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Conserved domains on  [gi|291084742|ref|NP_001166925|]
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pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial isoform 2 precursor [Homo sapiens]

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

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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 ...
96-408 0e+00

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: 509.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084742   96 REDGLKYYRMMQTVRRMELKADQLYKQKIIRGFCHLCDGQEACCVGLEAGINPTDHLITAYRAHGFTFTRGLSVREILAE 175
Cdd:TIGR03182   1 KEELLELYRDMLLIRRFEEKAGQLYGMGKIGGFCHLYIGQEAVAVGLIAALKPDDYVITSYRDHGHALARGVPPKEVMAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084742  176 LTGRKGGCAKGKGGSMHMYA--KNFYGGNGIVGAQVPLGAGIALACKYNGKDEVCLTLYGDGAANQGQIFEAYNMAALWK 253
Cdd:TIGR03182  81 LTGRETGCSKGKGGSMHMFDreKNFYGGHGIVGAQVPLATGLAFANKYRGNDNVTACFFGDGAANQGQFYESFNMAALWK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084742  254 LPCIFICENNRYGMGTSVERAAASTDYYKRGDF--IPGLRVDGMDILCVREATRFAAAYCRSGKGPILMELQTYRYHGHS 331
Cdd:TIGR03182 161 LPVIFVIENNLYAMGTAVERSSSVTDLYKRGESfgIPGERVDGMDVLAVREAAKEAVERARSGKGPILLEMKTYRFRGHS 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 291084742  332 MSDPGvSYRTREEIQEVRsKSDPIMLLKDRMVNSNLASVEELKEIDVEVRKEIEDAAQFATADPEPPLEELGYHIYS 408
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 ...
96-408 0e+00

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: 509.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084742   96 REDGLKYYRMMQTVRRMELKADQLYKQKIIRGFCHLCDGQEACCVGLEAGINPTDHLITAYRAHGFTFTRGLSVREILAE 175
Cdd:TIGR03182   1 KEELLELYRDMLLIRRFEEKAGQLYGMGKIGGFCHLYIGQEAVAVGLIAALKPDDYVITSYRDHGHALARGVPPKEVMAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084742  176 LTGRKGGCAKGKGGSMHMYA--KNFYGGNGIVGAQVPLGAGIALACKYNGKDEVCLTLYGDGAANQGQIFEAYNMAALWK 253
Cdd:TIGR03182  81 LTGRETGCSKGKGGSMHMFDreKNFYGGHGIVGAQVPLATGLAFANKYRGNDNVTACFFGDGAANQGQFYESFNMAALWK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084742  254 LPCIFICENNRYGMGTSVERAAASTDYYKRGDF--IPGLRVDGMDILCVREATRFAAAYCRSGKGPILMELQTYRYHGHS 331
Cdd:TIGR03182 161 LPVIFVIENNLYAMGTAVERSSSVTDLYKRGESfgIPGERVDGMDVLAVREAAKEAVERARSGKGPILLEMKTYRFRGHS 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 291084742  332 MSDPGvSYRTREEIQEVRsKSDPIMLLKDRMVNSNLASVEELKEIDVEVRKEIEDAAQFATADPEPPLEELGYHIYS 408
Cdd:TIGR03182 241 MSDPA-KYRSKEEVEEWR-KRDPIEKLKARLIEQGIASEEELKEIDKEVRAEVEEAVEFAENSPEPPVEELYTDVYA 315
PLN02269 PLN02269
Pyruvate dehydrogenase E1 component subunit alpha
69-418 1.83e-171

