NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|6679263|ref|NP_032837|]
View 

pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrial precursor [Mus musculus]

Protein Classification

pyruvate dehydrogenase (acetyl-transferring) E1 component subunit alpha( domain architecture ID 10799057)

pyruvate dehydrogenase (acetyl-transferring) E1 component subunit alpha is part of the thiamine pyrophosphate-dependent enzyme complex that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2)

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PDH_E1_alph_y TIGR03182
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the ...
59-371 2.77e-177

pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the alpha subunit of the E1 component of pyruvate dehydrogenase (PDH). This model represents one branch of a larger family that E1-alpha proteins from 2-oxoisovalerate dehydrogenase, acetoin dehydrogenase, another PDH clade, etc. [Energy metabolism, Pyruvate dehydrogenase]


:

Pssm-ID: 274473 [Multi-domain]  Cd Length: 315  Bit Score: 495.55  E-value: 2.77e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679263     59 RAEALKYYRTMQVIRRMELKADQLYKQKFIRGFCHLCDGQEACCVGLEAGINPTDHVITSYRAHGFCYTRGLSVKSILAE 138
Cdd:TIGR03182   1 KEELLELYRDMLLIRRFEEKAGQLYGMGKIGGFCHLYIGQEAVAVGLIAALKPDDYVITSYRDHGHALARGVPPKEVMAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679263    139 LTGRKGGCAKGKGGSMHMYG--KNFYGGNGIVGAQVPLGAGVAFACKYLKNGQVCLALYGDGAANQGQVFEAYNMSALWK 216
Cdd:TIGR03182  81 LTGRETGCSKGKGGSMHMFDreKNFYGGHGIVGAQVPLATGLAFANKYRGNDNVTACFFGDGAANQGQFYESFNMAALWK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679263    217 LPCVFICENNLYGMGTSNERSAASTDYHKKG--FIIPGLRVNGMDILCVREATKFAADHCRSGKGPIVMELQTYRYHGHS 294
Cdd:TIGR03182 161 LPVIFVIENNLYAMGTAVERSSSVTDLYKRGesFGIPGERVDGMDVLAVREAAKEAVERARSGKGPILLEMKTYRFRGHS 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6679263    295 MSDPGiSYRSREEVHNVRsKSDPIMLLRERIISNNLSNIEELKEIDADVKKEVEDAAQFATTDPEPAVEDIANYLYH 371
Cdd:TIGR03182 241 MSDPA-KYRSKEEVEEWR-KRDPIEKLKARLIEQGIASEEELKEIDKEVRAEVEEAVEFAENSPEPPVEELYTDVYA 315
 
Name Accession Description Interval E-value
PDH_E1_alph_y TIGR03182
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the ...
59-371 2.77e-177

pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the alpha subunit of the E1 component of pyruvate dehydrogenase (PDH). This model represents one branch of a larger family that E1-alpha proteins from 2-oxoisovalerate dehydrogenase, acetoin dehydrogenase, another PDH clade, etc. [Energy metabolism, Pyruvate dehydrogenase]


Pssm-ID: 274473 [Multi-domain]  Cd Length: 315  Bit Score: 495.55  E-value: 2.77e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679263     59 RAEALKYYRTMQVIRRMELKADQLYKQKFIRGFCHLCDGQEACCVGLEAGINPTDHVITSYRAHGFCYTRGLSVKSILAE 138
Cdd:TIGR03182   1 KEELLELYRDMLLIRRFEEKAGQLYGMGKIGGFCHLYIGQEAVAVGLIAALKPDDYVITSYRDHGHALARGVPPKEVMAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679263    139 LTGRKGGCAKGKGGSMHMYG--KNFYGGNGIVGAQVPLGAGVAFACKYLKNGQVCLALYGDGAANQGQVFEAYNMSALWK 216
Cdd:TIGR03182  81 LTGRETGCSKGKGGSMHMFDreKNFYGGHGIVGAQVPLATGLAFANKYRGNDNVTACFFGDGAANQGQFYESFNMAALWK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679263    217 LPCVFICENNLYGMGTSNERSAASTDYHKKG--FIIPGLRVNGMDILCVREATKFAADHCRSGKGPIVMELQTYRYHGHS 294
Cdd:TIGR03182 161 LPVIFVIENNLYAMGTAVERSSSVTDLYKRGesFGIPGERVDGMDVLAVREAAKEAVERARSGKGPILLEMKTYRFRGHS 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6679263    295 MSDPGiSYRSREEVHNVRsKSDPIMLLRERIISNNLSNIEELKEIDADVKKEVEDAAQFATTDPEPAVEDIANYLYH 371
Cdd:TIGR03182 241 MSDPA-KYRSKEEVEEWR-KRDPIEKLKARLIEQGIASEEELKEIDKEVRAEVEEAVEFAENSPEPPVEELYTDVYA 315
PLN02269 PLN02269
Pyruvate dehydrogenase E1 component subunit alpha
32-381 2.20e-160

