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Conserved domains on  [gi|1603859121|ref|WP_134360466|]
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pyruvate dehydrogenase (acetyl-transferring) E1 component subunit alpha [Cryobacterium sp. TMT1-3]

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 ...
 8-350 4.09e-168

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: 472.40  E-value: 4.09e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603859121   8 PVQLLSPDGERMpagDFDPwVEDLDGPALLALYRDLVVVRRIDTEATALQRQGELGLWPPLLGQEAAQVGSARALRSDDF 87
Cdd:TIGR03181   2 LVQVLDEDGNVV---DPEP-APDLSDEELVELYRDMVLTRRFDTKALALQRQGRLGTYAPNLGQEAAQVGSALALRKDDW 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603859121  88 VFPSYRENAVAYCRGVNLTDIVTVWRGNAQSGWDPYTVNVATPAIIIGAQTLHATGWALGAQRDDVDSVAITYFGDGATS 167
Cdd:TIGR03181  78 VFPSYRDHAAMLARGVPLVEILLYWRGDERGSWDPEGVNILPPNIPIGTQYLHAAGVAYALKLRGEDNVAVTYFGDGGTS 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603859121 168 EGDVNEAMVFAASFQAPVVFFCQNNHWAISEPVGVQ-AHRNIADRAPGFGIPSLRIDGNDVIAVLAATRIALDRARTGGG 246
Cdd:TIGR03181 158 EGDFYEALNFAGVFKAPVVFFVQNNQWAISVPRSKQtAAPTLAQKAIAYGIPGVQVDGNDVLAVYAVTKEAVERARSGGG 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603859121 247 PTFIEAVTYRMGPHTTADDPTRYRDPAELAEWKTRDPLLRLHRLLTALGEITPEVEAATQALADAAAVELRAGCIGMPDP 326
Cdd:TIGR03181 238 PTLIEAVTYRLGPHTTADDPTRYRTKEEEEEWRKKDPILRLRKYLERKGLWDEEQEEALEEEAEAEVAEAVAEALALPPP 317

                         330       340
                  ....*....|....*....|....
gi 1603859121 327 EPLSVFDHVYATPNATLERQRTDY 350
Cdd:TIGR03181 318 PVDDIFDHVYAELPPELEEQRAEL 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 ...
 8-350 4.09e-168

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: 472.40  E-value: 4.09e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603859121   8 PVQLLSPDGERMpagDFDPwVEDLDGPALLALYRDLVVVRRIDTEATALQRQGELGLWPPLLGQEAAQVGSARALRSDDF 87
Cdd:TIGR03181   2 LVQVLDEDGNVV---DPEP-APDLSDEELVELYRDMVLTRRFDTKALALQRQGRLGTYAPNLGQEAAQVGSALALRKDDW 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603859121  88 VFPSYRENAVAYCRGVNLTDIVTVWRGNAQSGWDPYTVNVATPAIIIGAQTLHATGWALGAQRDDVDSVAITYFGDGATS 167
Cdd:TIGR03181  78 VFPSYRDHAAMLARGVPLVEILLYWRGDERGSWDPEGVNILPPNIPIGTQYLHAAGVAYALKLRGEDNVAVTYFGDGGTS 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603859121 168 EGDVNEAMVFAASFQAPVVFFCQNNHWAISEPVGVQ-AHRNIADRAPGFGIPSLRIDGNDVIAVLAATRIALDRARTGGG 246
Cdd:TIGR03181 158 EGDFYEALNFAGVFKAPVVFFVQNNQWAISVPRSKQtAAPTLAQKAIAYGIPGVQVDGNDVLAVYAVTKEAVERARSGGG 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603859121 247 PTFIEAVTYRMGPHTTADDPTRYRDPAELAEWKTRDPLLRLHRLLTALGEITPEVEAATQALADAAAVELRAGCIGMPDP 326
Cdd:TIGR03181 238 PTLIEAVTYRLGPHTTADDPTRYRTKEEEEEWRKKDPILRLRKYLERKGLWDEEQEEALEEEAEAEVAEAVAEALALPPP 317

                         330       340
                  ....*....|....*....|....
gi 1603859121 327 EPLSVFDHVYATPNATLERQRTDY 350
Cdd:TIGR03181 318 PVDDIFDHVYAELPPELEEQRAEL 341
AcoA COG1071
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ...
 8-352 1.32e-150