Pyruvate dehydrogenase E1 component subunit alpha


Pssm-ID: 215152 [Multi-domain]  Cd Length: 362  Bit Score: 484.22  E-value: 1.83e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084742  69 ANDATFEIKKC-DLHRLEEgPPVTTVLTREDGLKYYRMMQTVRRMELKADQLYKQKIIRGFCHLCDGQEACCVGLEAGIN 147
Cdd:PLN02269   2 TDPITIETPVPfKGHLCDP-PSRTVETSKQELVDFFRDMYLMRRMEIAADSLYKAKLIRGFCHLYDGQEAVAVGMEAAIT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084742 148 PTDHLITAYRAHGFTFTRGLSVREILAELTGRKGGCAKGKGGSMHMYAK--NFYGGNGIVGAQVPLGAGIALACKYNGKD 225
Cdd:PLN02269  81 KEDAIITAYRDHCTHLGRGGTVLEVFAELMGRKDGCSRGKGGSMHFYKKdaNFYGGHGIVGAQVPLGAGLAFAQKYNKEE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084742 226 EVCLTLYGDGAANQGQIFEAYNMAALWKLPCIFICENNRYGMGTSVERAAASTDYYKRGDFIPGLRVDGMDILCVREATR 305
Cdd:PLN02269 161 NVAFALYGDGAANQGQLFEALNIAALWDLPVIFVCENNHYGMGTAEWRAAKSPAYYKRGDYVPGLKVDGMDVLAVKQACK 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084742 306 FAAAYCRSgKGPILMELQTYRYHGHSMSDPGVSYRTREEIQEVRSKSDPIMLLKDRMVNSNLASVEELKEIDVEVRKEIE 385
Cdd:PLN02269 241 FAKEHALS-NGPIVLEMDTYRYHGHSMSDPGSTYRTRDEISGVRQERDPIERVRKLLLAHELATEAELKDIEKEIRKEVD 319
                        330       340       350
                 ....*....|....*....|....*....|...
gi 291084742 386 DAAQFATADPEPPLEELGYHIYSSDPPFEVRGA 418
Cdd:PLN02269 320 DAVAKAKESPMPDPSELFTNVYVKGLGVESYGA 352
E1_dh pfam00676
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ...
104-400 3.43e-154

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: 438.30  E-value: 3.43e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084742  104 RMMQTVRRMELKADQLYKQKIIRGFCHLCDGQEACCVGLEAGINPTDHLITAYRAHGFTFTRGLSVREILAELTGRKGGC 183
Cdd:pfam00676   1 RRMMTLRRMEDARDALYKRQGIRGFYHLYAGQEAAQVGIAAALEPGDYIIPGYRDHGNLLARGLSLEEIFAELYGRVAKG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084742  184 AKGkggSMHMYAK----NFYGGNGIVGAQVPLGAGIALACKYNGKDEVCLTLYGDGAANQGQIFEAYNMAALWKLPCIFI 259
Cdd:pfam00676  81 KGG---SMHGYYGakgnRFYGGNGILGAQVPLGAGIALAAKYRGKKEVAITLYGDGAANQGDFFEGLNFAALWKLPVIFV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084742  260 CENNRYGMGTSVERAAASTDYYK--RGDFIPGLRVDGMDILCVREATRFAAAYCRSGKGPILMELQTYRYHGHSMSDPGV 337
Cdd:pfam00676 158 CENNQYGISTPAERASASTTYADraRGYGIPGLHVDGMDPLAVYQASKFAAERARTGKGPFLIELVTYRYGGHSMSDDPS 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 291084742  338 SYRTREEIQEVRSKSDPIMLLKDRMVNSNLASVEELKEIDVEVRKEIEDAAQFATADPEPPLE 400
Cdd:pfam00676 238 TYRTRDEYEEVRKKKDPIQRFKEHLVSKGVWSEEELKAIEKEVRKEVEEAFKKAESAPEPHPE 300
TPP_E1_PDC_ADC_BCADC cd02000
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ...
102-391 5.91e-143

