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Conserved domains on  [gi|501246444|ref|WP_012289462|]
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pyruvate dehydrogenase (acetyl-transferring) E1 component subunit alpha [Halobacterium salinarum]

Protein Classification

thiamine pyrophosphate-dependent dehydrogenase E1 component subunit alpha( domain architecture ID 10799054)

thiamine pyrophosphate-dependent dehydrogenase E1 component subunit alpha is part of the E1 component of a multi-enzyme dehydrogenase complex such as pyruvate dehydrogenase, which catalyzes the overall conversion of pyruvate to acetyl-CoA and carbon dioxide

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PDH_E1_alph_x TIGR03181
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the ...
11-356 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: 213783 [Multi-domain]  Cd Length: 341  Bit Score: 537.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246444   11 DTYRVLDENGELVDGAEVPDLTDDELVEMYRYMKLARRFDERAVSLQRQGRIGTYPPLSGQEGAQIASAMALADDDWIVP 90
Cdd:TIGR03181   1 ELVQVLDEDGNVVDPEPAPDLSDEELVELYRDMVLTRRFDTKALALQRQGRLGTYAPNLGQEAAQVGSALALRKDDWVFP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246444   91 SYREHGASLVRGLPLKDTLLYWMGDERGNAIPAEENIFTVAVPIASQIPHATGMGWASQLKDEsDTAFMCYFGDGATSEG 170
Cdd:TIGR03181  81 SYRDHAAMLARGVPLVEILLYWRGDERGSWDPEGVNILPPNIPIGTQYLHAAGVAYALKLRGE-DNVAVTYFGDGGTSEG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246444  171 DFHEGLNFAGVYDTPNVFFCNNNQWAISVPREQQTATDTLAQKAAAYGFEGVQVDGMDPLAVYQVAHDAIEKAKDPDede 250
Cdd:TIGR03181 160 DFYEALNFAGVFKAPVVFFVQNNQWAISVPRSKQTAAPTLAQKAIAYGIPGVQVDGNDVLAVYAVTKEAVERARSGG--- 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246444  251 mRPTLIEAVQYRFGAHTTADDPSVYREESEVEAWKDKDPIPRLETFLVETDRLDDAAIESIEADIEDAVADAIEAAEETP 330
Cdd:TIGR03181 237 -GPTLIEAVTYRLGPHTTADDPTRYRTKEEEEEWRKKDPILRLRKYLERKGLWDEEQEEALEEEAEAEVAEAVAEALALP 315
                         330       340
                  ....*....|....*....|....*.
gi 501246444  331 RPDPASMFENVYAEMPQRLEQQLEYF 356
Cdd:TIGR03181 316 PPPVDDIFDHVYAELPPELEEQRAEL 341
 
Name Accession Description Interval E-value
PDH_E1_alph_x TIGR03181
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the ...
11-356 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: 213783 [Multi-domain]  Cd Length: 341  Bit Score: 537.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246444   11 DTYRVLDENGELVDGAEVPDLTDDELVEMYRYMKLARRFDERAVSLQRQGRIGTYPPLSGQEGAQIASAMALADDDWIVP 90
Cdd:TIGR03181   1 ELVQVLDEDGNVVDPEPAPDLSDEELVELYRDMVLTRRFDTKALALQRQGRLGTYAPNLGQEAAQVGSALALRKDDWVFP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246444   91 SYREHGASLVRGLPLKDTLLYWMGDERGNAIPAEENIFTVAVPIASQIPHATGMGWASQLKDEsDTAFMCYFGDGATSEG 170
Cdd:TIGR03181  81 SYRDHAAMLARGVPLVEILLYWRGDERGSWDPEGVNILPPNIPIGTQYLHAAGVAYALKLRGE-DNVAVTYFGDGGTSEG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246444  171 DFHEGLNFAGVYDTPNVFFCNNNQWAISVPREQQTATDTLAQKAAAYGFEGVQVDGMDPLAVYQVAHDAIEKAKDPDede 250
Cdd:TIGR03181 160 DFYEALNFAGVFKAPVVFFVQNNQWAISVPRSKQTAAPTLAQKAIAYGIPGVQVDGNDVLAVYAVTKEAVERARSGG--- 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246444  251 mRPTLIEAVQYRFGAHTTADDPSVYREESEVEAWKDKDPIPRLETFLVETDRLDDAAIESIEADIEDAVADAIEAAEETP 330
Cdd:TIGR03181 237 -GPTLIEAVTYRLGPHTTADDPTRYRTKEEEEEWRKKDPILRLRKYLERKGLWDEEQEEALEEEAEAEVAEAVAEALALP 315
                         330       340
                  ....*....|....*....|....*.
gi 501246444  331 RPDPASMFENVYAEMPQRLEQQLEYF 356
Cdd:TIGR03181 316 PPPVDDIFDHVYAELPPELEEQRAEL 341
AcoA COG1071
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ...
12-356 8.88e-169