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: 428.41  E-value: 1.32e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603859121   8 PVQLLSPDGErmpagdfDPWVEDLDGPALLALYRDLVVVRRIDTEATALQRQGELGLWPPLLGQEAAQVGSARALRSDDF 87
Cdd:COG1071     1 LVQVLDPDGT-------EAALPDLSKEELLELYRDMLLIRRFEERALALQRQGKIGFYHLSIGQEAAQVGAAAALRPGDW 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603859121  88 VFPSYRENAVAYCRGVNLTDIVTVWRGNAQS----GWDPY-----TVNVATPAIIIGAQTLHATGWALGAQRDDVDSVAI 158
Cdd:COG1071    74 IFPTYRDHGHALARGVDPKELMAELFGKATGpskgRGGSMhffdkELNFLGGSGIVGGQLPHAVGAALAAKLRGEDEVAV 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603859121 159 TYFGDGATSEGDVNEAMVFAASFQAPVVFFCQNNHWAISEPVGVQ-AHRNIADRAPGFGIPSLRIDGNDVIAVLAATRIA 237
Cdd:COG1071   154 AFFGDGATSEGDFHEALNFAAVWKLPVVFVCENNGYAISTPVERQtAVETIADRAAGYGIPGVRVDGNDVLAVYAAVKEA 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603859121 238 LDRARTGGGPTFIEAVTYRMGPHTTADDPTRYRDPAELAEWKTRDPLLRLHRLLTALGEITPEVEAATQALADAAAVELR 317
Cdd:COG1071   234 VERARAGEGPTLIEAKTYRLGGHSTSDDPTRYRTKEEVEEWRERDPIERLRAYLLEEGLLTEEELEAIEAEAKAEVEEAV 313

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1603859121 318 AGCIGMPDPEPLSVFDHVYATPNATLERQRTDYAG 352
Cdd:COG1071   314 EFAEASPEPDPEELFDDVYAEPPPHLAEQRAELAA 348
TPP_E1_PDC_ADC_BCADC cd02000
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ...
 39-302 2.07e-115

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: 336.78  E-value: 2.07e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603859121  39 LYRDLVVVRRIDTEATALQRQGEL-GLWPPLLGQEAAQVGSARALRSDDFVFPSYRENAVAYCRGVNLTDIVTVWRGNA- 116
Cdd:cd02000     1 LYRTMVLIRRFDERLLELYRQGKIgGFYHLSIGQEAVAVGVAAALRPGDWVFPTYRDHGHALARGVDLKEMLAELFGKEt 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603859121 117 --QSG------WDPYTVNVATPAIIIGAQTLHATGWALGAQRDDVDSVAITYFGDGATSEGDVNEAMVFAASFQAPVVFF 188
Cdd:cd02000    81 gpCKGrggsmhIGDKEKNFFGGNGIVGGQVPLAAGAALALKYRGEDRVAVCFFGDGATNEGDFHEALNFAALWKLPVIFV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603859121 189 CQNNHWAISEPVGVQ-AHRNIADRAPGFGIPSLRIDGNDVIAVLAATRIALDRARTGGGPTFIEAVTYRMGPHTTADDPT 267
Cdd:cd02000   161 CENNGYAISTPTSRQtAGTSIADRAAAYGIPGIRVDGNDVLAVYEAAKEAVERARAGGGPTLIEAVTYRLGGHSTSDDPS 240

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1603859121 268 RYRDPAELAEWKTRDPLLRLHRLLTALGEITPEVE 302
Cdd:cd02000   241 RYRTKEEVEEWKKRDPILRLRKYLIEAGILTEEEL 275
E1_dh pfam00676
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ...
 41-302 6.96e-87

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: 264.57  E-value: 6.96e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603859121  41 RDLVVVRRIDTEATAL-QRQGELGLWPPLLGQEAAQVGSARALRSDDFVFPSYRENAVAYCRGVNLTDIVTVWRGNAQSG 119
Cdd:pfam00676   1 RRMMTLRRMEDARDALyKRQGIRGFYHLYAGQEAAQVGIAAALEPGDYIIPGYRDHGNLLARGLSLEEIFAELYGRVAKG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603859121 120 --------WDPYTVNVATPAIIIGAQTLHATGWALGAQRDDVDSVAITYFGDGATSEGDVNEAMVFAASFQAPVVFFCQN 191
Cdd:pfam00676  81 kggsmhgyYGAKGNRFYGGNGILGAQVPLGAGIALAAKYRGKKEVAITLYGDGAANQGDFFEGLNFAALWKLPVIFVCEN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603859121 192 NHWAISEPVGVQ-AHRNIADRAPGFGIPSLRIDGNDVIAVLAATRIALDRARTGGGPTFIEAVTYRMGPHTTADDPTRYR 270
Cdd:pfam00676 161 NQYGISTPAERAsASTTYADRARGYGIPGLHVDGMDPLAVYQASKFAAERARTGKGPFLIELVTYRYGGHSMSDDPSTYR 240

