdd:PRK11892   7 MPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEGVKVNTPIAVLLEEGESASD 86

                         90       100       110
                 ....*....|....*....|....*....|...
gi 52076491  142 IPADASFGGEQKEQSIASEAQKVETDAAKESSI 174
Cdd:PRK11892  87 AGAAPAAAAEAAAAAPAAAAAAAAKKAAPAPAA 119
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 62-131 1.27e-27

Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.


Pssm-ID: 133458 [Multi-domain]  Cd Length: 74  Bit Score: 105.18  E-value: 1.27e-27
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491  62 MPALSPTMNQGNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSKdVQVGQPIAV 131
Cdd:cd06849   5 MPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAV 73
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 62-131 2.85e-25

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


Pssm-ID: 440274 [Multi-domain]  Cd Length: 77  Bit Score: 98.60  E-value: 2.85e-25
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491  62 MPALSPTMNQGNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSKdVQVGQPIAV 131
Cdd:COG0508   7 MPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDT-VPVGAVIAV 75
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 60-168 2.48e-16

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 80.37  E-value: 2.48e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491   60 VGMPALSPTMNQGNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSkDVQVGQPIAV----TVED 135
Cdd:PRK14875   5 ITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGE-TLPVGALLAVvadaEVSD 83

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 52076491  136 LED---IKNIPADASFGGEQkEQSIASEAQKVETDA 168
Cdd:PRK14875  84 AEIdafIAPFARRFAPEGID-EEDAGPAPRKARIGG 118
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 59-131 2.82e-16

Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.


Pssm-ID: 395290 [Multi-domain]  Cd Length: 73  Bit Score: 73.40  E-value: 2.82e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 52076491    59 VVGMPALSPTMNQGnIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSKdVQVGQPIAV 131
Cdd:pfam00364   2 EIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDT-VEVGDPLAK 72
Biotinyl_lipoyl_domains cd06663
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ...
 60-129 1.91e-15

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


Pssm-ID: 133456 [Multi-domain]  Cd Length: 73  Bit Score: 70.93  E-value: 1.91e-15
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491  60 VGMPALSPTMNQGNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSKdVQVGQPI 129
Cdd:cd06663   2 ILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTK-VEGDTPL 70
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
 296-474 8.21e-10

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


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 61.44  E-value: 8.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491   296 NELKEQHGVKVSVNDIVIKAVALALRNVPEANAYWN--NDKEQAQKCVSVDISIAVATEK-----GLMTPIIRNADQKTI 368
Cdd:PRK12270  160 NHLKRTRGGKVSFTHLIGYALVQALKAFPNMNRHYAevDGKPTLVTPAHVNLGLAIDLPKkdgsrQLVVPAIKGAETMDF 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491   369 SAISSEVKQLAEKARAGKLAPNEFQGGTFSISNLGMYPVDHFCAIINPPQSGILAVGRgnkiIEPVVDSDGTEKATV--- 445
Cdd:PRK12270  240 AQFWAAYEDIVRRARDGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGA----MEYPAEFQGASEERLael 315

                         170       180       190
                  ....*....|....*....|....*....|.
gi 52076491   446 -VTK-MSLTLSADHRVFDGQVGGKFFTELSQ 474
Cdd:PRK12270  316 gISKvMTLTSTYDHRIIQGAESGEFLRTIHQ 346
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 71-131 3.49e-06

The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.


Pssm-ID: 133459 [Multi-domain]  Cd Length: 67  Bit Score: 44.33  E-value: 3.49e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 52076491  71 QGNIAKWRKQEGEKIEVGDVICEIETDKATLEFESLEEGYLAKILAPEGSKdVQVGQPIAV 131
Cdd:cd06850   7 PGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQ-VEAGQLLVV 66
E3_binding pfam02817
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ...
 177-211 1.55e-05

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


Pssm-ID: 460710 [Multi-domain]  Cd Length: 36  Bit Score: 41.90  E-value: 1.55e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 52076491   177 RISPAAKLLIKEHRLDQSVLNASGPRGTLLKGDVL 211
Cdd:pfam02817   2 LASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
PRK09282 PRK09282
pyruvate carboxylase subunit B; Validated
 22-131 2.61e-04

pyruvate carboxylase subunit B; Validated


Pssm-ID: 236449 [Multi-domain]  Cd Length: 592  Bit Score: 43.68  E-value: 2.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52076491   22 GRCVSSSRPSYLASLGRHYKVPME-IRWLSSTGFPPHLVVGmpALSPTMnQGNIAKWRKQEGEKIEVGDVICEIETDKAT 100
Cdd:PRK09282 483 GVKAEGKRPFYLRVDGMPEEVVVEpLKEIVVGGRPRASAPG--AVTSPM-PGTVVKVKVKEGDKVKAGDTVLVLEAMKME 559

                         90       100       110
                 ....*....|....*....|....*....|.
gi 52076491  101 LEFESLEEGYLAKILAPEGsKDVQVGQPIAV 131
Cdd:PRK09282 560 NEIQAPVDGTVKEILVKEG-DRVNPGDVLME 589
 
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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