Pyruvate dehydrogenase E1 component subunit alpha


Pssm-ID: 215152 [Multi-domain]  Cd Length: 362  Bit Score: 454.94  E-value: 2.20e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679263    32 SNDATCDIKKC-DLYRLEegPPTSTVLT-RAEALKYYRTMQVIRRMELKADQLYKQKFIRGFCHLCDGQEACCVGLEAGI 109
Cdd:PLN02269   2 TDPITIETPVPfKGHLCD--PPSRTVETsKQELVDFFRDMYLMRRMEIAADSLYKAKLIRGFCHLYDGQEAVAVGMEAAI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679263   110 NPTDHVITSYRAHGFCYTRGLSVKSILAELTGRKGGCAKGKGGSMHMYGK--NFYGGNGIVGAQVPLGAGVAFACKYLKN 187
Cdd:PLN02269  80 TKEDAIITAYRDHCTHLGRGGTVLEVFAELMGRKDGCSRGKGGSMHFYKKdaNFYGGHGIVGAQVPLGAGLAFAQKYNKE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679263   188 GQVCLALYGDGAANQGQVFEAYNMSALWKLPCVFICENNLYGMGTSNERSAASTDYHKKGFIIPGLRVNGMDILCVREAT 267
Cdd:PLN02269 160 ENVAFALYGDGAANQGQLFEALNIAALWDLPVIFVCENNHYGMGTAEWRAAKSPAYYKRGDYVPGLKVDGMDVLAVKQAC 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679263   268 KFAADHCRSgKGPIVMELQTYRYHGHSMSDPGISYRSREEVHNVRSKSDPIMLLRERIISNNLSNIEELKEIDADVKKEV 347
Cdd:PLN02269 240 KFAKEHALS-NGPIVLEMDTYRYHGHSMSDPGSTYRTRDEISGVRQERDPIERVRKLLLAHELATEAELKDIEKEIRKEV 318
                        330       340       350
                 ....*....|....*....|....*....|....
gi 6679263   348 EDAAQFATTDPEPAVEDIANYLYHQDPPFEVRGA 381
Cdd:PLN02269 319 DDAVAKAKESPMPDPSELFTNVYVKGLGVESYGA 352
E1_dh pfam00676
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ...
67-363 2.77e-142

Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family includes pyruvate dehydrogenase, 2-oxoglutarate dehydrogenase and 2-oxoisovalerate dehydrogenase.


Pssm-ID: 395548 [Multi-domain]  Cd Length: 300  Bit Score: 406.33  E-value: 2.77e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679263     67 RTMQVIRRMELKADQLYKQKFIRGFCHLCDGQEACCVGLEAGINPTDHVITSYRAHGFCYTRGLSVKSILAELTGRKGGC 146
Cdd:pfam00676   1 RRMMTLRRMEDARDALYKRQGIRGFYHLYAGQEAAQVGIAAALEPGDYIIPGYRDHGNLLARGLSLEEIFAELYGRVAKG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679263    147 AKGkggSMHMY----GKNFYGGNGIVGAQVPLGAGVAFACKYLKNGQVCLALYGDGAANQGQVFEAYNMSALWKLPCVFI 222
Cdd:pfam00676  81 KGG---SMHGYygakGNRFYGGNGILGAQVPLGAGIALAAKYRGKKEVAITLYGDGAANQGDFFEGLNFAALWKLPVIFV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679263    223 CENNLYGMGTSNERSAASTDYHKK--GFIIPGLRVNGMDILCVREATKFAADHCRSGKGPIVMELQTYRYHGHSMSDPGI 300
Cdd:pfam00676 158 CENNQYGISTPAERASASTTYADRarGYGIPGLHVDGMDPLAVYQASKFAAERARTGKGPFLIELVTYRYGGHSMSDDPS 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6679263    301 SYRSREEVHNVRSKSDPIMLLRERIISNNLSNIEELKEIDADVKKEVEDAAQFATTDPEPAVE 363
Cdd:pfam00676 238 TYRTRDEYEEVRKKKDPIQRFKEHLVSKGVWSEEELKAIEKEVRKEVEEAFKKAESAPEPHPE 300
TPP_E1_PDC_ADC_BCADC cd02000
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ...
65-354 3.33e-139

Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; composed of proteins similar to the E1 components of the human pyruvate dehydrogenase complex (PDC), the acetoin dehydrogenase complex (ADC) and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC). PDC catalyzes the irreversible oxidative decarboxylation of pyruvate to produce acetyl-CoA in the bridging step between glycolysis and the citric acid cycle. ADC participates in the breakdown of acetoin while BCADC participates in the breakdown of branched chain amino acids. BCADC catalyzes the oxidative decarboxylation of 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate (branched chain 2-oxo acids derived from the transamination of leucine, valine and isoleucine).


Pssm-ID: 238958 [Multi-domain]  Cd Length: 293  Bit Score: 398.41  E-value: 3.33e-139
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679263   65 YYRTMQVIRRMELKADQLYKQKFIRGFCHLCDGQEACCVGLEAGINPTDHVITSYRAHGFCYTRGLSVKSILAELTGRKG 144
Cdd:cd02000   1 LYRTMVLIRRFDERLLELYRQGKIGGFYHLSIGQEAVAVGVAAALRPGDWVFPTYRDHGHALARGVDLKEMLAELFGKET 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679263  145 GCAKGKGGSMHM--YGKNFYGGNGIVGAQVPLGAGVAFACKYLKNGQVCLALYGDGAANQGQVFEAYNMSALWKLPCVFI 222
Cdd:cd02000  81 GPCKGRGGSMHIgdKEKNFFGGNGIVGGQVPLAAGAALALKYRGEDRVAVCFFGDGATNEGDFHEALNFAALWKLPVIFV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679263  223 CENNLYGMGTSNERSAASTDYHKKG--FIIPGLRVNGMDILCVREATKFAADHCRSGKGPIVMELQTYRYHGHSMSDPGI 300
Cdd:cd02000 161 CENNGYAISTPTSRQTAGTSIADRAaaYGIPGIRVDGNDVLAVYEAAKEAVERARAGGGPTLIEAVTYRLGGHSTSDDPS 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 6679263  301 SYRSREEVhNVRSKSDPIMLLRERIISNNLSNIEELKEIDADVKKEVEDAAQFA 354
Cdd:cd02000 241 RYRTKEEV-EEWKKRDPILRLRKYLIEAGILTEEELAAIEAEVKAEVEEAVEFA 293
AcoA COG1071
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ...
57-375 3.18e-134

TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and conversion]; TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 440689 [Multi-domain]  Cd Length: 348  Bit Score: 387.57  E-value: 3.18e-134
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679263   57 LTRAEALKYYRTMQVIRRMELKADQLYKQKFIrGFCHLCDGQEACCVGLEAGINPTDHVITSYRAHGFCYTRGLSVKSIL 136
Cdd:COG1071  17 LSKEELLELYRDMLLIRRFEERALALQRQGKI-GFYHLSIGQEAAQVGAAAALRPGDWIFPTYRDHGHALARGVDPKELM 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679263  137 AELTGRKGGCAKGKGGSMHMYGK--NFYGGNGIVGAQVPLGAGVAFACKYLKNGQVCLALYGDGAANQGQVFEAYNMSAL 214
Cdd:COG1071  96 AELFGKATGPSKGRGGSMHFFDKelNFLGGSGIVGGQLPHAVGAALAAKLRGEDEVAVAFFGDGATSEGDFHEALNFAAV 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679263  215 WKLPCVFICENNLYGMGTSNERSAASTDYHKK--GFIIPGLRVNGMDILCVREATKFAADHCRSGKGPIVMELQTYRYHG 292
Cdd:COG1071 176 WKLPVVFVCENNGYAISTPVERQTAVETIADRaaGYGIPGVRVDGNDVLAVYAAVKEAVERARAGEGPTLIEAKTYRLGG 255
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679263  293 HSMSDPGISYRSREEVHNVRSKsDPIMLLRERIISNNLSNIEELKEIDADVKKEVEDAAQFATTDPEPAVEDIANYLYHQ 372
Cdd:COG1071 256 HSTSDDPTRYRTKEEVEEWRER-DPIERLRAYLLEEGLLTEEELEAIEAEAKAEVEEAVEFAEASPEPDPEELFDDVYAE 334