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1603859121 271 DPAEL-AEWKTRDPLLRLHRLLTALGEITPEVE 302
Cdd:pfam00676 241 TRDEYeEVRKKKDPIQRFKEHLVSKGVWSEEEL 273
PLN02374 PLN02374
pyruvate dehydrogenase (acetyl-transferring)
 37-339 4.28e-34

pyruvate dehydrogenase (acetyl-transferring)


Pssm-ID: 215213 [Multi-domain]  Cd Length: 433  Bit Score: 130.45  E-value: 4.28e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603859121  37 LALYRDLVVVRRIDTEATALQRQGEL-GLWPPLLGQEAAQVGSARALRSDDFVFPSYRENAVAYCRGVNLTDIVTVWRGN 115
Cdd:PLN02374   89 LELYEDMVLGRSFEDMCAQMYYRGKMfGFVHLYNGQEAVSTGFIKLLKKDDSVVSTYRDHVHALSKGVPARAVMSELFGK 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603859121 116 A------QSGW-----DPYtvNVATPAIIIGAQTLHATGWALGAQ-------RDDVDSVAITYFGDGATSEGDVNEAMVF 177
Cdd:PLN02374  169 AtgccrgQGGSmhmfsKEH--NLLGGFAFIGEGIPVATGAAFSSKyrrevlkEESCDDVTLAFFGDGTCNNGQFFECLNM 246

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603859121 178 AASFQAPVVFFCQNNHWAIS-EPVGVQAHRNIADRAPGFGIPSLRIDGNDVIAVLAATRIALDRARTGGGPTFIEAVTYR 256
Cdd:PLN02374  247 AALWKLPIVFVVENNLWAIGmSHLRATSDPEIWKKGPAFGMPGVHVDGMDVLKVREVAKEAIERARRGEGPTLVECETYR 326

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603859121 257 MGPHTTAdDPTRYRDPAELAEWKTRDPLLRLHRLLTAlGEITPEVEAATQALADAAAVElraGCIGMPDPEPL----SVF 332
Cdd:PLN02374  327 FRGHSLA-DPDELRDPAEKAHYAARDPIAALKKYLIE-NGLATEAELKAIEKKIDEVVE---DAVEFADASPLpprsQLL 401


                  ....*..
gi 1603859121 333 DHVYATP 339
Cdd:PLN02374  402 ENVFADP 408
 
Name Accession Description Interval E-value
PDH_E1_alph_x TIGR03181
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the ...
 8-350 4.09e-168

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: 472.40  E-value: 4.09e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603859121   8 PVQLLSPDGERMpagDFDPwVEDLDGPALLALYRDLVVVRRIDTEATALQRQGELGLWPPLLGQEAAQVGSARALRSDDF 87
Cdd:TIGR03181   2 LVQVLDEDGNVV---DPEP-APDLSDEELVELYRDMVLTRRFDTKALALQRQGRLGTYAPNLGQEAAQVGSALALRKDDW 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603859121  88 VFPSYRENAVAYCRGVNLTDIVTVWRGNAQSGWDPYTVNVATPAIIIGAQTLHATGWALGAQRDDVDSVAITYFGDGATS 167
Cdd:TIGR03181  78 VFPSYRDHAAMLARGVPLVEILLYWRGDERGSWDPEGVNILPPNIPIGTQYLHAAGVAYALKLRGEDNVAVTYFGDGGTS 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603859121 168 EGDVNEAMVFAASFQAPVVFFCQNNHWAISEPVGVQ-AHRNIADRAPGFGIPSLRIDGNDVIAVLAATRIALDRARTGGG 246
Cdd:TIGR03181 158 EGDFYEALNFAGVFKAPVVFFVQNNQWAISVPRSKQtAAPTLAQKAIAYGIPGVQVDGNDVLAVYAVTKEAVERARSGGG 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603859121 247 PTFIEAVTYRMGPHTTADDPTRYRDPAELAEWKTRDPLLRLHRLLTALGEITPEVEAATQALADAAAVELRAGCIGMPDP 326
Cdd:TIGR03181 238 PTLIEAVTYRLGPHTTADDPTRYRTKEEEEEWRKKDPILRLRKYLERKGLWDEEQEEALEEEAEAEVAEAVAEALALPPP 317

                         330       340
                  ....*....|....*....|....
gi 1603859121 327 EPLSVFDHVYATPNATLERQRTDY 350
Cdd:TIGR03181 318 PVDDIFDHVYAELPPELEEQRAEL 341
AcoA COG1071
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ...
 8-352 1.32e-150

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: 428.41  E-value: 1.32e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603859121   8 PVQLLSPDGErmpagdfDPWVEDLDGPALLALYRDLVVVRRIDTEATALQRQGELGLWPPLLGQEAAQVGSARALRSDDF 87
Cdd:COG1071     1 LVQVLDPDGT-------EAALPDLSKEELLELYRDMLLIRRFEERALALQRQGKIGFYHLSIGQEAAQVGAAAALRPGDW 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603859121  88 VFPSYRENAVAYCRGVNLTDIVTVWRGNAQS----GWDPY-----TVNVATPAIIIGAQTLHATGWALGAQRDDVDSVAI 158
Cdd:COG1071    74 IFPTYRDHGHALARGVDPKELMAELFGKATGpskgRGGSMhffdkELNFLGGSGIVGGQLPHAVGAALAAKLRGEDEVAV 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603859121 159 TYFGDGATSEGDVNEAMVFAASFQAPVVFFCQNNHWAISEPVGVQ-AHRNIADRAPGFGIPSLRIDGNDVIAVLAATRIA 237
Cdd:COG1071   154 AFFGDGATSEGDFHEALNFAAVWKLPVVFVCENNGYAISTPVERQtAVETIADRAAGYGIPGVRVDGNDVLAVYAAVKEA 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603859121 238 LDRARTGGGPTFIEAVTYRMGPHTTADDPTRYRDPAELAEWKTRDPLLRLHRLLTALGEITPEVEAATQALADAAAVELR 317
Cdd:COG1071   234 VERARAGEGPTLIEAKTYRLGGHSTSDDPTRYRTKEEVEEWRERDPIERLRAYLLEEGLLTEEELEAIEAEAKAEVEEAV 313

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1603859121 318 AGCIGMPDPEPLSVFDHVYATPNATLERQRTDYAG 352
Cdd:COG1071   314 EFAEASPEPDPEELFDDVYAEPPPHLAEQRAELAA 348
TPP_E1_PDC_ADC_BCADC cd02000
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ...
 39-302 2.07e-115

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: 336.78  E-value: 2.07e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603859121  39 LYRDLVVVRRIDTEATALQRQGEL-GLWPPLLGQEAAQVGSARALRSDDFVFPSYRENAVAYCRGVNLTDIVTVWRGNA- 116
Cdd:cd02000     1 LYRTMVLIRRFDERLLELYRQGKIgGFYHLSIGQEAVAVGVAAALRPGDWVFPTYRDHGHALARGVDLKEMLAELFGKEt 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603859121 117 --QSG------WDPYTVNVATPAIIIGAQTLHATGWALGAQRDDVDSVAITYFGDGATSEGDVNEAMVFAASFQAPVVFF 188
Cdd:cd02000    81 gpCKGrggsmhIGDKEKNFFGGNGIVGGQVPLAAGAALALKYRGEDRVAVCFFGDGATNEGDFHEALNFAALWKLPVIFV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603859121 189 CQNNHWAISEPVGVQ-AHRNIADRAPGFGIPSLRIDGNDVIAVLAATRIALDRARTGGGPTFIEAVTYRMGPHTTADDPT 267
Cdd:cd02000   161 CENNGYAISTPTSRQtAGTSIADRAAAYGIPGIRVDGNDVLAVYEAAKEAVERARAGGGPTLIEAVTYRLGGHSTSDDPS 240

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1603859121 268 RYRDPAELAEWKTRDPLLRLHRLLTALGEITPEVE 302
Cdd:cd02000   241 RYRTKEEVEEWKKRDPILRLRKYLIEAGILTEEEL 275
E1_dh pfam00676
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ...
 41-302 6.96e-87