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: 474.63  E-value: 8.88e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246444  12 TYRVLDENGElvdGAEVPDLTDDELVEMYRYMKLARRFDERAVSLQRQGRIGTYPPLSGQEGAQIASAMALADDDWIVPS 91
Cdd:COG1071    1 LVQVLDPDGT---EAALPDLSKEELLELYRDMLLIRRFEERALALQRQGKIGFYHLSIGQEAAQVGAAAALRPGDWIFPT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246444  92 YREHGASLVRGLPLKDTLLYWMGDE----RGNAIP-----AEENIFTVAVPIASQIPHATGMGWASQLKDEsDTAFMCYF 162
Cdd:COG1071   78 YRDHGHALARGVDPKELMAELFGKAtgpsKGRGGSmhffdKELNFLGGSGIVGGQLPHAVGAALAAKLRGE-DEVAVAFF 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246444 163 GDGATSEGDFHEGLNFAGVYDTPNVFFCNNNQWAISVPREQQTATDTLAQKAAAYGFEGVQVDGMDPLAVYQVAHDAIEK 242
Cdd:COG1071  157 GDGATSEGDFHEALNFAAVWKLPVVFVCENNGYAISTPVERQTAVETIADRAAGYGIPGVRVDGNDVLAVYAAVKEAVER 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246444 243 AKDPDedemRPTLIEAVQYRFGAHTTADDPSVYREESEVEAWKDKDPIPRLETFLVETDRLDDAAIESIEADIEDAVADA 322
Cdd:COG1071  237 ARAGE----GPTLIEAKTYRLGGHSTSDDPTRYRTKEEVEEWRERDPIERLRAYLLEEGLLTEEELEAIEAEAKAEVEEA 312
                        330       340       350
                 ....*....|....*....|....*....|....
gi 501246444 323 IEAAEETPRPDPASMFENVYAEMPQRLEQQLEYF 356
Cdd:COG1071  313 VEFAEASPEPDPEELFDDVYAEPPPHLAEQRAEL 346
TPP_E1_PDC_ADC_BCADC cd02000
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ...
39-326 3.23e-133

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: 382.23  E-value: 3.23e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246444  39 MYRYMKLARRFDERAVSLQRQGRI-GTYPPLSGQEGAQIASAMALADDDWIVPSYREHGASLVRGLPLKDTLLYWMGDER 117
Cdd:cd02000    1 LYRTMVLIRRFDERLLELYRQGKIgGFYHLSIGQEAVAVGVAAALRPGDWVFPTYRDHGHALARGVDLKEMLAELFGKET 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246444 118 GNA---------IPAEENIFTVAVPIASQIPHATGMGWASQLKDESDTAFmCYFGDGATSEGDFHEGLNFAGVYDTPNVF 188
Cdd:cd02000   81 GPCkgrggsmhiGDKEKNFFGGNGIVGGQVPLAAGAALALKYRGEDRVAV-CFFGDGATNEGDFHEALNFAALWKLPVIF 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246444 189 FCNNNQWAISVPREQQTATDTLAQKAAAYGFEGVQVDGMDPLAVYQVAHDAIEKAkdpdEDEMRPTLIEAVQYRFGAHTT 268
Cdd:cd02000  160 VCENNGYAISTPTSRQTAGTSIADRAAAYGIPGIRVDGNDVLAVYEAAKEAVERA----RAGGGPTLIEAVTYRLGGHST 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 501246444 269 ADDPSVYREESEVEAWKDKDPIPRLETFLVETDRLDDAAIESIEADIEDAVADAIEAA 326
Cdd:cd02000  236 SDDPSRYRTKEEVEEWKKRDPILRLRKYLIEAGILTEEELAAIEAEVKAEVEEAVEFA 293
E1_dh pfam00676
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ...
40-334 2.20e-91