                ...
gi 6679263  373 DPP 375
Cdd:COG1071 335 PPP 337
 
Name Accession Description Interval E-value
PDH_E1_alph_y TIGR03182
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the ...
59-371 2.77e-177

pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the alpha subunit of the E1 component of pyruvate dehydrogenase (PDH). This model represents one branch of a larger family that E1-alpha proteins from 2-oxoisovalerate dehydrogenase, acetoin dehydrogenase, another PDH clade, etc. [Energy metabolism, Pyruvate dehydrogenase]


Pssm-ID: 274473 [Multi-domain]  Cd Length: 315  Bit Score: 495.55  E-value: 2.77e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679263     59 RAEALKYYRTMQVIRRMELKADQLYKQKFIRGFCHLCDGQEACCVGLEAGINPTDHVITSYRAHGFCYTRGLSVKSILAE 138
Cdd:TIGR03182   1 KEELLELYRDMLLIRRFEEKAGQLYGMGKIGGFCHLYIGQEAVAVGLIAALKPDDYVITSYRDHGHALARGVPPKEVMAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679263    139 LTGRKGGCAKGKGGSMHMYG--KNFYGGNGIVGAQVPLGAGVAFACKYLKNGQVCLALYGDGAANQGQVFEAYNMSALWK 216
Cdd:TIGR03182  81 LTGRETGCSKGKGGSMHMFDreKNFYGGHGIVGAQVPLATGLAFANKYRGNDNVTACFFGDGAANQGQFYESFNMAALWK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679263    217 LPCVFICENNLYGMGTSNERSAASTDYHKKG--FIIPGLRVNGMDILCVREATKFAADHCRSGKGPIVMELQTYRYHGHS 294
Cdd:TIGR03182 161 LPVIFVIENNLYAMGTAVERSSSVTDLYKRGesFGIPGERVDGMDVLAVREAAKEAVERARSGKGPILLEMKTYRFRGHS 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6679263    295 MSDPGiSYRSREEVHNVRsKSDPIMLLRERIISNNLSNIEELKEIDADVKKEVEDAAQFATTDPEPAVEDIANYLYH 371
Cdd:TIGR03182 241 MSDPA-KYRSKEEVEEWR-KRDPIEKLKARLIEQGIASEEELKEIDKEVRAEVEEAVEFAENSPEPPVEELYTDVYA 315
PLN02269 PLN02269
Pyruvate dehydrogenase E1 component subunit alpha
32-381 2.20e-160