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: 264.57  E-value: 6.96e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603859121  41 RDLVVVRRIDTEATAL-QRQGELGLWPPLLGQEAAQVGSARALRSDDFVFPSYRENAVAYCRGVNLTDIVTVWRGNAQSG 119
Cdd:pfam00676   1 RRMMTLRRMEDARDALyKRQGIRGFYHLYAGQEAAQVGIAAALEPGDYIIPGYRDHGNLLARGLSLEEIFAELYGRVAKG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603859121 120 --------WDPYTVNVATPAIIIGAQTLHATGWALGAQRDDVDSVAITYFGDGATSEGDVNEAMVFAASFQAPVVFFCQN 191
Cdd:pfam00676  81 kggsmhgyYGAKGNRFYGGNGILGAQVPLGAGIALAAKYRGKKEVAITLYGDGAANQGDFFEGLNFAALWKLPVIFVCEN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603859121 192 NHWAISEPVGVQ-AHRNIADRAPGFGIPSLRIDGNDVIAVLAATRIALDRARTGGGPTFIEAVTYRMGPHTTADDPTRYR 270
Cdd:pfam00676 161 NQYGISTPAERAsASTTYADRARGYGIPGLHVDGMDPLAVYQASKFAAERARTGKGPFLIELVTYRYGGHSMSDDPSTYR 240

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1603859121 271 DPAEL-AEWKTRDPLLRLHRLLTALGEITPEVE 302
Cdd:pfam00676 241 TRDEYeEVRKKKDPIQRFKEHLVSKGVWSEEEL 273
PLN02374 PLN02374
pyruvate dehydrogenase (acetyl-transferring)
 37-339 4.28e-34

pyruvate dehydrogenase (acetyl-transferring)


Pssm-ID: 215213 [Multi-domain]  Cd Length: 433  Bit Score: 130.45  E-value: 4.28e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603859121  37 LALYRDLVVVRRIDTEATALQRQGEL-GLWPPLLGQEAAQVGSARALRSDDFVFPSYRENAVAYCRGVNLTDIVTVWRGN 115
Cdd:PLN02374   89 LELYEDMVLGRSFEDMCAQMYYRGKMfGFVHLYNGQEAVSTGFIKLLKKDDSVVSTYRDHVHALSKGVPARAVMSELFGK 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603859121 116 A------QSGW-----DPYtvNVATPAIIIGAQTLHATGWALGAQ-------RDDVDSVAITYFGDGATSEGDVNEAMVF 177
Cdd:PLN02374  169 AtgccrgQGGSmhmfsKEH--NLLGGFAFIGEGIPVATGAAFSSKyrrevlkEESCDDVTLAFFGDGTCNNGQFFECLNM 246

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603859121 178 AASFQAPVVFFCQNNHWAIS-EPVGVQAHRNIADRAPGFGIPSLRIDGNDVIAVLAATRIALDRARTGGGPTFIEAVTYR 256
Cdd:PLN02374  247 AALWKLPIVFVVENNLWAIGmSHLRATSDPEIWKKGPAFGMPGVHVDGMDVLKVREVAKEAIERARRGEGPTLVECETYR 326

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603859121 257 MGPHTTAdDPTRYRDPAELAEWKTRDPLLRLHRLLTAlGEITPEVEAATQALADAAAVElraGCIGMPDPEPL----SVF 332
Cdd:PLN02374  327 FRGHSLA-DPDELRDPAEKAHYAARDPIAALKKYLIE-NGLATEAELKAIEKKIDEVVE---DAVEFADASPLpprsQLL 401


                  ....*..
gi 1603859121 333 DHVYATP 339
Cdd:PLN02374  402 ENVFADP 408
odpA CHL00149
pyruvate dehydrogenase E1 component alpha subunit; Reviewed
 36-287 1.01e-33

pyruvate dehydrogenase E1 component alpha subunit; Reviewed


Pssm-ID: 177069 [Multi-domain]  Cd Length: 341  Bit Score: 127.67  E-value: 1.01e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603859121  36 LLALYRDLVVVRRIDTEATALQRQGEL-GLWPPLLGQEAAQVGSARALRSDDFVFPSYRENAVAYCRGVNLTDIVTVWRG 114
Cdd:CHL00149   22 LLVLYEDMLLGRNFEDMCAQMYYRGKMfGFVHLYNGQEAVSTGVIKLLAETDYVCSTYRDHVHALSKGVPPKNVMAELFG 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603859121 115 N---AQSGWDPYTVNVATPAIIIGAQTLHATGW--ALGAQRDDVDS-----------VAITYFGDGATSEGDVNEAMVFA 178
Cdd:CHL00149  102 KetgCSRGRGGSMHIFSAPHNFLGGFAFIGEGIpiALGAAFQSIYRqqvlkevqplrVTACFFGDGTTNNGQFFECLNMA 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603859121 179 ASFQAPVVFFCQNNHWAIsepvGVQAHRN-----IADRAPGFGIPSLRIDGNDVIAVLAATRIALDRARTGGGPTFIEAV 253
Cdd:CHL00149  182 VLWKLPIIFVVENNQWAI----GMAHHRStsipeIHKKAEAFGLPGIEVDGMDVLAVREVAKEAVERARQGDGPTLIEAL 257

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1603859121 254 TYRMGPHTTAdDPTRYRDPAELAEWKTRDPLLRL 287
Cdd:CHL00149  258 TYRFRGHSLA-DPDELRSKQEKEAWVARDPIKKL 290
PLN02269 PLN02269
Pyruvate dehydrogenase E1 component subunit alpha
 36-339 7.61e-30

Pyruvate dehydrogenase E1 component subunit alpha


Pssm-ID: 215152 [Multi-domain]  Cd Length: 362  Bit Score: 117.51  E-value: 7.61e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603859121  36 LLALYRDLVVVRRIDTEATALQR----QGELGLWPpllGQEAAQVGSARALRSDDFVFPSYRENAVAYCRGVNLTDIVTV 111
Cdd:PLN02269   32 LVDFFRDMYLMRRMEIAADSLYKakliRGFCHLYD---GQEAVAVGMEAAITKEDAIITAYRDHCTHLGRGGTVLEVFAE 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603859121 112 WRG--------------------NAQSGWDpytvnvatpaiIIGAQTLHATGWALGAQRDDVDSVAITYFGDGATSEGDV 171
Cdd:PLN02269  109 LMGrkdgcsrgkggsmhfykkdaNFYGGHG-----------IVGAQVPLGAGLAFAQKYNKEENVAFALYGDGAANQGQL 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603859121 172 NEAMVFAASFQAPVVFFCQNNHWAIsepvGVQAHRniADRAP-----GFGIPSLRIDGNDVIAVLAATRIALDRARTgGG 246
Cdd:PLN02269  178 FEALNIAALWDLPVIFVCENNHYGM----GTAEWR--AAKSPayykrGDYVPGLKVDGMDVLAVKQACKFAKEHALS-NG 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603859121 247 PTFIEAVTYRMGPHTTADDPTRYRDPAELAEWK-TRDPLLRLHRLLTAlGEITPEVEAATQALADAAAVE---LRAGCIG 322
Cdd:PLN02269  251 PIVLEMDTYRYHGHSMSDPGSTYRTRDEISGVRqERDPIERVRKLLLA-HELATEAELKDIEKEIRKEVDdavAKAKESP 329

                         330
                  ....*....|....*..
gi 1603859121 323 MPDPEPLsvFDHVYATP 339
Cdd:PLN02269  330 MPDPSEL--FTNVYVKG 344
TPP_TK cd02012
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ...
 141-254 2.36e-10

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: 60.21  E-value: 2.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603859121 141 ATGWALGAQRDDVDSVAITYFGDGATSEGDVNEAMVFAASFQ-APVVFFCQNNHWAISEPVGVQAH-RNIADRAPGFGIP 218
Cdd:cd02012   114 AVGMALAEKLLGFDYRVYVLLGDGELQEGSVWEAASFAGHYKlDNLIAIVDSNRIQIDGPTDDILFtEDLAKKFEAFGWN 193

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1603859121 219 SLRIDGNDVIAVLAatriALDRARTGGG-PTFIEAVT 254
Cdd:cd02012   194 VIEVDGHDVEEILA----ALEEAKKSKGkPTLIIAKT 226
TPP_enzymes cd00568
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ...
 140-254 6.11e-06

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.


Pssm-ID: 238318 [Multi-domain]  Cd Length: 168  Bit Score: 46.09  E-value: 6.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603859121 140 HATGWALGAQRDDVDSVAITYFGDGATSEGdVNEAMVfAASFQAPVVFFCQNNH-----------WAISEPVGVQAHR-N 207
Cdd:cd00568    50 YGLPAAIGAALAAPDRPVVCIAGDGGFMMT-GQELAT-AVRYGLPVIVVVFNNGgygtirmhqeaFYGGRVSGTDLSNpD 127

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1603859121 208 IADRAPGFGIPSLRIDGndvIAVLAAtriALDRARTGGGPTFIEAVT 254
Cdd:cd00568   128 FAALAEAYGAKGVRVED---PEDLEA---ALAEALAAGGPALIEVKT 168
TPP_DXS cd02007
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ...
 141-254 1.06e-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: 45.62  E-value: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603859121 141 ATGWALGAQRDDVDSVAITYFGDGATSEGDVNEAMVFAASFQAPVVFFCQNNHWAISEPVGVQAhrNIADrapGFGI--- 217
Cdd:cd02007    84 ALGMAVARDLKGKKRKVIAVIGDGALTGGMAFEALNNAGYLKSNMIVILNDNEMSISPNVGTPG--NLFE---ELGFryi 158

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1603859121 218 -PslrIDGNDVIAVLAatriALDRARTGGGPTFIEAVT 254
Cdd:cd02007   159 gP---VDGHNIEALIK----VLKEVKDLKGPVLLHVVT 189
PRK05899 PRK05899
transketolase; Reviewed
 162-254 1.36e-05

transketolase; Reviewed


Pssm-ID: 235639 [Multi-domain]  Cd Length: 586  Bit Score: 47.05  E-value: 1.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603859121 162 GDGATSEGDVNEAMVFAASFQ-APVVFFCQNNHWAISEPVGVQAHRNIADRAPGFGIPSLRIDGNDVIAVLAatriALDR 240
Cdd:PRK05899  158 GDGDLMEGISHEACSLAGHLKlGNLIVIYDDNRISIDGPTEGWFTEDVKKRFEAYGWHVIEVDGHDVEAIDA----AIEE 233

                          90
                  ....*....|....
gi 1603859121 241 ARTGGGPTFIEAVT 254
Cdd:PRK05899  234 AKASTKPTLIIAKT 247
TPP_E1_OGDC_like cd02016
Thiamine pyrophosphate (TPP) family, E1 of OGDC-like subfamily, TPP-binding module; composed ...
 210-267 7.71e-04

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: 40.59  E-value: 7.71e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1603859121 210 DRAPGFGIPSLRIDGNDVIAVLAATRIALDRARTGGGPTFIEAVTYRMGPHTTADDPT 267
Cdd:cd02016   201 DVAKMIGAPIFHVNGDDPEAVVRATRLALEYRQKFKKDVVIDLVCYRRHGHNELDEPS 258
TPP_enzyme_C pfam02775
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
143-252 4.86e-03

Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;


Pssm-ID: 460689 [Multi-domain]  Cd Length: 151  Bit Score: 37.18  E-value: 4.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603859121 143 GWALGAQRDDVDSVAITYFGDGATseGDVNEAMVFAASFQAPVVFFCQNNHW--------------AISEPVGVQAHR-N 207
Cdd:pfam02775  35 PAAIGAKLARPDRPVVAIAGDGGF--QMNLQELATAVRYNLPITVVVLNNGGygmtrgqqtpfgggRYSGPSGKILPPvD 112

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1603859121 208 IADRAPGFGIPSLRID-GNDVIAvlaatriALDRARTGGGPTFIEA 252
Cdd:pfam02775 113 FAKLAEAYGAKGARVEsPEELEE-------ALKEALEHDGPALIDV 151
PRK12571 PRK12571
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
 143-251 8.67e-03

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


Pssm-ID: 183601 [Multi-domain]  Cd Length: 641  Bit Score: 38.17  E-value: 8.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1603859121 143 GWALG-------AQRDDvDSVAItyFGDGATSEGDVNEAMVFAASFQAPVVFFCQNNHWAISEPVGVQAHrNIADRAPGF 215
Cdd:PRK12571  126 SAALGfakaralGQPDG-DVVAV--IGDGSLTAGMAYEALNNAGAADRRLIVILNDNEMSIAPPVGALAA-YLSTLRSSD 201

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1603859121 216 GIPSLRIDGNDVIAVL-AATRIALDRARTG-----GGPTFIE 251
Cdd:PRK12571  202 PFARLRAIAKGVEERLpGPLRDGARRARELvtgmiGGGTLFE 243
 
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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