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: 276.13  E-value: 2.20e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246444   40 YRYMKLARRFDERAVSLQRQGRIGTYPPLSGQEGAQIASAMALADDDWIVPSYREHGASLVRGLPLKDTLLYWMGDE--- 116
Cdd:pfam00676   1 RRMMTLRRMEDARDALYKRQGIRGFYHLYAGQEAAQVGIAAALEPGDYIIPGYRDHGNLLARGLSLEEIFAELYGRVakg 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246444  117 -----RGNAIPAEENIFTVAVPIASQIPHATGMGWASQLKDESDTAFmCYFGDGATSEGDFHEGLNFAGVYDTPNVFFCN 191
Cdd:pfam00676  81 kggsmHGYYGAKGNRFYGGNGILGAQVPLGAGIALAAKYRGKKEVAI-TLYGDGAANQGDFFEGLNFAALWKLPVIFVCE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246444  192 NNQWAISVPREQQTATDTLAQKAAAYGFEGVQVDGMDPLAVYQVAHDAIEKAKDPDedemRPTLIEAVQYRFGAHTTADD 271
Cdd:pfam00676 160 NNQYGISTPAERASASTTYADRARGYGIPGLHVDGMDPLAVYQASKFAAERARTGK----GPFLIELVTYRYGGHSMSDD 235
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501246444  272 PSVYREESEVEA-WKDKDPIPRLETFLVETDRLDDAAIESIEADIEDAVADAIEAAEETPRPDP 334
Cdd:pfam00676 236 PSTYRTRDEYEEvRKKKDPIQRFKEHLVSKGVWSEEELKAIEKEVRKEVEEAFKKAESAPEPHP 299
PLN02374 PLN02374
pyruvate dehydrogenase (acetyl-transferring)
31-344 1.41e-54

pyruvate dehydrogenase (acetyl-transferring)


Pssm-ID: 215213 [Multi-domain]  Cd Length: 433  Bit Score: 185.53  E-value: 1.41e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246444  31 LTDDELVEMYRYMKLARRFDERAVSLQRQGRIGTYPPL-SGQEGAQIASAMALADDDWIVPSYREHGASLVRGLPLKDTL 109
Cdd:PLN02374  83 VTREEGLELYEDMVLGRSFEDMCAQMYYRGKMFGFVHLyNGQEAVSTGFIKLLKKDDSVVSTYRDHVHALSKGVPARAVM 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246444 110 LYWMGDERG---------NAIPAEENIFTVAVPIASQIPHATGMGWASQ-----LKDESDTAFMC-YFGDGATSEGDFHE 174
Cdd:PLN02374 163 SELFGKATGccrgqggsmHMFSKEHNLLGGFAFIGEGIPVATGAAFSSKyrrevLKEESCDDVTLaFFGDGTCNNGQFFE 242
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246444 175 GLNFAGVYDTPNVFFCNNNQWAISVPREQQTATDTLAQKAAAYGFEGVQVDGMDPLAVYQVAHDAIEKAKDPDEdemrPT 254
Cdd:PLN02374 243 CLNMAALWKLPIVFVVENNLWAIGMSHLRATSDPEIWKKGPAFGMPGVHVDGMDVLKVREVAKEAIERARRGEG----PT 318
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246444 255 LIEAVQYRFGAHTTAdDPSVYREESEVEAWKDKDPIPRLETFLVETDRLDDAAIESIEADIEDAVADAIEAAEETPRPDP 334
Cdd:PLN02374 319 LVECETYRFRGHSLA-DPDELRDPAEKAHYAARDPIAALKKYLIENGLATEAELKAIEKKIDEVVEDAVEFADASPLPPR 397
                        330
                 ....*....|
gi 501246444 335 ASMFENVYAE 344
Cdd:PLN02374 398 SQLLENVFAD 407
 