Pyruvate dehydrogenase E1 component subunit alpha


Pssm-ID: 215152 [Multi-domain]  Cd Length: 362  Bit Score: 454.94  E-value: 2.20e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679263    32 SNDATCDIKKC-DLYRLEegPPTSTVLT-RAEALKYYRTMQVIRRMELKADQLYKQKFIRGFCHLCDGQEACCVGLEAGI 109
Cdd:PLN02269   2 TDPITIETPVPfKGHLCD--PPSRTVETsKQELVDFFRDMYLMRRMEIAADSLYKAKLIRGFCHLYDGQEAVAVGMEAAI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679263   110 NPTDHVITSYRAHGFCYTRGLSVKSILAELTGRKGGCAKGKGGSMHMYGK--NFYGGNGIVGAQVPLGAGVAFACKYLKN 187
Cdd:PLN02269  80 TKEDAIITAYRDHCTHLGRGGTVLEVFAELMGRKDGCSRGKGGSMHFYKKdaNFYGGHGIVGAQVPLGAGLAFAQKYNKE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679263   188 GQVCLALYGDGAANQGQVFEAYNMSALWKLPCVFICENNLYGMGTSNERSAASTDYHKKGFIIPGLRVNGMDILCVREAT 267
Cdd:PLN02269 160 ENVAFALYGDGAANQGQLFEALNIAALWDLPVIFVCENNHYGMGTAEWRAAKSPAYYKRGDYVPGLKVDGMDVLAVKQAC 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679263   268 KFAADHCRSgKGPIVMELQTYRYHGHSMSDPGISYRSREEVHNVRSKSDPIMLLRERIISNNLSNIEELKEIDADVKKEV 347
Cdd:PLN02269 240 KFAKEHALS-NGPIVLEMDTYRYHGHSMSDPGSTYRTRDEISGVRQERDPIERVRKLLLAHELATEAELKDIEKEIRKEV 318
                        330       340       350
                 ....*....|....*....|....*....|....
gi 6679263   348 EDAAQFATTDPEPAVEDIANYLYHQDPPFEVRGA 381
Cdd:PLN02269 319 DDAVAKAKESPMPDPSELFTNVYVKGLGVESYGA 352
E1_dh pfam00676
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ...
67-363 2.77e-142

Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family includes pyruvate dehydrogenase, 2-oxoglutarate dehydrogenase and 2-oxoisovalerate dehydrogenase.


Pssm-ID: 395548 [Multi-domain]  Cd Length: 300  Bit Score: 406.33  E-value: 2.77e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679263     67 RTMQVIRRMELKADQLYKQKFIRGFCHLCDGQEACCVGLEAGINPTDHVITSYRAHGFCYTRGLSVKSILAELTGRKGGC 146
Cdd:pfam00676   1 RRMMTLRRMEDARDALYKRQGIRGFYHLYAGQEAAQVGIAAALEPGDYIIPGYRDHGNLLARGLSLEEIFAELYGRVAKG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679263    147 AKGkggSMHMY----GKNFYGGNGIVGAQVPLGAGVAFACKYLKNGQVCLALYGDGAANQGQVFEAYNMSALWKLPCVFI 222
Cdd:pfam00676  81 KGG---SMHGYygakGNRFYGGNGILGAQVPLGAGIALAAKYRGKKEVAITLYGDGAANQGDFFEGLNFAALWKLPVIFV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679263    223 CENNLYGMGTSNERSAASTDYHKK--GFIIPGLRVNGMDILCVREATKFAADHCRSGKGPIVMELQTYRYHGHSMSDPGI 300
Cdd:pfam00676 158 CENNQYGISTPAERASASTTYADRarGYGIPGLHVDGMDPLAVYQASKFAAERARTGKGPFLIELVTYRYGGHSMSDDPS 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6679263    301 SYRSREEVHNVRSKSDPIMLLRERIISNNLSNIEELKEIDADVKKEVEDAAQFATTDPEPAVE 363
Cdd:pfam00676 238 TYRTRDEYEEVRKKKDPIQRFKEHLVSKGVWSEEELKAIEKEVRKEVEEAFKKAESAPEPHPE 300
TPP_E1_PDC_ADC_BCADC cd02000
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ...
65-354 3.33e-139

Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; composed of proteins similar to the E1 components of the human pyruvate dehydrogenase complex (PDC), the acetoin dehydrogenase complex (ADC) and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC). PDC catalyzes the irreversible oxidative decarboxylation of pyruvate to produce acetyl-CoA in the bridging step between glycolysis and the citric acid cycle. ADC participates in the breakdown of acetoin while BCADC participates in the breakdown of branched chain amino acids. BCADC catalyzes the oxidative decarboxylation of 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate (branched chain 2-oxo acids derived from the transamination of leucine, valine and isoleucine).