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: 409.19  E-value: 5.91e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084742 102 YYRMMQTVRRMELKADQLYKQKIIRGFCHLCDGQEACCVGLEAGINPTDHLITAYRAHGFTFTRGLSVREILAELTGRKG 181
Cdd:cd02000    1 LYRTMVLIRRFDERLLELYRQGKIGGFYHLSIGQEAVAVGVAAALRPGDWVFPTYRDHGHALARGVDLKEMLAELFGKET 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084742 182 GCAKGKGGSMHM--YAKNFYGGNGIVGAQVPLGAGIALACKYNGKDEVCLTLYGDGAANQGQIFEAYNMAALWKLPCIFI 259
Cdd:cd02000   81 GPCKGRGGSMHIgdKEKNFFGGNGIVGGQVPLAAGAALALKYRGEDRVAVCFFGDGATNEGDFHEALNFAALWKLPVIFV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084742 260 CENNRYGMGTSVERAAASTDYYKRGDF--IPGLRVDGMDILCVREATRFAAAYCRSGKGPILMELQTYRYHGHSMSDPGV 337
Cdd:cd02000  161 CENNGYAISTPTSRQTAGTSIADRAAAygIPGIRVDGNDVLAVYEAAKEAVERARAGGGPTLIEAVTYRLGGHSTSDDPS 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 291084742 338 SYRTREEIQEvRSKSDPIMLLKDRMVNSNLASVEELKEIDVEVRKEIEDAAQFA 391
Cdd:cd02000  241 RYRTKEEVEE-WKKRDPILRLRKYLIEAGILTEEELAAIEAEVKAEVEEAVEFA 293
AcoA COG1071
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ...
94-412 1.90e-137

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: 397.59  E-value: 1.90e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084742  94 LTREDGLKYYRMMQTVRRMELKADQLYKQKIIrGFCHLCDGQEACCVGLEAGINPTDHLITAYRAHGFTFTRGLSVREIL 173
Cdd:COG1071   17 LSKEELLELYRDMLLIRRFEERALALQRQGKI-GFYHLSIGQEAAQVGAAAALRPGDWIFPTYRDHGHALARGVDPKELM 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084742 174 AELTGRKGGCAKGKGGSMHMY--AKNFYGGNGIVGAQVPLGAGIALACKYNGKDEVCLTLYGDGAANQGQIFEAYNMAAL 251
Cdd:COG1071   96 AELFGKATGPSKGRGGSMHFFdkELNFLGGSGIVGGQLPHAVGAALAAKLRGEDEVAVAFFGDGATSEGDFHEALNFAAV 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084742 252 WKLPCIFICENNRYGMGTSVERAAASTDYYKRGD-F-IPGLRVDGMDILCVREATRFAAAYCRSGKGPILMELQTYRYHG 329
Cdd:COG1071  176 WKLPVVFVCENNGYAISTPVERQTAVETIADRAAgYgIPGVRVDGNDVLAVYAAVKEAVERARAGEGPTLIEAKTYRLGG 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084742 330 HSMSDPGVSYRTREEIQEVRSKsDPIMLLKDRMVNSNLASVEELKEIDVEVRKEIEDAAQFATADPEPPLEELGYHIYSS 409
Cdd:COG1071  256 HSTSDDPTRYRTKEEVEEWRER-DPIERLRAYLLEEGLLTEEELEAIEAEAKAEVEEAVEFAEASPEPDPEELFDDVYAE 334

                 ...
gi 291084742 410 DPP 412
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 ...
96-408 0e+00

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: 509.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084742   96 REDGLKYYRMMQTVRRMELKADQLYKQKIIRGFCHLCDGQEACCVGLEAGINPTDHLITAYRAHGFTFTRGLSVREILAE 175
Cdd:TIGR03182   1 KEELLELYRDMLLIRRFEEKAGQLYGMGKIGGFCHLYIGQEAVAVGLIAALKPDDYVITSYRDHGHALARGVPPKEVMAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084742  176 LTGRKGGCAKGKGGSMHMYA--KNFYGGNGIVGAQVPLGAGIALACKYNGKDEVCLTLYGDGAANQGQIFEAYNMAALWK 253
Cdd:TIGR03182  81 LTGRETGCSKGKGGSMHMFDreKNFYGGHGIVGAQVPLATGLAFANKYRGNDNVTACFFGDGAANQGQFYESFNMAALWK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084742  254 LPCIFICENNRYGMGTSVERAAASTDYYKRGDF--IPGLRVDGMDILCVREATRFAAAYCRSGKGPILMELQTYRYHGHS 331
Cdd:TIGR03182 161 LPVIFVIENNLYAMGTAVERSSSVTDLYKRGESfgIPGERVDGMDVLAVREAAKEAVERARSGKGPILLEMKTYRFRGHS 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 291084742  332 MSDPGvSYRTREEIQEVRsKSDPIMLLKDRMVNSNLASVEELKEIDVEVRKEIEDAAQFATADPEPPLEELGYHIYS 408
Cdd:TIGR03182 241 MSDPA-KYRSKEEVEEWR-KRDPIEKLKARLIEQGIASEEELKEIDKEVRAEVEEAVEFAENSPEPPVEELYTDVYA 315
PLN02269 PLN02269
Pyruvate dehydrogenase E1 component subunit alpha
69-418 1.83e-171

Pyruvate dehydrogenase E1 component subunit alpha


Pssm-ID: 215152 [Multi-domain]  Cd Length: 362  Bit Score: 484.22  E-value: 1.83e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084742  69 ANDATFEIKKC-DLHRLEEgPPVTTVLTREDGLKYYRMMQTVRRMELKADQLYKQKIIRGFCHLCDGQEACCVGLEAGIN 147
Cdd:PLN02269   2 TDPITIETPVPfKGHLCDP-PSRTVETSKQELVDFFRDMYLMRRMEIAADSLYKAKLIRGFCHLYDGQEAVAVGMEAAIT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084742 148 PTDHLITAYRAHGFTFTRGLSVREILAELTGRKGGCAKGKGGSMHMYAK--NFYGGNGIVGAQVPLGAGIALACKYNGKD 225
Cdd:PLN02269  81 KEDAIITAYRDHCTHLGRGGTVLEVFAELMGRKDGCSRGKGGSMHFYKKdaNFYGGHGIVGAQVPLGAGLAFAQKYNKEE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084742 226 EVCLTLYGDGAANQGQIFEAYNMAALWKLPCIFICENNRYGMGTSVERAAASTDYYKRGDFIPGLRVDGMDILCVREATR 305
Cdd:PLN02269 161 NVAFALYGDGAANQGQLFEALNIAALWDLPVIFVCENNHYGMGTAEWRAAKSPAYYKRGDYVPGLKVDGMDVLAVKQACK 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084742 306 FAAAYCRSgKGPILMELQTYRYHGHSMSDPGVSYRTREEIQEVRSKSDPIMLLKDRMVNSNLASVEELKEIDVEVRKEIE 385
Cdd:PLN02269 241 FAKEHALS-NGPIVLEMDTYRYHGHSMSDPGSTYRTRDEISGVRQERDPIERVRKLLLAHELATEAELKDIEKEIRKEVD 319
                        330       340       350
                 ....*....|....*....|....*....|...
gi 291084742 386 DAAQFATADPEPPLEELGYHIYSSDPPFEVRGA 418
Cdd:PLN02269 320 DAVAKAKESPMPDPSELFTNVYVKGLGVESYGA 352
E1_dh pfam00676
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ...
104-400 3.43e-154

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: 438.30  E-value: 3.43e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084742  104 RMMQTVRRMELKADQLYKQKIIRGFCHLCDGQEACCVGLEAGINPTDHLITAYRAHGFTFTRGLSVREILAELTGRKGGC 183
Cdd:pfam00676   1 RRMMTLRRMEDARDALYKRQGIRGFYHLYAGQEAAQVGIAAALEPGDYIIPGYRDHGNLLARGLSLEEIFAELYGRVAKG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084742  184 AKGkggSMHMYAK----NFYGGNGIVGAQVPLGAGIALACKYNGKDEVCLTLYGDGAANQGQIFEAYNMAALWKLPCIFI 259
Cdd:pfam00676  81 KGG---SMHGYYGakgnRFYGGNGILGAQVPLGAGIALAAKYRGKKEVAITLYGDGAANQGDFFEGLNFAALWKLPVIFV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084742  260 CENNRYGMGTSVERAAASTDYYK--RGDFIPGLRVDGMDILCVREATRFAAAYCRSGKGPILMELQTYRYHGHSMSDPGV 337
Cdd:pfam00676 158 CENNQYGISTPAERASASTTYADraRGYGIPGLHVDGMDPLAVYQASKFAAERARTGKGPFLIELVTYRYGGHSMSDDPS 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 291084742  338 SYRTREEIQEVRSKSDPIMLLKDRMVNSNLASVEELKEIDVEVRKEIEDAAQFATADPEPPLE 400
Cdd:pfam00676 238 TYRTRDEYEEVRKKKDPIQRFKEHLVSKGVWSEEELKAIEKEVRKEVEEAFKKAESAPEPHPE 300
TPP_E1_PDC_ADC_BCADC cd02000
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ...
102-391 5.91e-143

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: 409.19  E-value: 5.91e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084742 102 YYRMMQTVRRMELKADQLYKQKIIRGFCHLCDGQEACCVGLEAGINPTDHLITAYRAHGFTFTRGLSVREILAELTGRKG 181
Cdd:cd02000    1 LYRTMVLIRRFDERLLELYRQGKIGGFYHLSIGQEAVAVGVAAALRPGDWVFPTYRDHGHALARGVDLKEMLAELFGKET 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084742 182 GCAKGKGGSMHM--YAKNFYGGNGIVGAQVPLGAGIALACKYNGKDEVCLTLYGDGAANQGQIFEAYNMAALWKLPCIFI 259
Cdd:cd02000   81 GPCKGRGGSMHIgdKEKNFFGGNGIVGGQVPLAAGAALALKYRGEDRVAVCFFGDGATNEGDFHEALNFAALWKLPVIFV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084742 260 CENNRYGMGTSVERAAASTDYYKRGDF--IPGLRVDGMDILCVREATRFAAAYCRSGKGPILMELQTYRYHGHSMSDPGV 337
Cdd:cd02000  161 CENNGYAISTPTSRQTAGTSIADRAAAygIPGIRVDGNDVLAVYEAAKEAVERARAGGGPTLIEAVTYRLGGHSTSDDPS 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 291084742 338 SYRTREEIQEvRSKSDPIMLLKDRMVNSNLASVEELKEIDVEVRKEIEDAAQFA 391
Cdd:cd02000  241 RYRTKEEVEE-WKKRDPILRLRKYLIEAGILTEEELAAIEAEVKAEVEEAVEFA 293
AcoA COG1071
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ...
94-412 1.90e-137

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: 397.59  E-value: 1.90e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084742  94 LTREDGLKYYRMMQTVRRMELKADQLYKQKIIrGFCHLCDGQEACCVGLEAGINPTDHLITAYRAHGFTFTRGLSVREIL 173
Cdd:COG1071   17 LSKEELLELYRDMLLIRRFEERALALQRQGKI-GFYHLSIGQEAAQVGAAAALRPGDWIFPTYRDHGHALARGVDPKELM 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084742 174 AELTGRKGGCAKGKGGSMHMY--AKNFYGGNGIVGAQVPLGAGIALACKYNGKDEVCLTLYGDGAANQGQIFEAYNMAAL 251
Cdd:COG1071   96 AELFGKATGPSKGRGGSMHFFdkELNFLGGSGIVGGQLPHAVGAALAAKLRGEDEVAVAFFGDGATSEGDFHEALNFAAV 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084742 252 WKLPCIFICENNRYGMGTSVERAAASTDYYKRGD-F-IPGLRVDGMDILCVREATRFAAAYCRSGKGPILMELQTYRYHG 329
Cdd:COG1071  176 WKLPVVFVCENNGYAISTPVERQTAVETIADRAAgYgIPGVRVDGNDVLAVYAAVKEAVERARAGEGPTLIEAKTYRLGG 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084742 330 HSMSDPGVSYRTREEIQEVRSKsDPIMLLKDRMVNSNLASVEELKEIDVEVRKEIEDAAQFATADPEPPLEELGYHIYSS 409
Cdd:COG1071  256 HSTSDDPTRYRTKEEVEEWRER-DPIERLRAYLLEEGLLTEEELEAIEAEAKAEVEEAVEFAEASPEPDPEELFDDVYAE 334

                 ...
gi 291084742 410 DPP 412
Cdd:COG1071  335 PPP 337
PLN02374 PLN02374
pyruvate dehydrogenase (acetyl-transferring)
93-411 4.17e-75

pyruvate dehydrogenase (acetyl-transferring)


Pssm-ID: 215213 [Multi-domain]  Cd Length: 433  Bit Score: 241.00  E-value: 4.17e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084742  93 VLTREDGLKYYRMMQTVRRMELKADQLYKQKIIRGFCHLCDGQEACCVGLEAGINPTDHLITAYRAHGFTFTRGLSVREI 172
Cdd:PLN02374  82 LVTREEGLELYEDMVLGRSFEDMCAQMYYRGKMFGFVHLYNGQEAVSTGFIKLLKKDDSVVSTYRDHVHALSKGVPARAV 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084742 173 LAELTGRKGGCAKGKGGSMHMYAK--NFYGGNGIVGAQVPLGAGIALACKY-------NGKDEVCLTLYGDGAANQGQIF 243
Cdd:PLN02374 162 MSELFGKATGCCRGQGGSMHMFSKehNLLGGFAFIGEGIPVATGAAFSSKYrrevlkeESCDDVTLAFFGDGTCNNGQFF 241
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084742 244 EAYNMAALWKLPCIFICENNRYGMGTSVERAAASTDYYKRGDF--IPGLRVDGMDILCVREATRFAAAYCRSGKGPILME 321
Cdd:PLN02374 242 ECLNMAALWKLPIVFVVENNLWAIGMSHLRATSDPEIWKKGPAfgMPGVHVDGMDVLKVREVAKEAIERARRGEGPTLVE 321
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084742 322 LQTYRYHGHSMSDPgvsyrtrEEIQEVRSKS-----DPIMLLKDRMVNSNLASVEELKEIDVEVRKEIEDAAQFATADPE 396
Cdd:PLN02374 322 CETYRFRGHSLADP-------DELRDPAEKAhyaarDPIAALKKYLIENGLATEAELKAIEKKIDEVVEDAVEFADASPL 394
                        330
                 ....*....|....*
gi 291084742 397 PPLEELGYHIYsSDP 411
Cdd:PLN02374 395 PPRSQLLENVF-ADP 408
odpA CHL00149
pyruvate dehydrogenase E1 component alpha subunit; Reviewed
94-409 1.23e-70

pyruvate dehydrogenase E1 component alpha subunit; Reviewed


Pssm-ID: 177069 [Multi-domain]  Cd Length: 341  Bit Score: 226.29  E-value: 1.23e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084742  94 LTREDGLKYYRMMQTVRRMELKADQLYKQKIIRGFCHLCDGQEACCVGLEAGINPTDHLITAYRAHGFTFTRGLSVREIL 173
Cdd:CHL00149  17 INSMWLLVLYEDMLLGRNFEDMCAQMYYRGKMFGFVHLYNGQEAVSTGVIKLLAETDYVCSTYRDHVHALSKGVPPKNVM 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084742 174 AELTGRKGGCAKGKGGSMHMY--AKNFYGGNGIVGAQVPLGAGIALA-------CKYNGKDEVCLTLYGDGAANQGQIFE 244
Cdd:CHL00149  97 AELFGKETGCSRGRGGSMHIFsaPHNFLGGFAFIGEGIPIALGAAFQsiyrqqvLKEVQPLRVTACFFGDGTTNNGQFFE 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084742 245 AYNMAALWKLPCIFICENNRYGMGTSVERAAASTDYYKRGDF--IPGLRVDGMDILCVREATRFAAAYCRSGKGPILMEL 322
Cdd:CHL00149 177 CLNMAVLWKLPIIFVVENNQWAIGMAHHRSTSIPEIHKKAEAfgLPGIEVDGMDVLAVREVAKEAVERARQGDGPTLIEA 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084742 323 QTYRYHGHSMSDPGvSYRTREEiQEVRSKSDPIMLLKDRMVNSNLASVEELKEIDVEVRKEIEDAAQFATADPEPPLEEL 402
Cdd:CHL00149 257 LTYRFRGHSLADPD-ELRSKQE-KEAWVARDPIKKLKSYIIDNELASQKELNKIQREVKIEIEQAVQFAISSPEPNISDL 334

                 ....*..
gi 291084742 403 GYHIYSS 409
Cdd:CHL00149 335 KKYLFAD 341
TPP_TK cd02012
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ...
209-334 1.27e-06

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: 49.42  E-value: 1.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084742 209 VPLGAGIALACKYNGKDEVCLTLYGDGAANQGQIFEAYNMAALWKL-PCIFICENNRYGMGTSVERAAASTDYYKR---- 283
Cdd:cd02012  111 LSVAVGMALAEKLLGFDYRVYVLLGDGELQEGSVWEAASFAGHYKLdNLIAIVDSNRIQIDGPTDDILFTEDLAKKfeaf 190
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 291084742 284 GDFIpgLRVDGMDILCVREAtrFAAAY----------CRS--GKGPILMElQTYRYHGHSMSD 334
Cdd:cd02012  191 GWNV--IEVDGHDVEEILAA--LEEAKkskgkptliiAKTikGKGVPFME-NTAKWHGKPLGE 248
TPP_E1_OGDC_like cd02016
Thiamine pyrophosphate (TPP) family, E1 of OGDC-like subfamily, TPP-binding module; composed ...
210-334 1.73e-06

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: 49.06  E-value: 1.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084742 210 PLGAGIALACKYNGKDE-----VCLTLYGDGA-ANQGQIFEAYNMaalWKLP------CIFICENNRYGMGTSVERAAAS 277
Cdd:cd02016  120 PVVMGKTRAKQDYRGDGerdkvLPILIHGDAAfAGQGVVYETLNL---SNLPgyttggTIHIVVNNQIGFTTDPRDSRSS 196
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084742 278 ---TDYYKRGDfIPGLRVDGMDILCVREATRFAAAYCRSGKGPILMELQTYRYHGHSMSD 334
Cdd:cd02016  197 pycTDVAKMIG-APIFHVNGDDPEAVVRATRLALEYRQKFKKDVVIDLVCYRRHGHNELD 255
TPP_BFDC cd02002
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ...
198-324 5.27e-04

Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins similar to Pseudomonas putida benzoylformate decarboxylase (BFDC). P. putida BFDC plays a role in the mandelate pathway, catalyzing the conversion of benzoylformate to benzaldehyde and carbon dioxide. This enzyme is dependent on TPP and a divalent metal cation as cofactors.


Pssm-ID: 238960 [Multi-domain]  Cd Length: 178  Bit Score: 40.66  E-value: 5.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084742 198 FYGGNGIvGAQVPLGAGIALACKynGKDEVCLTlyGDGAANqgqifeaYNMAALW-----KLPCIFICENNR-YG-MGTS 270
Cdd:cd02002   45 TLRGGGL-GWGLPAAVGAALANP--DRKVVAII--GDGSFM-------YTIQALWtaaryGLPVTVVILNNRgYGaLRSF 112
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 291084742 271 VER----AAASTDYYKRGDFIPGLRVD------GMDILCVREATRFAAAYCR--SGKGPILMELQT 324
Cdd:cd02002  113 LKRvgpeGPGENAPDGLDLLDPGIDFAaiakafGVEAERVETPEELDEALREalAEGGPALIEVVV 178
PRK07092 PRK07092
benzoylformate decarboxylase; Reviewed
198-324 9.40e-04

benzoylformate decarboxylase; Reviewed


Pssm-ID: 235931 [Multi-domain]  Cd Length: 530  Bit Score: 41.48  E-value: 9.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084742 198 FYGGNGIVGAQVPLGAGIALACKynGKDEVCLTlyGDGAANqgqifeaYNMAALW-----KLPCIFICENNRygmgtsve 272
Cdd:PRK07092 402 YTMASGGLGYGLPAAVGVALAQP--GRRVIGLI--GDGSAM-------YSIQALWsaaqlKLPVTFVILNNG-------- 462
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 291084742 273 RAAASTDYYKRGDF--IPGLRVDGMDIL-------C----VREATRFAAAYCR--SGKGPILMELQT 324
Cdd:PRK07092 463 RYGALRWFAPVFGVrdVPGLDLPGLDFValargygCeavrVSDAAELADALARalAADGPVLVEVEV 529
 
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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