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Conserved domains on  [gi|528478848|ref|XP_005165191|]
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pyruvate dehydrogenase E1 alpha 1 isoform X1 [Danio rerio]

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 ...
68-379 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: 540.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478848   68 REEGLQYYRTMQTMRRMELKADQLYKQKIIRGFCHLYDGQEACAVGIEAGINLSDHLITAYRAHGYTLTRGGTVREIMAE 147
Cdd:TIGR03182   1 KEELLELYRDMLLIRRFEEKAGQLYGMGKIGGFCHLYIGQEAVAVGLIAALKPDDYVITSYRDHGHALARGVPPKEVMAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478848  148 LTGRRGGIAKGKGGSMHMYT--KHFYGGNGIVGAQVPLGAGVALACKYQGKNELCVCLYGDGAANQGQIFETYNMASLWK 225
Cdd:TIGR03182  81 LTGRETGCSKGKGGSMHMFDreKNFYGGHGIVGAQVPLATGLAFANKYRGNDNVTACFFGDGAANQGQFYESFNMAALWK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478848  226 LPCIFICENNKYGMGTSVERAAASTDYYKRGDF--IPGLRVDGMDVLCVREATKFAAEHCRSGKGPILMELQTYRYHGHS 303
Cdd:TIGR03182 161 LPVIFVIENNLYAMGTAVERSSSVTDLYKRGESfgIPGERVDGMDVLAVREAAKEAVERARSGKGPILLEMKTYRFRGHS 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528478848  304 MSDPGvSYRTREEIQEVRsKSDPISLLKDRMLSNNMASVEELKEIDVEVRKEIEDAAQFATTDPEPPLEDLCNHIF 379
Cdd:TIGR03182 241 MSDPA-KYRSKEEVEEWR-KRDPIEKLKARLIEQGIASEEELKEIDKEVRAEVEEAVEFAENSPEPPVEELYTDVY 314
 
Name Accession Description Interval E-value
PDH_E1_alph_y TIGR03182
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the ...
68-379 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: 540.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478848   68 REEGLQYYRTMQTMRRMELKADQLYKQKIIRGFCHLYDGQEACAVGIEAGINLSDHLITAYRAHGYTLTRGGTVREIMAE 147
Cdd:TIGR03182   1 KEELLELYRDMLLIRRFEEKAGQLYGMGKIGGFCHLYIGQEAVAVGLIAALKPDDYVITSYRDHGHALARGVPPKEVMAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478848  148 LTGRRGGIAKGKGGSMHMYT--KHFYGGNGIVGAQVPLGAGVALACKYQGKNELCVCLYGDGAANQGQIFETYNMASLWK 225
Cdd:TIGR03182  81 LTGRETGCSKGKGGSMHMFDreKNFYGGHGIVGAQVPLATGLAFANKYRGNDNVTACFFGDGAANQGQFYESFNMAALWK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478848  226 LPCIFICENNKYGMGTSVERAAASTDYYKRGDF--IPGLRVDGMDVLCVREATKFAAEHCRSGKGPILMELQTYRYHGHS 303
Cdd:TIGR03182 161 LPVIFVIENNLYAMGTAVERSSSVTDLYKRGESfgIPGERVDGMDVLAVREAAKEAVERARSGKGPILLEMKTYRFRGHS 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528478848  304 MSDPGvSYRTREEIQEVRsKSDPISLLKDRMLSNNMASVEELKEIDVEVRKEIEDAAQFATTDPEPPLEDLCNHIF 379
Cdd:TIGR03182 241 MSDPA-KYRSKEEVEEWR-KRDPIEKLKARLIEQGIASEEELKEIDKEVRAEVEEAVEFAENSPEPPVEELYTDVY 314
PLN02269 PLN02269
Pyruvate dehydrogenase E1 component subunit alpha
41-392 0e+00

Pyruvate dehydrogenase E1 component subunit alpha


Pssm-ID: 215152 [Multi-domain]  Cd Length: 362  Bit Score: 516.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478848  41 TPQATFDIKKC-DVHKLEEgPAVQAVLTREEGLQYYRTMQTMRRMELKADQLYKQKIIRGFCHLYDGQEACAVGIEAGIN 119
Cdd:PLN02269   2 TDPITIETPVPfKGHLCDP-PSRTVETSKQELVDFFRDMYLMRRMEIAADSLYKAKLIRGFCHLYDGQEAVAVGMEAAIT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478848 120 LSDHLITAYRAHGYTLTRGGTVREIMAELTGRRGGIAKGKGGSMHMYTK--HFYGGNGIVGAQVPLGAGVALACKYQGKN 197
Cdd:PLN02269  81 KEDAIITAYRDHCTHLGRGGTVLEVFAELMGRKDGCSRGKGGSMHFYKKdaNFYGGHGIVGAQVPLGAGLAFAQKYNKEE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478848 198 ELCVCLYGDGAANQGQIFETYNMASLWKLPCIFICENNKYGMGTSVERAAASTDYYKRGDFIPGLRVDGMDVLCVREATK 277
Cdd:PLN02269 161 NVAFALYGDGAANQGQLFEALNIAALWDLPVIFVCENNHYGMGTAEWRAAKSPAYYKRGDYVPGLKVDGMDVLAVKQACK 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478848 278 FAAEHCRSgKGPILMELQTYRYHGHSMSDPGVSYRTREEIQEVRSKSDPISLLKDRMLSNNMASVEELKEIDVEVRKEIE 357
Cdd:PLN02269 241 FAKEHALS-NGPIVLEMDTYRYHGHSMSDPGSTYRTRDEISGVRQERDPIERVRKLLLAHELATEAELKDIEKEIRKEVD 319
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 528478848 358 DAAQFATTDPEPPLEDLCNHIFYNDPPLEVRGTNP 392
Cdd:PLN02269 320 DAVAKAKESPMPDPSELFTNVYVKGLGVESYGADR 354
E1_dh pfam00676
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ...
76-372 3.61e-155

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: 439.45  E-value: 3.61e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478848   76 RTMQTMRRMELKADQLYKQKIIRGFCHLYDGQEACAVGIEAGINLSDHLITAYRAHGYTLTRGGTVREIMAELTGRRGgi 155
Cdd:pfam00676   1 RRMMTLRRMEDARDALYKRQGIRGFYHLYAGQEAAQVGIAAALEPGDYIIPGYRDHGNLLARGLSLEEIFAELYGRVA-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478848  156 aKGKGGSMHMYTK----HFYGGNGIVGAQVPLGAGVALACKYQGKNELCVCLYGDGAANQGQIFETYNMASLWKLPCIFI 231
Cdd:pfam00676  79 -KGKGGSMHGYYGakgnRFYGGNGILGAQVPLGAGIALAAKYRGKKEVAITLYGDGAANQGDFFEGLNFAALWKLPVIFV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478848  232 CENNKYGMGTSVERAAASTDYYK--RGDFIPGLRVDGMDVLCVREATKFAAEHCRSGKGPILMELQTYRYHGHSMSDPGV 309
Cdd:pfam00676 158 CENNQYGISTPAERASASTTYADraRGYGIPGLHVDGMDPLAVYQASKFAAERARTGKGPFLIELVTYRYGGHSMSDDPS 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528478848  310 SYRTREEIQEVRSKSDPISLLKDRMLSNNMASVEELKEIDVEVRKEIEDAAQFATTDPEPPLE 372
Cdd:pfam00676 238 TYRTRDEYEEVRKKKDPIQRFKEHLVSKGVWSEEELKAIEKEVRKEVEEAFKKAESAPEPHPE 300
TPP_E1_PDC_ADC_BCADC cd02000
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ...
74-363 1.32e-152

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: 432.69  E-value: 1.32e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478848  74 YYRTMQTMRRMELKADQLYKQKIIRGFCHLYDGQEACAVGIEAGINLSDHLITAYRAHGYTLTRGGTVREIMAELTGRRG 153
Cdd:cd02000    1 LYRTMVLIRRFDERLLELYRQGKIGGFYHLSIGQEAVAVGVAAALRPGDWVFPTYRDHGHALARGVDLKEMLAELFGKET 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478848 154 GIAKGKGGSMHM--YTKHFYGGNGIVGAQVPLGAGVALACKYQGKNELCVCLYGDGAANQGQIFETYNMASLWKLPCIFI 231
Cdd:cd02000   81 GPCKGRGGSMHIgdKEKNFFGGNGIVGGQVPLAAGAALALKYRGEDRVAVCFFGDGATNEGDFHEALNFAALWKLPVIFV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478848 232 CENNKYGMGTSVERAAASTDYYKRGDF--IPGLRVDGMDVLCVREATKFAAEHCRSGKGPILMELQTYRYHGHSMSDPGV 309
Cdd:cd02000  161 CENNGYAISTPTSRQTAGTSIADRAAAygIPGIRVDGNDVLAVYEAAKEAVERARAGGGPTLIEAVTYRLGGHSTSDDPS 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 528478848 310 SYRTREEIQEvRSKSDPISLLKDRMLSNNMASVEELKEIDVEVRKEIEDAAQFA 363
Cdd:cd02000  241 RYRTKEEVEE-WKKRDPILRLRKYLIEAGILTEEELAAIEAEVKAEVEEAVEFA 293
AcoA COG1071
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ...
57-384 1.02e-148

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: 424.94  E-value: 1.02e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478848  57 EEGPAVQAVLTREEGLQYYRTMQTMRRMELKADQLYKQKIIrGFCHLYDGQEACAVGIEAGINLSDHLITAYRAHGYTLT 136
Cdd:COG1071    8 DGTEAALPDLSKEELLELYRDMLLIRRFEERALALQRQGKI-GFYHLSIGQEAAQVGAAAALRPGDWIFPTYRDHGHALA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478848 137 RGGTVREIMAELTGRRGGIAKGKGGSMHMYTK--HFYGGNGIVGAQVPLGAGVALACKYQGKNELCVCLYGDGAANQGQI 214
Cdd:COG1071   87 RGVDPKELMAELFGKATGPSKGRGGSMHFFDKelNFLGGSGIVGGQLPHAVGAALAAKLRGEDEVAVAFFGDGATSEGDF 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478848 215 FETYNMASLWKLPCIFICENNKYGMGTSVERAAASTDYYKRGD-F-IPGLRVDGMDVLCVREATKFAAEHCRSGKGPILM 292
Cdd:COG1071  167 HEALNFAAVWKLPVVFVCENNGYAISTPVERQTAVETIADRAAgYgIPGVRVDGNDVLAVYAAVKEAVERARAGEGPTLI 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478848 293 ELQTYRYHGHSMSDPGVSYRTREEIQEVRSKsDPISLLKDRMLSNNMASVEELKEIDVEVRKEIEDAAQFATTDPEPPLE 372
Cdd:COG1071  247 EAKTYRLGGHSTSDDPTRYRTKEEVEEWRER-DPIERLRAYLLEEGLLTEEELEAIEAEAKAEVEEAVEFAEASPEPDPE 325
                        330
                 ....*....|..
gi 528478848 373 DLCNHIFYNDPP 384
Cdd:COG1071  326 ELFDDVYAEPPP 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 ...
68-379 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: 540.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478848   68 REEGLQYYRTMQTMRRMELKADQLYKQKIIRGFCHLYDGQEACAVGIEAGINLSDHLITAYRAHGYTLTRGGTVREIMAE 147
Cdd:TIGR03182   1 KEELLELYRDMLLIRRFEEKAGQLYGMGKIGGFCHLYIGQEAVAVGLIAALKPDDYVITSYRDHGHALARGVPPKEVMAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478848  148 LTGRRGGIAKGKGGSMHMYT--KHFYGGNGIVGAQVPLGAGVALACKYQGKNELCVCLYGDGAANQGQIFETYNMASLWK 225
Cdd:TIGR03182  81 LTGRETGCSKGKGGSMHMFDreKNFYGGHGIVGAQVPLATGLAFANKYRGNDNVTACFFGDGAANQGQFYESFNMAALWK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478848  226 LPCIFICENNKYGMGTSVERAAASTDYYKRGDF--IPGLRVDGMDVLCVREATKFAAEHCRSGKGPILMELQTYRYHGHS 303
Cdd:TIGR03182 161 LPVIFVIENNLYAMGTAVERSSSVTDLYKRGESfgIPGERVDGMDVLAVREAAKEAVERARSGKGPILLEMKTYRFRGHS 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528478848  304 MSDPGvSYRTREEIQEVRsKSDPISLLKDRMLSNNMASVEELKEIDVEVRKEIEDAAQFATTDPEPPLEDLCNHIF 379
Cdd:TIGR03182 241 MSDPA-KYRSKEEVEEWR-KRDPIEKLKARLIEQGIASEEELKEIDKEVRAEVEEAVEFAENSPEPPVEELYTDVY 314
PLN02269 PLN02269
Pyruvate dehydrogenase E1 component subunit alpha
41-392 0e+00

Pyruvate dehydrogenase E1 component subunit alpha


Pssm-ID: 215152 [Multi-domain]  Cd Length: 362  Bit Score: 516.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478848  41 TPQATFDIKKC-DVHKLEEgPAVQAVLTREEGLQYYRTMQTMRRMELKADQLYKQKIIRGFCHLYDGQEACAVGIEAGIN 119
Cdd:PLN02269   2 TDPITIETPVPfKGHLCDP-PSRTVETSKQELVDFFRDMYLMRRMEIAADSLYKAKLIRGFCHLYDGQEAVAVGMEAAIT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478848 120 LSDHLITAYRAHGYTLTRGGTVREIMAELTGRRGGIAKGKGGSMHMYTK--HFYGGNGIVGAQVPLGAGVALACKYQGKN 197
Cdd:PLN02269  81 KEDAIITAYRDHCTHLGRGGTVLEVFAELMGRKDGCSRGKGGSMHFYKKdaNFYGGHGIVGAQVPLGAGLAFAQKYNKEE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478848 198 ELCVCLYGDGAANQGQIFETYNMASLWKLPCIFICENNKYGMGTSVERAAASTDYYKRGDFIPGLRVDGMDVLCVREATK 277
Cdd:PLN02269 161 NVAFALYGDGAANQGQLFEALNIAALWDLPVIFVCENNHYGMGTAEWRAAKSPAYYKRGDYVPGLKVDGMDVLAVKQACK 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478848 278 FAAEHCRSgKGPILMELQTYRYHGHSMSDPGVSYRTREEIQEVRSKSDPISLLKDRMLSNNMASVEELKEIDVEVRKEIE 357
Cdd:PLN02269 241 FAKEHALS-NGPIVLEMDTYRYHGHSMSDPGSTYRTRDEISGVRQERDPIERVRKLLLAHELATEAELKDIEKEIRKEVD 319
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 528478848 358 DAAQFATTDPEPPLEDLCNHIFYNDPPLEVRGTNP 392
Cdd:PLN02269 320 DAVAKAKESPMPDPSELFTNVYVKGLGVESYGADR 354
E1_dh pfam00676
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ...
76-372 3.61e-155

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: 439.45  E-value: 3.61e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478848   76 RTMQTMRRMELKADQLYKQKIIRGFCHLYDGQEACAVGIEAGINLSDHLITAYRAHGYTLTRGGTVREIMAELTGRRGgi 155
Cdd:pfam00676   1 RRMMTLRRMEDARDALYKRQGIRGFYHLYAGQEAAQVGIAAALEPGDYIIPGYRDHGNLLARGLSLEEIFAELYGRVA-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478848  156 aKGKGGSMHMYTK----HFYGGNGIVGAQVPLGAGVALACKYQGKNELCVCLYGDGAANQGQIFETYNMASLWKLPCIFI 231
Cdd:pfam00676  79 -KGKGGSMHGYYGakgnRFYGGNGILGAQVPLGAGIALAAKYRGKKEVAITLYGDGAANQGDFFEGLNFAALWKLPVIFV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478848  232 CENNKYGMGTSVERAAASTDYYK--RGDFIPGLRVDGMDVLCVREATKFAAEHCRSGKGPILMELQTYRYHGHSMSDPGV 309
Cdd:pfam00676 158 CENNQYGISTPAERASASTTYADraRGYGIPGLHVDGMDPLAVYQASKFAAERARTGKGPFLIELVTYRYGGHSMSDDPS 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528478848  310 SYRTREEIQEVRSKSDPISLLKDRMLSNNMASVEELKEIDVEVRKEIEDAAQFATTDPEPPLE 372
Cdd:pfam00676 238 TYRTRDEYEEVRKKKDPIQRFKEHLVSKGVWSEEELKAIEKEVRKEVEEAFKKAESAPEPHPE 300
TPP_E1_PDC_ADC_BCADC cd02000
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ...
74-363 1.32e-152

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: 432.69  E-value: 1.32e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478848  74 YYRTMQTMRRMELKADQLYKQKIIRGFCHLYDGQEACAVGIEAGINLSDHLITAYRAHGYTLTRGGTVREIMAELTGRRG 153
Cdd:cd02000    1 LYRTMVLIRRFDERLLELYRQGKIGGFYHLSIGQEAVAVGVAAALRPGDWVFPTYRDHGHALARGVDLKEMLAELFGKET 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478848 154 GIAKGKGGSMHM--YTKHFYGGNGIVGAQVPLGAGVALACKYQGKNELCVCLYGDGAANQGQIFETYNMASLWKLPCIFI 231
Cdd:cd02000   81 GPCKGRGGSMHIgdKEKNFFGGNGIVGGQVPLAAGAALALKYRGEDRVAVCFFGDGATNEGDFHEALNFAALWKLPVIFV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478848 232 CENNKYGMGTSVERAAASTDYYKRGDF--IPGLRVDGMDVLCVREATKFAAEHCRSGKGPILMELQTYRYHGHSMSDPGV 309
Cdd:cd02000  161 CENNGYAISTPTSRQTAGTSIADRAAAygIPGIRVDGNDVLAVYEAAKEAVERARAGGGPTLIEAVTYRLGGHSTSDDPS 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 528478848 310 SYRTREEIQEvRSKSDPISLLKDRMLSNNMASVEELKEIDVEVRKEIEDAAQFA 363
Cdd:cd02000  241 RYRTKEEVEE-WKKRDPILRLRKYLIEAGILTEEELAAIEAEVKAEVEEAVEFA 293
AcoA COG1071
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ...
57-384 1.02e-148

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: 424.94  E-value: 1.02e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478848  57 EEGPAVQAVLTREEGLQYYRTMQTMRRMELKADQLYKQKIIrGFCHLYDGQEACAVGIEAGINLSDHLITAYRAHGYTLT 136
Cdd:COG1071    8 DGTEAALPDLSKEELLELYRDMLLIRRFEERALALQRQGKI-GFYHLSIGQEAAQVGAAAALRPGDWIFPTYRDHGHALA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478848 137 RGGTVREIMAELTGRRGGIAKGKGGSMHMYTK--HFYGGNGIVGAQVPLGAGVALACKYQGKNELCVCLYGDGAANQGQI 214
Cdd:COG1071   87 RGVDPKELMAELFGKATGPSKGRGGSMHFFDKelNFLGGSGIVGGQLPHAVGAALAAKLRGEDEVAVAFFGDGATSEGDF 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478848 215 FETYNMASLWKLPCIFICENNKYGMGTSVERAAASTDYYKRGD-F-IPGLRVDGMDVLCVREATKFAAEHCRSGKGPILM 292
Cdd:COG1071  167 HEALNFAAVWKLPVVFVCENNGYAISTPVERQTAVETIADRAAgYgIPGVRVDGNDVLAVYAAVKEAVERARAGEGPTLI 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478848 293 ELQTYRYHGHSMSDPGVSYRTREEIQEVRSKsDPISLLKDRMLSNNMASVEELKEIDVEVRKEIEDAAQFATTDPEPPLE 372
Cdd:COG1071  247 EAKTYRLGGHSTSDDPTRYRTKEEVEEWRER-DPIERLRAYLLEEGLLTEEELEAIEAEAKAEVEEAVEFAEASPEPDPE 325
                        330
                 ....*....|..
gi 528478848 373 DLCNHIFYNDPP 384
Cdd:COG1071  326 ELFDDVYAEPPP 337
PLN02374 PLN02374
pyruvate dehydrogenase (acetyl-transferring)
61-383 3.39e-86

pyruvate dehydrogenase (acetyl-transferring)


Pssm-ID: 215213 [Multi-domain]  Cd Length: 433  Bit Score: 268.73  E-value: 3.39e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478848  61 AVQAVLTREEGLQYYRTMQTMRRMELKADQLYKQKIIRGFCHLYDGQEACAVGIEAGINLSDHLITAYRAHGYTLTRGGT 140
Cdd:PLN02374  78 ASDLLVTREEGLELYEDMVLGRSFEDMCAQMYYRGKMFGFVHLYNGQEAVSTGFIKLLKKDDSVVSTYRDHVHALSKGVP 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478848 141 VREIMAELTGRRGGIAKGKGGSMHMYTK--HFYGGNGIVGAQVPLGAGVALACKYQ-------GKNELCVCLYGDGAANQ 211
Cdd:PLN02374 158 ARAVMSELFGKATGCCRGQGGSMHMFSKehNLLGGFAFIGEGIPVATGAAFSSKYRrevlkeeSCDDVTLAFFGDGTCNN 237
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478848 212 GQIFETYNMASLWKLPCIFICENNKYGMGTSVERAAASTDYYKRGDF--IPGLRVDGMDVLCVREATKFAAEHCRSGKGP 289
Cdd:PLN02374 238 GQFFECLNMAALWKLPIVFVVENNLWAIGMSHLRATSDPEIWKKGPAfgMPGVHVDGMDVLKVREVAKEAIERARRGEGP 317
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478848 290 ILMELQTYRYHGHSMSDPgvsyrtrEEIQEVRSKS-----DPISLLKDRMLSNNMASVEELKEIDVEVRKEIEDAAQFAT 364
Cdd:PLN02374 318 TLVECETYRFRGHSLADP-------DELRDPAEKAhyaarDPIAALKKYLIENGLATEAELKAIEKKIDEVVEDAVEFAD 390
                        330
                 ....*....|....*....
gi 528478848 365 TDPEPPLEDLCNHIFyNDP 383
Cdd:PLN02374 391 ASPLPPRSQLLENVF-ADP 408
odpA CHL00149
pyruvate dehydrogenase E1 component alpha subunit; Reviewed
66-379 1.26e-84

pyruvate dehydrogenase E1 component alpha subunit; Reviewed


Pssm-ID: 177069 [Multi-domain]  Cd Length: 341  Bit Score: 261.34  E-value: 1.26e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478848  66 LTREEGLQYYRTMQTMRRMELKADQLYKQKIIRGFCHLYDGQEACAVGIEAGINLSDHLITAYRAHGYTLTRGGTVREIM 145
Cdd:CHL00149  17 INSMWLLVLYEDMLLGRNFEDMCAQMYYRGKMFGFVHLYNGQEAVSTGVIKLLAETDYVCSTYRDHVHALSKGVPPKNVM 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478848 146 AELTGRRGGIAKGKGGSMHMYTK--HFYGGNGIVGAQVPLGAGVALACKYQ-------GKNELCVCLYGDGAANQGQIFE 216
Cdd:CHL00149  97 AELFGKETGCSRGRGGSMHIFSAphNFLGGFAFIGEGIPIALGAAFQSIYRqqvlkevQPLRVTACFFGDGTTNNGQFFE 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478848 217 TYNMASLWKLPCIFICENNKYGMGTSVERAAASTDYYKRGDF--IPGLRVDGMDVLCVREATKFAAEHCRSGKGPILMEL 294
Cdd:CHL00149 177 CLNMAVLWKLPIIFVVENNQWAIGMAHHRSTSIPEIHKKAEAfgLPGIEVDGMDVLAVREVAKEAVERARQGDGPTLIEA 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478848 295 QTYRYHGHSMSDPGvSYRTREEiQEVRSKSDPISLLKDRMLSNNMASVEELKEIDVEVRKEIEDAAQFATTDPEPPLEDL 374
Cdd:CHL00149 257 LTYRFRGHSLADPD-ELRSKQE-KEAWVARDPIKKLKSYIIDNELASQKELNKIQREVKIEIEQAVQFAISSPEPNISDL 334

                 ....*
gi 528478848 375 CNHIF 379
Cdd:CHL00149 335 KKYLF 339
TPP_E1_OGDC_like cd02016
Thiamine pyrophosphate (TPP) family, E1 of OGDC-like subfamily, TPP-binding module; composed ...
195-306 3.46e-07

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: 50.99  E-value: 3.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478848 195 GKNELCVCLYGDGA-ANQGQIFETYNMaslWKLP------CIFICENNKYGMGTSVERAAAS---TDYYKRGDfIPGLRV 264
Cdd:cd02016  138 RDKVLPILIHGDAAfAGQGVVYETLNL---SNLPgyttggTIHIVVNNQIGFTTDPRDSRSSpycTDVAKMIG-APIFHV 213
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 528478848 265 DGMDVLCVREATKFAAEHCRSGKGPILMELQTYRYHGHSMSD 306
Cdd:cd02016  214 NGDDPEAVVRATRLALEYRQKFKKDVVIDLVCYRRHGHNELD 255
TPP_TK cd02012
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ...
181-306 5.62e-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: 47.50  E-value: 5.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478848 181 VPLGAGVALACKYQGKNELCVCLYGDGAANQGQIFETYNMASLWKL-PCIFICENNKYGMGTSVERAAASTDYYKR---- 255
Cdd:cd02012  111 LSVAVGMALAEKLLGFDYRVYVLLGDGELQEGSVWEAASFAGHYKLdNLIAIVDSNRIQIDGPTDDILFTEDLAKKfeaf 190
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528478848 256 GDFIpgLRVDGMDVLCVREATKFAAEH--------CRS--GKGPILMElQTYRYHGHSMSD 306
Cdd:cd02012  191 GWNV--IEVDGHDVEEILAALEEAKKSkgkptliiAKTikGKGVPFME-NTAKWHGKPLGE 248
TPP_DXS cd02007
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ...
148-296 1.36e-03

Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; 1-Deoxy-D-xylulose-5-phosphate synthase (DXS) is a regulatory enzyme of the mevalonate-independent pathway involved in terpenoid biosynthesis. Terpeniods are plant natural products with important pharmaceutical activity. DXS catalyzes a transketolase-type condensation of pyruvate with D-glyceraldehyde-3-phosphate to form 1-deoxy-D-xylulose-5-phosphate (DXP) and carbon dioxide. The formation of DXP leads to the formation of the terpene precursor IPP (isopentyl diphosphate) and to the formation of thiamine (vitamin B1) and pyridoxal (vitamin B6).


Pssm-ID: 238965 [Multi-domain]  Cd Length: 195  Bit Score: 39.45  E-value: 1.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478848 148 LTGRRGGIA--KGKGGsMHMYTK-----HFYGGNGIVGAQVPLGAGVALACKYQGKNELCVCLYGDGAANQGQIFETYNM 220
Cdd:cd02007   42 LTGRRDQFHtlRQYGG-LSGFTKrseseYDAFGTGHSSTSISAALGMAVARDLKGKKRKVIAVIGDGALTGGMAFEALNN 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478848 221 ASLWKLPCIFICENNKYGMGTSVEraaASTDYYKrgDFipGLR----VDGMDVlcvrEATKFAAEHCRSGKGPILMELQT 296
Cdd:cd02007  121 AGYLKSNMIVILNDNEMSISPNVG---TPGNLFE--EL--GFRyigpVDGHNI----EALIKVLKEVKDLKGPVLLHVVT 189
PLN02234 PLN02234
1-deoxy-D-xylulose-5-phosphate synthase
148-236 3.52e-03

1-deoxy-D-xylulose-5-phosphate synthase


Pssm-ID: 177878 [Multi-domain]  Cd Length: 641  Bit Score: 39.70  E-value: 3.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478848 148 LTGRRGGIAK-GKGGSMHMYTK-----HFYGGNGIVGAQVPLGAGVALACKYQGKNELCVCLYGDGAANQGQIFETYNMA 221
Cdd:PLN02234 144 LTGRRGKMKTiRQTNGLSGYTKrreseHDSFGTGHSSTTLSAGLGMAVGRDLKGMNNSVVSVIGDGAMTAGQAYEAMNNA 223
                         90
                 ....*....|....*
gi 528478848 222 SLWKLPCIFICENNK 236
Cdd:PLN02234 224 GYLHSNMIVILNDNK 238
 
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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