Pssm-ID: 238958 [Multi-domain]  Cd Length: 293  Bit Score: 398.41  E-value: 3.33e-139
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679263   65 YYRTMQVIRRMELKADQLYKQKFIRGFCHLCDGQEACCVGLEAGINPTDHVITSYRAHGFCYTRGLSVKSILAELTGRKG 144
Cdd:cd02000   1 LYRTMVLIRRFDERLLELYRQGKIGGFYHLSIGQEAVAVGVAAALRPGDWVFPTYRDHGHALARGVDLKEMLAELFGKET 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679263  145 GCAKGKGGSMHM--YGKNFYGGNGIVGAQVPLGAGVAFACKYLKNGQVCLALYGDGAANQGQVFEAYNMSALWKLPCVFI 222
Cdd:cd02000  81 GPCKGRGGSMHIgdKEKNFFGGNGIVGGQVPLAAGAALALKYRGEDRVAVCFFGDGATNEGDFHEALNFAALWKLPVIFV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679263  223 CENNLYGMGTSNERSAASTDYHKKG--FIIPGLRVNGMDILCVREATKFAADHCRSGKGPIVMELQTYRYHGHSMSDPGI 300
Cdd:cd02000 161 CENNGYAISTPTSRQTAGTSIADRAaaYGIPGIRVDGNDVLAVYEAAKEAVERARAGGGPTLIEAVTYRLGGHSTSDDPS 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 6679263  301 SYRSREEVhNVRSKSDPIMLLRERIISNNLSNIEELKEIDADVKKEVEDAAQFA 354
Cdd:cd02000 241 RYRTKEEV-EEWKKRDPILRLRKYLIEAGILTEEELAAIEAEVKAEVEEAVEFA 293
AcoA COG1071
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ...
57-375 3.18e-134

TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and conversion]; TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 440689 [Multi-domain]  Cd Length: 348  Bit Score: 387.57  E-value: 3.18e-134
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679263   57 LTRAEALKYYRTMQVIRRMELKADQLYKQKFIrGFCHLCDGQEACCVGLEAGINPTDHVITSYRAHGFCYTRGLSVKSIL 136
Cdd:COG1071  17 LSKEELLELYRDMLLIRRFEERALALQRQGKI-GFYHLSIGQEAAQVGAAAALRPGDWIFPTYRDHGHALARGVDPKELM 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679263  137 AELTGRKGGCAKGKGGSMHMYGK--NFYGGNGIVGAQVPLGAGVAFACKYLKNGQVCLALYGDGAANQGQVFEAYNMSAL 214
Cdd:COG1071  96 AELFGKATGPSKGRGGSMHFFDKelNFLGGSGIVGGQLPHAVGAALAAKLRGEDEVAVAFFGDGATSEGDFHEALNFAAV 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679263  215 WKLPCVFICENNLYGMGTSNERSAASTDYHKK--GFIIPGLRVNGMDILCVREATKFAADHCRSGKGPIVMELQTYRYHG 292
Cdd:COG1071 176 WKLPVVFVCENNGYAISTPVERQTAVETIADRaaGYGIPGVRVDGNDVLAVYAAVKEAVERARAGEGPTLIEAKTYRLGG 255
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679263  293 HSMSDPGISYRSREEVHNVRSKsDPIMLLRERIISNNLSNIEELKEIDADVKKEVEDAAQFATTDPEPAVEDIANYLYHQ 372
Cdd:COG1071 256 HSTSDDPTRYRTKEEVEEWRER-DPIERLRAYLLEEGLLTEEELEAIEAEAKAEVEEAVEFAEASPEPDPEELFDDVYAE 334

                ...
gi 6679263  373 DPP 375
Cdd:COG1071 335 PPP 337
odpA CHL00149
pyruvate dehydrogenase E1 component alpha subunit; Reviewed
40-370 3.42e-75