Name Accession Description Interval E-value
PDH_E1_alph_x TIGR03181
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the ...
11-356 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: 213783 [Multi-domain]  Cd Length: 341  Bit Score: 537.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246444   11 DTYRVLDENGELVDGAEVPDLTDDELVEMYRYMKLARRFDERAVSLQRQGRIGTYPPLSGQEGAQIASAMALADDDWIVP 90
Cdd:TIGR03181   1 ELVQVLDEDGNVVDPEPAPDLSDEELVELYRDMVLTRRFDTKALALQRQGRLGTYAPNLGQEAAQVGSALALRKDDWVFP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246444   91 SYREHGASLVRGLPLKDTLLYWMGDERGNAIPAEENIFTVAVPIASQIPHATGMGWASQLKDEsDTAFMCYFGDGATSEG 170
Cdd:TIGR03181  81 SYRDHAAMLARGVPLVEILLYWRGDERGSWDPEGVNILPPNIPIGTQYLHAAGVAYALKLRGE-DNVAVTYFGDGGTSEG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246444  171 DFHEGLNFAGVYDTPNVFFCNNNQWAISVPREQQTATDTLAQKAAAYGFEGVQVDGMDPLAVYQVAHDAIEKAKDPDede 250
Cdd:TIGR03181 160 DFYEALNFAGVFKAPVVFFVQNNQWAISVPRSKQTAAPTLAQKAIAYGIPGVQVDGNDVLAVYAVTKEAVERARSGG--- 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246444  251 mRPTLIEAVQYRFGAHTTADDPSVYREESEVEAWKDKDPIPRLETFLVETDRLDDAAIESIEADIEDAVADAIEAAEETP 330
Cdd:TIGR03181 237 -GPTLIEAVTYRLGPHTTADDPTRYRTKEEEEEWRKKDPILRLRKYLERKGLWDEEQEEALEEEAEAEVAEAVAEALALP 315
                         330       340
                  ....*....|....*....|....*.
gi 501246444  331 RPDPASMFENVYAEMPQRLEQQLEYF 356
Cdd:TIGR03181 316 PPPVDDIFDHVYAELPPELEEQRAEL 341
AcoA COG1071
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ...
12-356 8.88e-169

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: 474.63  E-value: 8.88e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246444  12 TYRVLDENGElvdGAEVPDLTDDELVEMYRYMKLARRFDERAVSLQRQGRIGTYPPLSGQEGAQIASAMALADDDWIVPS 91
Cdd:COG1071    1 LVQVLDPDGT---EAALPDLSKEELLELYRDMLLIRRFEERALALQRQGKIGFYHLSIGQEAAQVGAAAALRPGDWIFPT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246444  92 YREHGASLVRGLPLKDTLLYWMGDE----RGNAIP-----AEENIFTVAVPIASQIPHATGMGWASQLKDEsDTAFMCYF 162
Cdd:COG1071   78 YRDHGHALARGVDPKELMAELFGKAtgpsKGRGGSmhffdKELNFLGGSGIVGGQLPHAVGAALAAKLRGE-DEVAVAFF 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246444 163 GDGATSEGDFHEGLNFAGVYDTPNVFFCNNNQWAISVPREQQTATDTLAQKAAAYGFEGVQVDGMDPLAVYQVAHDAIEK 242
Cdd:COG1071  157 GDGATSEGDFHEALNFAAVWKLPVVFVCENNGYAISTPVERQTAVETIADRAAGYGIPGVRVDGNDVLAVYAAVKEAVER 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246444 243 AKDPDedemRPTLIEAVQYRFGAHTTADDPSVYREESEVEAWKDKDPIPRLETFLVETDRLDDAAIESIEADIEDAVADA 322
Cdd:COG1071  237 ARAGE----GPTLIEAKTYRLGGHSTSDDPTRYRTKEEVEEWRERDPIERLRAYLLEEGLLTEEELEAIEAEAKAEVEEA 312
                        330       340       350
                 ....*....|....*....|....*....|....
gi 501246444 323 IEAAEETPRPDPASMFENVYAEMPQRLEQQLEYF 356
Cdd:COG1071  313 VEFAEASPEPDPEELFDDVYAEPPPHLAEQRAEL 346
TPP_E1_PDC_ADC_BCADC cd02000
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ...
39-326 3.23e-133

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: 382.23  E-value: 3.23e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246444  39 MYRYMKLARRFDERAVSLQRQGRI-GTYPPLSGQEGAQIASAMALADDDWIVPSYREHGASLVRGLPLKDTLLYWMGDER 117
Cdd:cd02000    1 LYRTMVLIRRFDERLLELYRQGKIgGFYHLSIGQEAVAVGVAAALRPGDWVFPTYRDHGHALARGVDLKEMLAELFGKET 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246444 118 GNA---------IPAEENIFTVAVPIASQIPHATGMGWASQLKDESDTAFmCYFGDGATSEGDFHEGLNFAGVYDTPNVF 188
Cdd:cd02000   81 GPCkgrggsmhiGDKEKNFFGGNGIVGGQVPLAAGAALALKYRGEDRVAV-CFFGDGATNEGDFHEALNFAALWKLPVIF 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246444 189 FCNNNQWAISVPREQQTATDTLAQKAAAYGFEGVQVDGMDPLAVYQVAHDAIEKAkdpdEDEMRPTLIEAVQYRFGAHTT 268
Cdd:cd02000  160 VCENNGYAISTPTSRQTAGTSIADRAAAYGIPGIRVDGNDVLAVYEAAKEAVERA----RAGGGPTLIEAVTYRLGGHST 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 501246444 269 ADDPSVYREESEVEAWKDKDPIPRLETFLVETDRLDDAAIESIEADIEDAVADAIEAA 326
Cdd:cd02000  236 SDDPSRYRTKEEVEEWKKRDPILRLRKYLIEAGILTEEELAAIEAEVKAEVEEAVEFA 293
E1_dh pfam00676
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ...
40-334 2.20e-91

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: 276.13  E-value: 2.20e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246444   40 YRYMKLARRFDERAVSLQRQGRIGTYPPLSGQEGAQIASAMALADDDWIVPSYREHGASLVRGLPLKDTLLYWMGDE--- 116
Cdd:pfam00676   1 RRMMTLRRMEDARDALYKRQGIRGFYHLYAGQEAAQVGIAAALEPGDYIIPGYRDHGNLLARGLSLEEIFAELYGRVakg 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246444  117 -----RGNAIPAEENIFTVAVPIASQIPHATGMGWASQLKDESDTAFmCYFGDGATSEGDFHEGLNFAGVYDTPNVFFCN 191
Cdd:pfam00676  81 kggsmHGYYGAKGNRFYGGNGILGAQVPLGAGIALAAKYRGKKEVAI-TLYGDGAANQGDFFEGLNFAALWKLPVIFVCE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246444  192 NNQWAISVPREQQTATDTLAQKAAAYGFEGVQVDGMDPLAVYQVAHDAIEKAKDPDedemRPTLIEAVQYRFGAHTTADD 271
Cdd:pfam00676 160 NNQYGISTPAERASASTTYADRARGYGIPGLHVDGMDPLAVYQASKFAAERARTGK----GPFLIELVTYRYGGHSMSDD 235
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501246444  272 PSVYREESEVEA-WKDKDPIPRLETFLVETDRLDDAAIESIEADIEDAVADAIEAAEETPRPDP 334
Cdd:pfam00676 236 PSTYRTRDEYEEvRKKKDPIQRFKEHLVSKGVWSEEELKAIEKEVRKEVEEAFKKAESAPEPHP 299
PLN02374 PLN02374
pyruvate dehydrogenase (acetyl-transferring)
31-344 1.41e-54

pyruvate dehydrogenase (acetyl-transferring)


Pssm-ID: 215213 [Multi-domain]  Cd Length: 433  Bit Score: 185.53  E-value: 1.41e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246444  31 LTDDELVEMYRYMKLARRFDERAVSLQRQGRIGTYPPL-SGQEGAQIASAMALADDDWIVPSYREHGASLVRGLPLKDTL 109
Cdd:PLN02374  83 VTREEGLELYEDMVLGRSFEDMCAQMYYRGKMFGFVHLyNGQEAVSTGFIKLLKKDDSVVSTYRDHVHALSKGVPARAVM 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246444 110 LYWMGDERG---------NAIPAEENIFTVAVPIASQIPHATGMGWASQ-----LKDESDTAFMC-YFGDGATSEGDFHE 174
Cdd:PLN02374 163 SELFGKATGccrgqggsmHMFSKEHNLLGGFAFIGEGIPVATGAAFSSKyrrevLKEESCDDVTLaFFGDGTCNNGQFFE 242
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246444 175 GLNFAGVYDTPNVFFCNNNQWAISVPREQQTATDTLAQKAAAYGFEGVQVDGMDPLAVYQVAHDAIEKAKDPDEdemrPT 254
Cdd:PLN02374 243 CLNMAALWKLPIVFVVENNLWAIGMSHLRATSDPEIWKKGPAFGMPGVHVDGMDVLKVREVAKEAIERARRGEG----PT 318
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246444 255 LIEAVQYRFGAHTTAdDPSVYREESEVEAWKDKDPIPRLETFLVETDRLDDAAIESIEADIEDAVADAIEAAEETPRPDP 334
Cdd:PLN02374 319 LVECETYRFRGHSLA-DPDELRDPAEKAHYAARDPIAALKKYLIENGLATEAELKAIEKKIDEVVEDAVEFADASPLPPR 397
                        330
                 ....*....|
gi 501246444 335 ASMFENVYAE 344
Cdd:PLN02374 398 SQLLENVFAD 407
odpA CHL00149
pyruvate dehydrogenase E1 component alpha subunit; Reviewed
30-344 2.13e-54

pyruvate dehydrogenase E1 component alpha subunit; Reviewed


Pssm-ID: 177069 [Multi-domain]  Cd Length: 341  Bit Score: 182.37  E-value: 2.13e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246444  30 DLTDDELVEMYRYMKLARRFDERAVSLQRQGRIGTYPPL-SGQEGAQIASAMALADDDWIVPSYREHGASLVRGLPLKDT 108
Cdd:CHL00149  16 NINSMWLLVLYEDMLLGRNFEDMCAQMYYRGKMFGFVHLyNGQEAVSTGVIKLLAETDYVCSTYRDHVHALSKGVPPKNV 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246444 109 LLYWMGDE------RGNAI---PAEENIFTVAVPIASQIPHATGMGWAS--------QLKDESDTAfmCYFGDGATSEGD 171
Cdd:CHL00149  96 MAELFGKEtgcsrgRGGSMhifSAPHNFLGGFAFIGEGIPIALGAAFQSiyrqqvlkEVQPLRVTA--CFFGDGTTNNGQ 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246444 172 FHEGLNFAGVYDTPNVFFCNNNQWAISVPREQQTATDTLAQKAAAYGFEGVQVDGMDPLAVYQVAHDAIEKAKDPDEdem 251
Cdd:CHL00149 174 FFECLNMAVLWKLPIIFVVENNQWAIGMAHHRSTSIPEIHKKAEAFGLPGIEVDGMDVLAVREVAKEAVERARQGDG--- 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246444 252 rPTLIEAVQYRFGAHTTAdDPSVYREESEVEAWKDKDPIPRLETFLVETDRLDDAAIESIEADIEDAVADAIEAAEETPR 331
Cdd:CHL00149 251 -PTLIEALTYRFRGHSLA-DPDELRSKQEKEAWVARDPIKKLKSYIIDNELASQKELNKIQREVKIEIEQAVQFAISSPE 328
                        330
                 ....*....|...
gi 501246444 332 PDPASMFENVYAE 344
Cdd:CHL00149 329 PNISDLKKYLFAD 341
PLN02269 PLN02269
Pyruvate dehydrogenase E1 component subunit alpha
32-343 2.54e-42

Pyruvate dehydrogenase E1 component subunit alpha


Pssm-ID: 215152 [Multi-domain]  Cd Length: 362  Bit Score: 151.40  E-value: 2.54e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246444  32 TDDELVEMYRYMKLARRFDERAVSLQRQGRIGTYPPL-SGQEGAQIASAMALADDDWIVPSYREHGASLVRGLPLKDTLL 110
Cdd:PLN02269  28 SKQELVDFFRDMYLMRRMEIAADSLYKAKLIRGFCHLyDGQEAVAVGMEAAITKEDAIITAYRDHCTHLGRGGTVLEVFA 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246444 111 YWMGDERGNAI---------PAEENIFTVAVPIASQIPHATGMGWASQLKDESDTAFMCYfGDGATSEGDFHEGLNFAGV 181
Cdd:PLN02269 108 ELMGRKDGCSRgkggsmhfyKKDANFYGGHGIVGAQVPLGAGLAFAQKYNKEENVAFALY-GDGAANQGQLFEALNIAAL 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246444 182 YDTPNVFFCNNNQWAISvpreqqTATDTLAQKAAAYG----FEGVQVDGMDPLAVYQVAHDAIEKAKdpdedEMRPTLIE 257
Cdd:PLN02269 187 WDLPVIFVCENNHYGMG------TAEWRAAKSPAYYKrgdyVPGLKVDGMDVLAVKQACKFAKEHAL-----SNGPIVLE 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246444 258 AVQYRFGAHTTADDPSVYREESEVEAWK-DKDPIPRLETFLVETDRLDDAAIESIEADIEDAVADAIEAAEETPRPDPAS 336
Cdd:PLN02269 256 MDTYRYHGHSMSDPGSTYRTRDEISGVRqERDPIERVRKLLLAHELATEAELKDIEKEIRKEVDDAVAKAKESPMPDPSE 335

                 ....*..
gi 501246444 337 MFENVYA 343
Cdd:PLN02269 336 LFTNVYV 342
TPP_TK cd02012
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ...
138-258 8.36e-11

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: 61.75  E-value: 8.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246444 138 IPHATGMGWASQLKDESDTAFmCYFGDGATSEGDFHEGLNFAGVYDTPN-VFFCNNNQWAISVPREQQTATDTLAQKAAA 216
Cdd:cd02012  111 LSVAVGMALAEKLLGFDYRVY-VLLGDGELQEGSVWEAASFAGHYKLDNlIAIVDSNRIQIDGPTDDILFTEDLAKKFEA 189
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 501246444 217 YGFEGVQVDGMDPLAVYqvahDAIEKAKdpdEDEMRPTLIEA 258
Cdd:cd02012  190 FGWNVIEVDGHDVEEIL----AALEEAK---KSKGKPTLIIA 224
PRK05899 PRK05899
transketolase; Reviewed
163-258 2.33e-06

transketolase; Reviewed


Pssm-ID: 235639 [Multi-domain]  Cd Length: 586  Bit Score: 49.36  E-value: 2.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246444 163 GDGATSEGDFHEGLNFAGVYDTPN-VFFCNNNQWAISVPREQQTATDTlAQKAAAYGFEGVQVDGMDPLAVYQvahdAIE 241
Cdd:PRK05899 158 GDGDLMEGISHEACSLAGHLKLGNlIVIYDDNRISIDGPTEGWFTEDV-KKRFEAYGWHVIEVDGHDVEAIDA----AIE 232
                         90
                 ....*....|....*..
gi 501246444 242 KAKDPDedemRPTLIEA 258
Cdd:PRK05899 233 EAKAST----KPTLIIA 245
TPP_DXS cd02007
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ...
138-198 5.54e-05

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: 43.69  E-value: 5.54e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501246444 138 IPHATGMGWASQLKDESDTAfMCYFGDGATSEGDFHEGLNFAGVYDTPNVFFCNNNQWAIS 198
Cdd:cd02007   81 ISAALGMAVARDLKGKKRKV-IAVIGDGALTGGMAFEALNNAGYLKSNMIVILNDNEMSIS 140
Transketolase_N pfam00456
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes ...
133-257 2.30e-04

Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes EC:2.2.1.1. and also partially matches to 2-oxoisovalerate dehydrogenase beta subunit EC:1.2.4.4. Both these enzymes utilize thiamine pyrophosphate as a cofactor, suggesting there may be common aspects in their mechanism of catalysis.


Pssm-ID: 395366 [Multi-domain]  Cd Length: 334  Bit Score: 42.76  E-value: 2.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246444  133 PIASQIPHATGMGWASQLK---------DESDTAFMCYFGDGATSEGDFHEGLNFAGVYDTPN-VFFCNNNQWAISVPRE 202
Cdd:pfam00456 113 PLGQGIANAVGMAIAERNLaatynrpgfDIVDHYTYVFLGDGCLMEGVSSEASSLAGHLGLGNlIVFYDDNQISIDGETK 192
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 501246444  203 QQTATDTLAqKAAAYGFEGVQV-DGMDPLAVyqvaHDAIEKAKdpdEDEMRPTLIE 257
Cdd:pfam00456 193 ISFTEDTAA-RFEAYGWHVIEVeDGHDVEAI----AAAIEEAK---AEKDKPTLIK 240
PRK12315 PRK12315
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
138-197 1.83e-03

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


Pssm-ID: 237053 [Multi-domain]  Cd Length: 581  Bit Score: 40.37  E-value: 1.83e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 501246444 138 IPHATGMGWASQLKDESDTaFMCYFGDGATSEGDFHEGLNFAGVYDTPNVFFCNNNQWAI 197
Cdd:PRK12315 119 IALATGLAKARDLKGEKGN-IIAVIGDGSLSGGLALEGLNNAAELKSNLIIIVNDNQMSI 177
 
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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