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Conserved domains on  [gi|24639744|ref|NP_726946|]
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pyruvate dehydrogenase E1 alpha subunit, isoform D [Drosophila melanogaster]

Protein Classification

thiamine pyrophosphate-dependent enzyme( domain architecture ID 22)

thiamine pyrophosphate (TPP)-dependent enzyme uses thiamine pyrophosphate as a cofactor to catalyze various reactions including reversible decarboxylation

CATH:  3.40.50.1220
Gene Ontology:  GO:0030976|GO:0003824
PubMed:  12735696|15514159
SCOP:  3001790

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TPP_enzymes super family cl01629
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ...
34-382 3.71e-173

Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. These enzymes include, among others, the E1 components of the pyruvate, the acetoin and the branched chain alpha-keto acid dehydrogenase complexes.


The actual alignment was detected with superfamily member PLN02269:

Pssm-ID: 470272 [Multi-domain]  Cd Length: 362  Bit Score: 487.68  E-value: 3.71e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639744   34 ATEATVQVNRPFKLHRLDEgPATEVKLTKDQALKYYTQMQTIRRLETAAGNLYKEKIIRGFCHLYSGQEACAVGMKAAMR 113
Cdd:PLN02269   2 TDPITIETPVPFKGHLCDP-PSRTVETSKQELVDFFRDMYLMRRMEIAADSLYKAKLIRGFCHLYDGQEAVAVGMEAAIT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639744  114 DVDNIISAYRVHGwTYL-MGVSPSGVLAELTGVQGGCARGKGGSMHMYAP--NFYGGNGIVGAQVPLGAGVGLACKYKGN 190
Cdd:PLN02269  81 KEDAIITAYRDHC-THLgRGGTVLEVFAELMGRKDGCSRGKGGSMHFYKKdaNFYGGHGIVGAQVPLGAGLAFAQKYNKE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639744  191 GGMCLALYGDGAANQGQVFEAYNMAYLWKLPVIFVCENNNYGMGTSSERASCNTDYYTRGDALPGIWVDGMDVLAVRSAT 270
Cdd:PLN02269 160 ENVAFALYGDGAANQGQLFEALNIAALWDLPVIFVCENNHYGMGTAEWRAAKSPAYYKRGDYVPGLKVDGMDVLAVKQAC 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639744  271 EFAINYVNTHGPLVMETNTYRYSGHSMSDPGTSYRTREEIQEVRQKRDPITSFKELCIELGLITTDEVKAIDLKVRKEVD 350
Cdd:PLN02269 240 KFAKEHALSNGPIVLEMDTYRYHGHSMSDPGSTYRTRDEISGVRQERDPIERVRKLLLAHELATEAELKDIEKEIRKEVD 319
                        330       340       350
                 ....*....|....*....|....*....|..
gi 24639744  351 EATAFAKSDAELGVSHLWTDVYSNNLEPKLRG 382
Cdd:PLN02269 320 DAVAKAKESPMPDPSELFTNVYVKGLGVESYG 351
 
Name Accession Description Interval E-value
PLN02269 PLN02269
Pyruvate dehydrogenase E1 component subunit alpha
34-382 3.71e-173

Pyruvate dehydrogenase E1 component subunit alpha


Pssm-ID: 215152 [Multi-domain]  Cd Length: 362  Bit Score: 487.68  E-value: 3.71e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639744   34 ATEATVQVNRPFKLHRLDEgPATEVKLTKDQALKYYTQMQTIRRLETAAGNLYKEKIIRGFCHLYSGQEACAVGMKAAMR 113
Cdd:PLN02269   2 TDPITIETPVPFKGHLCDP-PSRTVETSKQELVDFFRDMYLMRRMEIAADSLYKAKLIRGFCHLYDGQEAVAVGMEAAIT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639744  114 DVDNIISAYRVHGwTYL-MGVSPSGVLAELTGVQGGCARGKGGSMHMYAP--NFYGGNGIVGAQVPLGAGVGLACKYKGN 190
Cdd:PLN02269  81 KEDAIITAYRDHC-THLgRGGTVLEVFAELMGRKDGCSRGKGGSMHFYKKdaNFYGGHGIVGAQVPLGAGLAFAQKYNKE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639744  191 GGMCLALYGDGAANQGQVFEAYNMAYLWKLPVIFVCENNNYGMGTSSERASCNTDYYTRGDALPGIWVDGMDVLAVRSAT 270
Cdd:PLN02269 160 ENVAFALYGDGAANQGQLFEALNIAALWDLPVIFVCENNHYGMGTAEWRAAKSPAYYKRGDYVPGLKVDGMDVLAVKQAC 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639744  271 EFAINYVNTHGPLVMETNTYRYSGHSMSDPGTSYRTREEIQEVRQKRDPITSFKELCIELGLITTDEVKAIDLKVRKEVD 350
Cdd:PLN02269 240 KFAKEHALSNGPIVLEMDTYRYHGHSMSDPGSTYRTRDEISGVRQERDPIERVRKLLLAHELATEAELKDIEKEIRKEVD 319
                        330       340       350
                 ....*....|....*....|....*....|..
gi 24639744  351 EATAFAKSDAELGVSHLWTDVYSNNLEPKLRG 382
Cdd:PLN02269 320 DAVAKAKESPMPDPSELFTNVYVKGLGVESYG 351
PDH_E1_alph_y TIGR03182
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the ...
62-373 7.99e-166

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: 467.05  E-value: 7.99e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639744    62 KDQALKYYTQMQTIRRLETAAGNLYKEKIIRGFCHLYSGQEACAVGMKAAMRDVDNIISAYRVHGWTYLMGVSPSGVLAE 141
Cdd:TIGR03182   1 KEELLELYRDMLLIRRFEEKAGQLYGMGKIGGFCHLYIGQEAVAVGLIAALKPDDYVITSYRDHGHALARGVPPKEVMAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639744   142 LTGVQGGCARGKGGSMHMYAP--NFYGGNGIVGAQVPLGAGVGLACKYKGNGGMCLALYGDGAANQGQVFEAYNMAYLWK 219
Cdd:TIGR03182  81 LTGRETGCSKGKGGSMHMFDRekNFYGGHGIVGAQVPLATGLAFANKYRGNDNVTACFFGDGAANQGQFYESFNMAALWK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639744   220 LPVIFVCENNNYGMGTSSERASCNTDYYTRGDA--LPGIWVDGMDVLAVRSATEFAINYV-NTHGPLVMETNTYRYSGHS 296
Cdd:TIGR03182 161 LPVIFVIENNLYAMGTAVERSSSVTDLYKRGESfgIPGERVDGMDVLAVREAAKEAVERArSGKGPILLEMKTYRFRGHS 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24639744   297 MSDPGtSYRTREEIQEVRqKRDPITSFKELCIELGLITTDEVKAIDLKVRKEVDEATAFAKSDAELGVSHLWTDVYS 373
Cdd:TIGR03182 241 MSDPA-KYRSKEEVEEWR-KRDPIEKLKARLIEQGIASEEELKEIDKEVRAEVEEAVEFAENSPEPPVEELYTDVYA 315
AcoA COG1071
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ...
51-374 5.16e-135

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: 390.27  E-value: 5.16e-135
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639744  51 DEGPATEVKLTKDQALKYYTQMQTIRRLETAAGNLYKEKIIrGFCHLYSGQEACAVGMKAAMRDVDNIISAYRVHGWTYL 130
Cdd:COG1071   8 DGTEAALPDLSKEELLELYRDMLLIRRFEERALALQRQGKI-GFYHLSIGQEAAQVGAAAALRPGDWIFPTYRDHGHALA 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639744 131 MGVSPSGVLAELTGVQGGCARGKGGSMHMYAP--NFYGGNGIVGAQVPLGAGVGLACKYKGNGGMCLALYGDGAANQGQV 208
Cdd:COG1071  87 RGVDPKELMAELFGKATGPSKGRGGSMHFFDKelNFLGGSGIVGGQLPHAVGAALAAKLRGEDEVAVAFFGDGATSEGDF 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639744 209 FEAYNMAYLWKLPVIFVCENNNYGMGTSSERASCNTDYYTRGDA--LPGIWVDGMDVLAVRSATEFAINYV-NTHGPLVM 285
Cdd:COG1071 167 HEALNFAAVWKLPVVFVCENNGYAISTPVERQTAVETIADRAAGygIPGVRVDGNDVLAVYAAVKEAVERArAGEGPTLI 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639744 286 ETNTYRYSGHSMSDPGTSYRTREEIQEVRqKRDPITSFKELCIELGLITTDEVKAIDLKVRKEVDEATAFAKSDAELGVS 365
Cdd:COG1071 247 EAKTYRLGGHSTSDDPTRYRTKEEVEEWR-ERDPIERLRAYLLEEGLLTEEELEAIEAEAKAEVEEAVEFAEASPEPDPE 325

                ....*....
gi 24639744 366 HLWTDVYSN 374
Cdd:COG1071 326 ELFDDVYAE 334
TPP_E1_PDC_ADC_BCADC cd02000
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ...
68-356 8.71e-135

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: 387.24  E-value: 8.71e-135
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639744  68 YYTQMQTIRRLETAAGNLYKEKIIRGFCHLYSGQEACAVGMKAAMRDVDNIISAYRVHGWTYLMGVSPSGVLAELTGVQG 147
Cdd:cd02000   1 LYRTMVLIRRFDERLLELYRQGKIGGFYHLSIGQEAVAVGVAAALRPGDWVFPTYRDHGHALARGVDLKEMLAELFGKET 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639744 148 GCARGKGGSMHM--YAPNFYGGNGIVGAQVPLGAGVGLACKYKGNGGMCLALYGDGAANQGQVFEAYNMAYLWKLPVIFV 225
Cdd:cd02000  81 GPCKGRGGSMHIgdKEKNFFGGNGIVGGQVPLAAGAALALKYRGEDRVAVCFFGDGATNEGDFHEALNFAALWKLPVIFV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639744 226 CENNNYGMGTSSERASCNTDYYTRGDA--LPGIWVDGMDVLAVRSATEFAINYV-NTHGPLVMETNTYRYSGHSMSDPGT 302
Cdd:cd02000 161 CENNGYAISTPTSRQTAGTSIADRAAAygIPGIRVDGNDVLAVYEAAKEAVERArAGGGPTLIEAVTYRLGGHSTSDDPS 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 24639744 303 SYRTREEIQEvRQKRDPITSFKELCIELGLITTDEVKAIDLKVRKEVDEATAFA 356
Cdd:cd02000 241 RYRTKEEVEE-WKKRDPILRLRKYLIEAGILTEEELAAIEAEVKAEVEEAVEFA 293
E1_dh pfam00676
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ...
72-365 3.37e-131

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: 378.59  E-value: 3.37e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639744    72 MQTIRRLETAAGNLYKEKIIRGFCHLYSGQEACAVGMKAAMRDVDNIISAYRVHGWTYLMGVSPSGVLAELTGVQGgcaR 151
Cdd:pfam00676   3 MMTLRRMEDARDALYKRQGIRGFYHLYAGQEAAQVGIAAALEPGDYIIPGYRDHGNLLARGLSLEEIFAELYGRVA---K 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639744   152 GKGGSMHMYA----PNFYGGNGIVGAQVPLGAGVGLACKYKGNGGMCLALYGDGAANQGQVFEAYNMAYLWKLPVIFVCE 227
Cdd:pfam00676  80 GKGGSMHGYYgakgNRFYGGNGILGAQVPLGAGIALAAKYRGKKEVAITLYGDGAANQGDFFEGLNFAALWKLPVIFVCE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639744   228 NNNYGMGTSSERASCNTDYYT--RGDALPGIWVDGMDVLAVRSATEFAINY-VNTHGPLVMETNTYRYSGHSMSDPGTSY 304
Cdd:pfam00676 160 NNQYGISTPAERASASTTYADraRGYGIPGLHVDGMDPLAVYQASKFAAERaRTGKGPFLIELVTYRYGGHSMSDDPSTY 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24639744   305 RTREEIQEVRQKRDPITSFKELCIELGLITTDEVKAIDLKVRKEVDEATAFAKSDAELGVS 365
Cdd:pfam00676 240 RTRDEYEEVRKKKDPIQRFKEHLVSKGVWSEEELKAIEKEVRKEVEEAFKKAESAPEPHPE 300
 
Name Accession Description Interval E-value
PLN02269 PLN02269
Pyruvate dehydrogenase E1 component subunit alpha
34-382 3.71e-173

Pyruvate dehydrogenase E1 component subunit alpha


Pssm-ID: 215152 [Multi-domain]  Cd Length: 362  Bit Score: 487.68  E-value: 3.71e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639744   34 ATEATVQVNRPFKLHRLDEgPATEVKLTKDQALKYYTQMQTIRRLETAAGNLYKEKIIRGFCHLYSGQEACAVGMKAAMR 113
Cdd:PLN02269   2 TDPITIETPVPFKGHLCDP-PSRTVETSKQELVDFFRDMYLMRRMEIAADSLYKAKLIRGFCHLYDGQEAVAVGMEAAIT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639744  114 DVDNIISAYRVHGwTYL-MGVSPSGVLAELTGVQGGCARGKGGSMHMYAP--NFYGGNGIVGAQVPLGAGVGLACKYKGN 190
Cdd:PLN02269  81 KEDAIITAYRDHC-THLgRGGTVLEVFAELMGRKDGCSRGKGGSMHFYKKdaNFYGGHGIVGAQVPLGAGLAFAQKYNKE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639744  191 GGMCLALYGDGAANQGQVFEAYNMAYLWKLPVIFVCENNNYGMGTSSERASCNTDYYTRGDALPGIWVDGMDVLAVRSAT 270
Cdd:PLN02269 160 ENVAFALYGDGAANQGQLFEALNIAALWDLPVIFVCENNHYGMGTAEWRAAKSPAYYKRGDYVPGLKVDGMDVLAVKQAC 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639744  271 EFAINYVNTHGPLVMETNTYRYSGHSMSDPGTSYRTREEIQEVRQKRDPITSFKELCIELGLITTDEVKAIDLKVRKEVD 350
Cdd:PLN02269 240 KFAKEHALSNGPIVLEMDTYRYHGHSMSDPGSTYRTRDEISGVRQERDPIERVRKLLLAHELATEAELKDIEKEIRKEVD 319
                        330       340       350
                 ....*....|....*....|....*....|..
gi 24639744  351 EATAFAKSDAELGVSHLWTDVYSNNLEPKLRG 382
Cdd:PLN02269 320 DAVAKAKESPMPDPSELFTNVYVKGLGVESYG 351
PDH_E1_alph_y TIGR03182
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the ...
62-373 7.99e-166

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: 467.05  E-value: 7.99e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639744    62 KDQALKYYTQMQTIRRLETAAGNLYKEKIIRGFCHLYSGQEACAVGMKAAMRDVDNIISAYRVHGWTYLMGVSPSGVLAE 141
Cdd:TIGR03182   1 KEELLELYRDMLLIRRFEEKAGQLYGMGKIGGFCHLYIGQEAVAVGLIAALKPDDYVITSYRDHGHALARGVPPKEVMAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639744   142 LTGVQGGCARGKGGSMHMYAP--NFYGGNGIVGAQVPLGAGVGLACKYKGNGGMCLALYGDGAANQGQVFEAYNMAYLWK 219
Cdd:TIGR03182  81 LTGRETGCSKGKGGSMHMFDRekNFYGGHGIVGAQVPLATGLAFANKYRGNDNVTACFFGDGAANQGQFYESFNMAALWK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639744   220 LPVIFVCENNNYGMGTSSERASCNTDYYTRGDA--LPGIWVDGMDVLAVRSATEFAINYV-NTHGPLVMETNTYRYSGHS 296
Cdd:TIGR03182 161 LPVIFVIENNLYAMGTAVERSSSVTDLYKRGESfgIPGERVDGMDVLAVREAAKEAVERArSGKGPILLEMKTYRFRGHS 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24639744   297 MSDPGtSYRTREEIQEVRqKRDPITSFKELCIELGLITTDEVKAIDLKVRKEVDEATAFAKSDAELGVSHLWTDVYS 373
Cdd:TIGR03182 241 MSDPA-KYRSKEEVEEWR-KRDPIEKLKARLIEQGIASEEELKEIDKEVRAEVEEAVEFAENSPEPPVEELYTDVYA 315
AcoA COG1071
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ...
51-374 5.16e-135

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: 390.27  E-value: 5.16e-135
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639744  51 DEGPATEVKLTKDQALKYYTQMQTIRRLETAAGNLYKEKIIrGFCHLYSGQEACAVGMKAAMRDVDNIISAYRVHGWTYL 130
Cdd:COG1071   8 DGTEAALPDLSKEELLELYRDMLLIRRFEERALALQRQGKI-GFYHLSIGQEAAQVGAAAALRPGDWIFPTYRDHGHALA 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639744 131 MGVSPSGVLAELTGVQGGCARGKGGSMHMYAP--NFYGGNGIVGAQVPLGAGVGLACKYKGNGGMCLALYGDGAANQGQV 208
Cdd:COG1071  87 RGVDPKELMAELFGKATGPSKGRGGSMHFFDKelNFLGGSGIVGGQLPHAVGAALAAKLRGEDEVAVAFFGDGATSEGDF 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639744 209 FEAYNMAYLWKLPVIFVCENNNYGMGTSSERASCNTDYYTRGDA--LPGIWVDGMDVLAVRSATEFAINYV-NTHGPLVM 285
Cdd:COG1071 167 HEALNFAAVWKLPVVFVCENNGYAISTPVERQTAVETIADRAAGygIPGVRVDGNDVLAVYAAVKEAVERArAGEGPTLI 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639744 286 ETNTYRYSGHSMSDPGTSYRTREEIQEVRqKRDPITSFKELCIELGLITTDEVKAIDLKVRKEVDEATAFAKSDAELGVS 365
Cdd:COG1071 247 EAKTYRLGGHSTSDDPTRYRTKEEVEEWR-ERDPIERLRAYLLEEGLLTEEELEAIEAEAKAEVEEAVEFAEASPEPDPE 325

                ....*....
gi 24639744 366 HLWTDVYSN 374
Cdd:COG1071 326 ELFDDVYAE 334
TPP_E1_PDC_ADC_BCADC cd02000
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ...
68-356 8.71e-135

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: 387.24  E-value: 8.71e-135
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639744  68 YYTQMQTIRRLETAAGNLYKEKIIRGFCHLYSGQEACAVGMKAAMRDVDNIISAYRVHGWTYLMGVSPSGVLAELTGVQG 147
Cdd:cd02000   1 LYRTMVLIRRFDERLLELYRQGKIGGFYHLSIGQEAVAVGVAAALRPGDWVFPTYRDHGHALARGVDLKEMLAELFGKET 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639744 148 GCARGKGGSMHM--YAPNFYGGNGIVGAQVPLGAGVGLACKYKGNGGMCLALYGDGAANQGQVFEAYNMAYLWKLPVIFV 225
Cdd:cd02000  81 GPCKGRGGSMHIgdKEKNFFGGNGIVGGQVPLAAGAALALKYRGEDRVAVCFFGDGATNEGDFHEALNFAALWKLPVIFV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639744 226 CENNNYGMGTSSERASCNTDYYTRGDA--LPGIWVDGMDVLAVRSATEFAINYV-NTHGPLVMETNTYRYSGHSMSDPGT 302
Cdd:cd02000 161 CENNGYAISTPTSRQTAGTSIADRAAAygIPGIRVDGNDVLAVYEAAKEAVERArAGGGPTLIEAVTYRLGGHSTSDDPS 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 24639744 303 SYRTREEIQEvRQKRDPITSFKELCIELGLITTDEVKAIDLKVRKEVDEATAFA 356
Cdd:cd02000 241 RYRTKEEVEE-WKKRDPILRLRKYLIEAGILTEEELAAIEAEVKAEVEEAVEFA 293
E1_dh pfam00676
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ...
72-365 3.37e-131

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: 378.59  E-value: 3.37e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639744    72 MQTIRRLETAAGNLYKEKIIRGFCHLYSGQEACAVGMKAAMRDVDNIISAYRVHGWTYLMGVSPSGVLAELTGVQGgcaR 151
Cdd:pfam00676   3 MMTLRRMEDARDALYKRQGIRGFYHLYAGQEAAQVGIAAALEPGDYIIPGYRDHGNLLARGLSLEEIFAELYGRVA---K 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639744   152 GKGGSMHMYA----PNFYGGNGIVGAQVPLGAGVGLACKYKGNGGMCLALYGDGAANQGQVFEAYNMAYLWKLPVIFVCE 227
Cdd:pfam00676  80 GKGGSMHGYYgakgNRFYGGNGILGAQVPLGAGIALAAKYRGKKEVAITLYGDGAANQGDFFEGLNFAALWKLPVIFVCE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639744   228 NNNYGMGTSSERASCNTDYYT--RGDALPGIWVDGMDVLAVRSATEFAINY-VNTHGPLVMETNTYRYSGHSMSDPGTSY 304
Cdd:pfam00676 160 NNQYGISTPAERASASTTYADraRGYGIPGLHVDGMDPLAVYQASKFAAERaRTGKGPFLIELVTYRYGGHSMSDDPSTY 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24639744   305 RTREEIQEVRQKRDPITSFKELCIELGLITTDEVKAIDLKVRKEVDEATAFAKSDAELGVS 365
Cdd:pfam00676 240 RTRDEYEEVRKKKDPIQRFKEHLVSKGVWSEEELKAIEKEVRKEVEEAFKKAESAPEPHPE 300
PLN02374 PLN02374
pyruvate dehydrogenase (acetyl-transferring)
55-374 2.88e-77

pyruvate dehydrogenase (acetyl-transferring)


Pssm-ID: 215213 [Multi-domain]  Cd Length: 433  Bit Score: 245.62  E-value: 2.88e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639744   55 ATEVKLTKDQALKYYTQMQTIRRLETAAGNLYKEKIIRGFCHLYSGQEACAVGMKAAMRDVDNIISAYRVHGWTYLMGVS 134
Cdd:PLN02374  78 ASDLLVTREEGLELYEDMVLGRSFEDMCAQMYYRGKMFGFVHLYNGQEAVSTGFIKLLKKDDSVVSTYRDHVHALSKGVP 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639744  135 PSGVLAELTGVQGGCARGKGGSMHMYAP--NFYGGNGIVGAQVPLGAGVGLACKYK-------GNGGMCLALYGDGAANQ 205
Cdd:PLN02374 158 ARAVMSELFGKATGCCRGQGGSMHMFSKehNLLGGFAFIGEGIPVATGAAFSSKYRrevlkeeSCDDVTLAFFGDGTCNN 237
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639744  206 GQVFEAYNMAYLWKLPVIFVCENNNYGMGTSSERASCNTDYYTRGDA--LPGIWVDGMDVLAVRSATEFAINYVNT-HGP 282
Cdd:PLN02374 238 GQFFECLNMAALWKLPIVFVVENNLWAIGMSHLRATSDPEIWKKGPAfgMPGVHVDGMDVLKVREVAKEAIERARRgEGP 317
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639744  283 LVMETNTYRYSGHSMSDPgtsyrtrEEIQEVRQK-----RDPITSFKELCIELGLITTDEVKAIDLKVRKEVDEATAFAK 357
Cdd:PLN02374 318 TLVECETYRFRGHSLADP-------DELRDPAEKahyaaRDPIAALKKYLIENGLATEAELKAIEKKIDEVVEDAVEFAD 390
                        330
                 ....*....|....*..
gi 24639744  358 SDAELGVSHLWTDVYSN 374
Cdd:PLN02374 391 ASPLPPRSQLLENVFAD 407
odpA CHL00149
pyruvate dehydrogenase E1 component alpha subunit; Reviewed
56-374 3.09e-74

pyruvate dehydrogenase E1 component alpha subunit; Reviewed


Pssm-ID: 177069 [Multi-domain]  Cd Length: 341  Bit Score: 234.76  E-value: 3.09e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639744   56 TEVKLTKDQALKYYTQMQTIRRLETAAGNLYKEKIIRGFCHLYSGQEACAVGMKAAMRDVDNIISAYRVHGWTYLMGVSP 135
Cdd:CHL00149  13 NENNINSMWLLVLYEDMLLGRNFEDMCAQMYYRGKMFGFVHLYNGQEAVSTGVIKLLAETDYVCSTYRDHVHALSKGVPP 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639744  136 SGVLAELTGVQGGCARGKGGSMHMY-AP-NFYGGNGIVGAQVPLGAGVGLA-------CKYKGNGGMCLALYGDGAANQG 206
Cdd:CHL00149  93 KNVMAELFGKETGCSRGRGGSMHIFsAPhNFLGGFAFIGEGIPIALGAAFQsiyrqqvLKEVQPLRVTACFFGDGTTNNG 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639744  207 QVFEAYNMAYLWKLPVIFVCENNNYGMGTSSERASCNTDYYTRGDA--LPGIWVDGMDVLAVRSATEFAINYVNT-HGPL 283
Cdd:CHL00149 173 QFFECLNMAVLWKLPIIFVVENNQWAIGMAHHRSTSIPEIHKKAEAfgLPGIEVDGMDVLAVREVAKEAVERARQgDGPT 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639744  284 VMETNTYRYSGHSMSDPgTSYRTREEiQEVRQKRDPITSFKELCIELGLITTDEVKAIDLKVRKEVDEATAFAKSDAELG 363
Cdd:CHL00149 253 LIEALTYRFRGHSLADP-DELRSKQE-KEAWVARDPIKKLKSYIIDNELASQKELNKIQREVKIEIEQAVQFAISSPEPN 330
                        330
                 ....*....|.
gi 24639744  364 VSHLWTDVYSN 374
Cdd:CHL00149 331 ISDLKKYLFAD 341
TPP_E1_OGDC_like cd02016
Thiamine pyrophosphate (TPP) family, E1 of OGDC-like subfamily, TPP-binding module; composed ...
193-299 1.21e-05

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: 46.37  E-value: 1.21e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639744 193 MCLALYGDGA-ANQGQVFEAYNMaylWKLP------VIFVCENNNYGMGTSSERAScNTDYYT---RGDALPGIWVDGMD 262
Cdd:cd02016 142 LPILIHGDAAfAGQGVVYETLNL---SNLPgyttggTIHIVVNNQIGFTTDPRDSR-SSPYCTdvaKMIGAPIFHVNGDD 217
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 24639744 263 VLAVRSATEFAINYVNTHG-PLVMETNTYRYSGHSMSD 299
Cdd:cd02016 218 PEAVVRATRLALEYRQKFKkDVVIDLVCYRRHGHNELD 255
TPP_TK cd02012
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ...
176-289 1.82e-03

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: 39.79  E-value: 1.82e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639744 176 PLGAGVGLACkykgngGMCLA------------LYGDGAANQGQVFEAYNMAYLWKL-PVIFVCENNNYGMGTSSERASC 242
Cdd:cd02012 106 SLGQGLSVAV------GMALAekllgfdyrvyvLLGDGELQEGSVWEAASFAGHYKLdNLIAIVDSNRIQIDGPTDDILF 179
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 24639744 243 NTDYYTRGDALpG---IWVDGMDVLAVRSATEFAinYVNTHGPLVMETNT 289
Cdd:cd02012 180 TEDLAKKFEAF-GwnvIEVDGHDVEEILAALEEA--KKSKGKPTLIIAKT 226
 
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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