pyruvate dehydrogenase E1 component alpha subunit; Reviewed


Pssm-ID: 177069 [Multi-domain]  Cd Length: 341  Bit Score: 237.07  E-value: 3.42e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679263    40 KKCDLyrlEEGPPTSTVLTRAEALKYYRTMQVIRRMELKADQLYKQKFIRGFCHLCDGQEACCVGLEAGINPTDHVITSY 119
Cdd:CHL00149   3 KKVNL---PLTNSNENNINSMWLLVLYEDMLLGRNFEDMCAQMYYRGKMFGFVHLYNGQEAVSTGVIKLLAETDYVCSTY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679263   120 RAHGFCYTRGLSVKSILAELTGRKGGCAKGKGGSMHMYGK--NFYGGNGIVGAQVPLGAGVAFA-------CKYLKNGQV 190
Cdd:CHL00149  80 RDHVHALSKGVPPKNVMAELFGKETGCSRGRGGSMHIFSAphNFLGGFAFIGEGIPIALGAAFQsiyrqqvLKEVQPLRV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679263   191 CLALYGDGAANQGQVFEAYNMSALWKLPCVFICENNLYGMGTSNERSAASTDYHKKG--FIIPGLRVNGMDILCVREATK 268
Cdd:CHL00149 160 TACFFGDGTTNNGQFFECLNMAVLWKLPIIFVVENNQWAIGMAHHRSTSIPEIHKKAeaFGLPGIEVDGMDVLAVREVAK 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679263   269 FAADHCRSGKGPIVMELQTYRYHGHSMSDPGiSYRSREEVHNVRSKsDPIMLLRERIISNNLSNIEELKEIDADVKKEVE 348
Cdd:CHL00149 240 EAVERARQGDGPTLIEALTYRFRGHSLADPD-ELRSKQEKEAWVAR-DPIKKLKSYIIDNELASQKELNKIQREVKIEIE 317
                        330       340
                 ....*....|....*....|..
gi 6679263   349 DAAQFATTDPEPAVEDIANYLY 370
Cdd:CHL00149 318 QAVQFAISSPEPNISDLKKYLF 339
PLN02374 PLN02374
pyruvate dehydrogenase (acetyl-transferring)
47-360 4.97e-75

pyruvate dehydrogenase (acetyl-transferring)


Pssm-ID: 215213 [Multi-domain]  Cd Length: 433  Bit Score: 239.46  E-value: 4.97e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679263    47 LEEGPPTST----VLTRAEALKYYRTMQVIRRMELKADQLYKQKFIRGFCHLCDGQEACCVGLEAGINPTDHVITSYRAH 122
Cdd:PLN02374  69 VKEKNSKASasdlLVTREEGLELYEDMVLGRSFEDMCAQMYYRGKMFGFVHLYNGQEAVSTGFIKLLKKDDSVVSTYRDH 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679263   123 GFCYTRGLSVKSILAELTGRKGGCAKGKGGSMHMYGK--NFYGGNGIVGAQVPLGAGVAFACKY----LKNG---QVCLA 193
Cdd:PLN02374 149 VHALSKGVPARAVMSELFGKATGCCRGQGGSMHMFSKehNLLGGFAFIGEGIPVATGAAFSSKYrrevLKEEscdDVTLA 228
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679263   194 LYGDGAANQGQVFEAYNMSALWKLPCVFICENNLYGMGTSNERSAASTDYHKKG--FIIPGLRVNGMDILCVREATKFAA 271
Cdd:PLN02374 229 FFGDGTCNNGQFFECLNMAALWKLPIVFVVENNLWAIGMSHLRATSDPEIWKKGpaFGMPGVHVDGMDVLKVREVAKEAI 308
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679263   272 DHCRSGKGPIVMELQTYRYHGHSMSDPGISYRSREEVHnvRSKSDPIMLLRERIISNNLSNIEELKEIDADVKKEVEDAA 351
Cdd:PLN02374 309 ERARRGEGPTLVECETYRFRGHSLADPDELRDPAEKAH--YAARDPIAALKKYLIENGLATEAELKAIEKKIDEVVEDAV 386

                 ....*....
gi 6679263   352 QFATTDPEP 360
Cdd:PLN02374 387 EFADASPLP 395
TPP_E1_OGDC_like cd02016
Thiamine pyrophosphate (TPP) family, E1 of OGDC-like subfamily, TPP-binding module; composed ...
190-297 3.32e-09

Thiamine pyrophosphate (TPP) family, E1 of OGDC-like subfamily, TPP-binding module; composed of proteins similar to the E1 component of the 2-oxoglutarate dehydrogenase multienzyme complex (OGDC). OGDC catalyzes the oxidative decarboxylation of 2-oxoglutarate to succinyl-CoA and carbon dioxide, a key reaction of the tricarboxylic acid cycle.


Pssm-ID: 238974 [Multi-domain]  Cd Length: 265  Bit Score: 57.15  E-value: 3.32e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679263  190 VCLALYGDGA-ANQGQVFEAYNMSalwKLP------CVFICENNLYGMGTSNERSAAS---TDYhKKGFIIPGLRVNGMD 259
Cdd:cd02016 142 LPILIHGDAAfAGQGVVYETLNLS---NLPgyttggTIHIVVNNQIGFTTDPRDSRSSpycTDV-AKMIGAPIFHVNGDD 217
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 6679263  260 ILCVREATKFAADHCRSGKGPIVMELQTYRYHGHSMSD 297
Cdd:cd02016 218 PEAVVRATRLALEYRQKFKKDVVIDLVCYRRHGHNELD 255
TPP_TK cd02012
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ...
172-297 4.44e-04

Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK catalyzes the transfer of a two-carbon unit from ketose phosphates to aldose phosphates. In heterotrophic organisms, TK provides a link between glycolysis and the pentose phosphate pathway and provides precursors for nucleotide, aromatic amino acid and vitamin biosynthesis. In addition, the enzyme plays a central role in the Calvin cycle in plants. Typically, TKs are homodimers. They require TPP and divalent cations, such as magnesium ions, for activity.


Pssm-ID: 238970 [Multi-domain]  Cd Length: 255  Bit Score: 41.34  E-value: 4.44e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679263  172 VPLGAGVAFACKYLK-NGQVClALYGDGAANQGQVFEAYNMSALWKLP--CVFICENNLYGMGTSNErSAASTDYHKK-- 246
Cdd:cd02012 111 LSVAVGMALAEKLLGfDYRVY-VLLGDGELQEGSVWEAASFAGHYKLDnlIAIVDSNRIQIDGPTDD-ILFTEDLAKKfe 188
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6679263  247 --GFIIpgLRVNGMDILCVREATKFAADH--------CRS--GKGPIVMElQTYRYHGHSMSD 297
Cdd:cd02012 189 afGWNV--IEVDGHDVEEILAALEEAKKSkgkptliiAKTikGKGVPFME-NTAKWHGKPLGE 248
sucA PRK09404
2-oxoglutarate dehydrogenase E1 component; Reviewed
196-297 5.47e-04

2-oxoglutarate dehydrogenase E1 component; Reviewed


Pssm-ID: 236499 [Multi-domain]  Cd Length: 924  Bit Score: 42.03  E-value: 5.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679263   196 GDGA-ANQGQVFEAYNMSalwKLP------CVFICENNLYGMGTSNERSAaSTDYHK---KGFIIPGLRVNGMDILCVRE 265
Cdd:PRK09404 350 GDAAfAGQGVVAETLNLS---QLRgyrtggTIHIVINNQIGFTTSPPDDR-STPYCTdvaKMVQAPIFHVNGDDPEAVVF 425
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 6679263   266 ATKFAAD-----HCrsgkgPIVMELQTYRYHGHSMSD 297
Cdd:PRK09404 426 ATRLALEyrqkfKK-----DVVIDLVCYRRHGHNEGD 457
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
192-364 7.84e-04

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


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 41.80  E-value: 7.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679263    192 LALYGDGA-ANQGQVFEAYNMSalwKLP------CVFICENNLYGMGTSNERSAAS---TDYhKKGFIIPGLRVNGMDI- 260
Cdd:PRK12270  651 ILLHGDAAfAGQGVVAETLNLS---QLRgyrtggTIHIVVNNQVGFTTAPESSRSSeyaTDV-AKMIQAPIFHVNGDDPe 726
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679263    261 LCVREAtKFAADHCRSGKGPIVMELQTYRYHGH------SMSDPgISYRSREEVHNVRsKSDPIMLLRERIISnnlsnIE 334
Cdd:PRK12270  727 AVVRVA-RLAFEYRQRFHKDVVIDLVCYRRRGHnegddpSMTQP-LMYDLIDAKRSVR-KLYTEALIGRGDIT-----VE 798
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 6679263    335 ELKEIDADVKKEVEDA------AQFATTDPEPAVED 364
Cdd:PRK12270  799 EAEQALRDYQGQLERVfnevreAEKKPPEPPESVES 834
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH