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Conserved domains on  [gi|258645172|ref|NP_001158255|]
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2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial isoform 2 precursor [Homo sapiens]

Protein Classification

thiamine pyrophosphate-dependent dehydrogenase E1 component subunit alpha( domain architecture ID 10787196)

thiamine pyrophosphate-dependent dehydrogenase E1 component subunit alpha is part of the E1 component of a multi-enzyme dehydrogenase complex such as branched-chain alpha-keto acid dehydrogenase, which catalyzes the multi-step oxidative decarboxylation of alpha-keto acids derived from the branched-chain amino-acids valine, leucine, and isoleucine

CATH:  3.40.50.970
EC:  1.2.4.-
Gene Ontology:  GO:0016624|GO:0030976
SCOP:  3001790

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AcoA COG1071
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ...
80-428 6.23e-148

TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and conversion]; TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha is part of the Pathway/BioSystem: Pyruvate oxidation


:

Pssm-ID: 440689 [Multi-domain]  Cd Length: 348  Bit Score: 424.55  E-value: 6.23e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258645172  80 RVMDRQGqiiNPSEDPHLPKEKVLKLYKSMTLLNTMDRILYESQRQGRISFYMTNYGEEGTHVGSAAALDNTDLVFGQYR 159
Cdd:COG1071    3 QVLDPDG---TEAALPDLSKEELLELYRDMLLIRRFEERALALQRQGKIGFYHLSIGQEAAQVGAAAALRPGDWIFPTYR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258645172 160 EAGVLMYRDYPLELFMAQCYGNISDLGKGRQMPVHYGCKERHFVTISSPLATQIPQAVGAAYAAKRANANRVVICYFGEG 239
Cdd:COG1071   80 DHGHALARGVDPKELMAELFGKATGPSKGRGGSMHFFDKELNFLGGSGIVGGQLPHAVGAALAAKLRGEDEVAVAFFGDG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258645172 240 AASEGDAHAGFNFAATLECPIIFFCRNNGYAISTPTSEQYRGDGIA-RGPGYGIMSIRVDGNDVFAVYNATKEARRRAVA 318
Cdd:COG1071  160 ATSEGDFHEALNFAAVWKLPVVFVCENNGYAISTPVERQTAVETIAdRAAGYGIPGVRVDGNDVLAVYAAVKEAVERARA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258645172 319 ENQPFLIEAMTYRIGHHSTSDDSSAYRSVDEVNYWDKQDhPISRLRHYLLSQGWWDEEQEKAWRKQSRRKVMEAFEQAER 398
Cdd:COG1071  240 GEGPTLIEAKTYRLGGHSTSDDPTRYRTKEEVEEWRERD-PIERLRAYLLEEGLLTEEELEAIEAEAKAEVEEAVEFAEA 318
                        330       340       350
                 ....*....|....*....|....*....|
gi 258645172 399 KPKPNPNLLFSDVYQEMPAQLRKQQESLAR 428
Cdd:COG1071  319 SPEPDPEELFDDVYAEPPPHLAEQRAELAA 348
 
Name Accession Description Interval E-value
AcoA COG1071
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ...
80-428 6.23e-148

TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and conversion]; TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 440689 [Multi-domain]  Cd Length: 348  Bit Score: 424.55  E-value: 6.23e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258645172  80 RVMDRQGqiiNPSEDPHLPKEKVLKLYKSMTLLNTMDRILYESQRQGRISFYMTNYGEEGTHVGSAAALDNTDLVFGQYR 159
Cdd:COG1071    3 QVLDPDG---TEAALPDLSKEELLELYRDMLLIRRFEERALALQRQGKIGFYHLSIGQEAAQVGAAAALRPGDWIFPTYR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258645172 160 EAGVLMYRDYPLELFMAQCYGNISDLGKGRQMPVHYGCKERHFVTISSPLATQIPQAVGAAYAAKRANANRVVICYFGEG 239
Cdd:COG1071   80 DHGHALARGVDPKELMAELFGKATGPSKGRGGSMHFFDKELNFLGGSGIVGGQLPHAVGAALAAKLRGEDEVAVAFFGDG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258645172 240 AASEGDAHAGFNFAATLECPIIFFCRNNGYAISTPTSEQYRGDGIA-RGPGYGIMSIRVDGNDVFAVYNATKEARRRAVA 318
Cdd:COG1071  160 ATSEGDFHEALNFAAVWKLPVVFVCENNGYAISTPVERQTAVETIAdRAAGYGIPGVRVDGNDVLAVYAAVKEAVERARA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258645172 319 ENQPFLIEAMTYRIGHHSTSDDSSAYRSVDEVNYWDKQDhPISRLRHYLLSQGWWDEEQEKAWRKQSRRKVMEAFEQAER 398
Cdd:COG1071  240 GEGPTLIEAKTYRLGGHSTSDDPTRYRTKEEVEEWRERD-PIERLRAYLLEEGLLTEEELEAIEAEAKAEVEEAVEFAEA 318
                        330       340       350
                 ....*....|....*....|....*....|
gi 258645172 399 KPKPNPNLLFSDVYQEMPAQLRKQQESLAR 428
Cdd:COG1071  319 SPEPDPEELFDDVYAEPPPHLAEQRAELAA 348
TPP_E1_PDC_ADC_BCADC cd02000
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ...
105-396 1.55e-145

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: 416.51  E-value: 1.55e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258645172 105 LYKSMTLLNTMDRILYESQRQGRIS-FYMTNYGEEGTHVGSAAALDNTDLVFGQYREAGVLMYRDYPLELFMAQCYGNIS 183
Cdd:cd02000    1 LYRTMVLIRRFDERLLELYRQGKIGgFYHLSIGQEAVAVGVAAALRPGDWVFPTYRDHGHALARGVDLKEMLAELFGKET 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258645172 184 DLGKGRQMPVHYGCKERHFVTISSPLATQIPQAVGAAYAAKRANANRVVICYFGEGAASEGDAHAGFNFAATLECPIIFF 263
Cdd:cd02000   81 GPCKGRGGSMHIGDKEKNFFGGNGIVGGQVPLAAGAALALKYRGEDRVAVCFFGDGATNEGDFHEALNFAALWKLPVIFV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258645172 264 CRNNGYAISTPTSEQYRGDGIA-RGPGYGIMSIRVDGNDVFAVYNATKEARRRAVAENQPFLIEAMTYRIGHHSTSDDSS 342
Cdd:cd02000  161 CENNGYAISTPTSRQTAGTSIAdRAAAYGIPGIRVDGNDVLAVYEAAKEAVERARAGGGPTLIEAVTYRLGGHSTSDDPS 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 258645172 343 AYRSVDEVNYWDKQDhPISRLRHYLLSQGWWDEEQEKAWRKQSRRKVMEAFEQA 396
Cdd:cd02000  241 RYRTKEEVEEWKKRD-PILRLRKYLIEAGILTEEELAAIEAEVKAEVEEAVEFA 293
E1_dh pfam00676
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ...
106-404 2.91e-137

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: 395.93  E-value: 2.91e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258645172  106 YKSMTLLNTMDRILYESQRQGRISFYMTNYGEEGTHVGSAAALDNTDLVFGQYREAGVLMYRDYPLELFMAQCYGNISDl 185
Cdd:pfam00676   1 RRMMTLRRMEDARDALYKRQGIRGFYHLYAGQEAAQVGIAAALEPGDYIIPGYRDHGNLLARGLSLEEIFAELYGRVAK- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258645172  186 GKGRQMPVHYGCKERHFVTISSPLATQIPQAVGAAYAAKRANANRVVICYFGEGAASEGDAHAGFNFAATLECPIIFFCR 265
Cdd:pfam00676  80 GKGGSMHGYYGAKGNRFYGGNGILGAQVPLGAGIALAAKYRGKKEVAITLYGDGAANQGDFFEGLNFAALWKLPVIFVCE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258645172  266 NNGYAISTPTSEQYRGDGIA-RGPGYGIMSIRVDGNDVFAVYNATKEARRRAVAENQPFLIEAMTYRIGHHSTSDDSSAY 344
Cdd:pfam00676 160 NNQYGISTPAERASASTTYAdRARGYGIPGLHVDGMDPLAVYQASKFAAERARTGKGPFLIELVTYRYGGHSMSDDPSTY 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 258645172  345 RSVDEVNYWDKQDHPISRLRHYLLSQGWWDEEQEKAWRKQSRRKVMEAFEQAERKPKPNP 404
Cdd:pfam00676 240 RTRDEYEEVRKKKDPIQRFKEHLVSKGVWSEEELKAIEKEVRKEVEEAFKKAESAPEPHP 299
PDH_E1_alph_x TIGR03181
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the ...
77-426 1.51e-120

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: 354.91  E-value: 1.51e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258645172   77 PIYRVMDRQGQIINPSEDPHLPKEKVLKLYKSMTLLNTMDRILYESQRQGRISFYMTNYGEEGTHVGSAAALDNTDLVFG 156
Cdd:TIGR03181   1 ELVQVLDEDGNVVDPEPAPDLSDEELVELYRDMVLTRRFDTKALALQRQGRLGTYAPNLGQEAAQVGSALALRKDDWVFP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258645172  157 QYREAGVLMYRDYPLELFMAQCYGNIsdlgKGRQMPVhygckERHFVTISSPLATQIPQAVGAAYAAKRANANRVVICYF 236
Cdd:TIGR03181  81 SYRDHAAMLARGVPLVEILLYWRGDE----RGSWDPE-----GVNILPPNIPIGTQYLHAAGVAYALKLRGEDNVAVTYF 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258645172  237 GEGAASEGDAHAGFNFAATLECPIIFFCRNNGYAISTPTSEQYRGDGIA-RGPGYGIMSIRVDGNDVFAVYNATKEARRR 315
Cdd:TIGR03181 152 GDGGTSEGDFYEALNFAGVFKAPVVFFVQNNQWAISVPRSKQTAAPTLAqKAIAYGIPGVQVDGNDVLAVYAVTKEAVER 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258645172  316 AVAENQPFLIEAMTYRIGHHSTSDDSSAYRSVDEVNYWDKQDhPISRLRHYLLSQGWWDEEQEKAWRKQSRRKVMEAFEQ 395
Cdd:TIGR03181 232 ARSGGGPTLIEAVTYRLGPHTTADDPTRYRTKEEEEEWRKKD-PILRLRKYLERKGLWDEEQEEALEEEAEAEVAEAVAE 310
                         330       340       350
                  ....*....|....*....|....*....|.
gi 258645172  396 AERKPKPNPNLLFSDVYQEMPAQLRKQQESL 426
Cdd:TIGR03181 311 ALALPPPPVDDIFDHVYAELPPELEEQRAEL 341
PLN02269 PLN02269
Pyruvate dehydrogenase E1 component subunit alpha
91-413 2.60e-42

Pyruvate dehydrogenase E1 component subunit alpha


Pssm-ID: 215152 [Multi-domain]  Cd Length: 362  Bit Score: 152.95  E-value: 2.60e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258645172  91 PSEDPHLPKEKVLKLYKSMTLLNTMD---RILYESQR-QGRISFYMtnyGEEGTHVGSAAALDNTDLVFGQYREAGVLMY 166
Cdd:PLN02269  21 PSRTVETSKQELVDFFRDMYLMRRMEiaaDSLYKAKLiRGFCHLYD---GQEAVAVGMEAAITKEDAIITAYRDHCTHLG 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258645172 167 RD-YPLELFmAQCYGNIS--DLGKGRQMpvHYGCKERHFVTISSPLATQIPQAVGAAYAAKRANANRVVICYFGEGAASE 243
Cdd:PLN02269  98 RGgTVLEVF-AELMGRKDgcSRGKGGSM--HFYKKDANFYGGHGIVGAQVPLGAGLAFAQKYNKEENVAFALYGDGAANQ 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258645172 244 GDAHAGFNFAATLECPIIFFCRNNGYAISTPT------SEQY-RGDGIargPGygimsIRVDGNDVFAVYNATKEARRRA 316
Cdd:PLN02269 175 GQLFEALNIAALWDLPVIFVCENNHYGMGTAEwraaksPAYYkRGDYV---PG-----LKVDGMDVLAVKQACKFAKEHA 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258645172 317 VAeNQPFLIEAMTYRIGHHSTSDDSSAYRSVDEVNYWDKQDHPISRLRHYLLSQGWWDEEQEKAWRKQSRRKVMEAFEQA 396
Cdd:PLN02269 247 LS-NGPIVLEMDTYRYHGHSMSDPGSTYRTRDEISGVRQERDPIERVRKLLLAHELATEAELKDIEKEIRKEVDDAVAKA 325
                        330
                 ....*....|....*..
gi 258645172 397 ERKPKPNPNLLFSDVYQ 413
Cdd:PLN02269 326 KESPMPDPSELFTNVYV 342
 
Name Accession Description Interval E-value
AcoA COG1071
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ...
80-428 6.23e-148

TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and conversion]; TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 440689 [Multi-domain]  Cd Length: 348  Bit Score: 424.55  E-value: 6.23e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258645172  80 RVMDRQGqiiNPSEDPHLPKEKVLKLYKSMTLLNTMDRILYESQRQGRISFYMTNYGEEGTHVGSAAALDNTDLVFGQYR 159
Cdd:COG1071    3 QVLDPDG---TEAALPDLSKEELLELYRDMLLIRRFEERALALQRQGKIGFYHLSIGQEAAQVGAAAALRPGDWIFPTYR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258645172 160 EAGVLMYRDYPLELFMAQCYGNISDLGKGRQMPVHYGCKERHFVTISSPLATQIPQAVGAAYAAKRANANRVVICYFGEG 239
Cdd:COG1071   80 DHGHALARGVDPKELMAELFGKATGPSKGRGGSMHFFDKELNFLGGSGIVGGQLPHAVGAALAAKLRGEDEVAVAFFGDG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258645172 240 AASEGDAHAGFNFAATLECPIIFFCRNNGYAISTPTSEQYRGDGIA-RGPGYGIMSIRVDGNDVFAVYNATKEARRRAVA 318
Cdd:COG1071  160 ATSEGDFHEALNFAAVWKLPVVFVCENNGYAISTPVERQTAVETIAdRAAGYGIPGVRVDGNDVLAVYAAVKEAVERARA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258645172 319 ENQPFLIEAMTYRIGHHSTSDDSSAYRSVDEVNYWDKQDhPISRLRHYLLSQGWWDEEQEKAWRKQSRRKVMEAFEQAER 398
Cdd:COG1071  240 GEGPTLIEAKTYRLGGHSTSDDPTRYRTKEEVEEWRERD-PIERLRAYLLEEGLLTEEELEAIEAEAKAEVEEAVEFAEA 318
                        330       340       350
                 ....*....|....*....|....*....|
gi 258645172 399 KPKPNPNLLFSDVYQEMPAQLRKQQESLAR 428
Cdd:COG1071  319 SPEPDPEELFDDVYAEPPPHLAEQRAELAA 348
TPP_E1_PDC_ADC_BCADC cd02000
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ...
105-396 1.55e-145

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: 416.51  E-value: 1.55e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258645172 105 LYKSMTLLNTMDRILYESQRQGRIS-FYMTNYGEEGTHVGSAAALDNTDLVFGQYREAGVLMYRDYPLELFMAQCYGNIS 183
Cdd:cd02000    1 LYRTMVLIRRFDERLLELYRQGKIGgFYHLSIGQEAVAVGVAAALRPGDWVFPTYRDHGHALARGVDLKEMLAELFGKET 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258645172 184 DLGKGRQMPVHYGCKERHFVTISSPLATQIPQAVGAAYAAKRANANRVVICYFGEGAASEGDAHAGFNFAATLECPIIFF 263
Cdd:cd02000   81 GPCKGRGGSMHIGDKEKNFFGGNGIVGGQVPLAAGAALALKYRGEDRVAVCFFGDGATNEGDFHEALNFAALWKLPVIFV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258645172 264 CRNNGYAISTPTSEQYRGDGIA-RGPGYGIMSIRVDGNDVFAVYNATKEARRRAVAENQPFLIEAMTYRIGHHSTSDDSS 342
Cdd:cd02000  161 CENNGYAISTPTSRQTAGTSIAdRAAAYGIPGIRVDGNDVLAVYEAAKEAVERARAGGGPTLIEAVTYRLGGHSTSDDPS 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 258645172 343 AYRSVDEVNYWDKQDhPISRLRHYLLSQGWWDEEQEKAWRKQSRRKVMEAFEQA 396
Cdd:cd02000  241 RYRTKEEVEEWKKRD-PILRLRKYLIEAGILTEEELAAIEAEVKAEVEEAVEFA 293
E1_dh pfam00676
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ...
106-404 2.91e-137

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: 395.93  E-value: 2.91e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258645172  106 YKSMTLLNTMDRILYESQRQGRISFYMTNYGEEGTHVGSAAALDNTDLVFGQYREAGVLMYRDYPLELFMAQCYGNISDl 185
Cdd:pfam00676   1 RRMMTLRRMEDARDALYKRQGIRGFYHLYAGQEAAQVGIAAALEPGDYIIPGYRDHGNLLARGLSLEEIFAELYGRVAK- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258645172  186 GKGRQMPVHYGCKERHFVTISSPLATQIPQAVGAAYAAKRANANRVVICYFGEGAASEGDAHAGFNFAATLECPIIFFCR 265
Cdd:pfam00676  80 GKGGSMHGYYGAKGNRFYGGNGILGAQVPLGAGIALAAKYRGKKEVAITLYGDGAANQGDFFEGLNFAALWKLPVIFVCE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258645172  266 NNGYAISTPTSEQYRGDGIA-RGPGYGIMSIRVDGNDVFAVYNATKEARRRAVAENQPFLIEAMTYRIGHHSTSDDSSAY 344
Cdd:pfam00676 160 NNQYGISTPAERASASTTYAdRARGYGIPGLHVDGMDPLAVYQASKFAAERARTGKGPFLIELVTYRYGGHSMSDDPSTY 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 258645172  345 RSVDEVNYWDKQDHPISRLRHYLLSQGWWDEEQEKAWRKQSRRKVMEAFEQAERKPKPNP 404
Cdd:pfam00676 240 RTRDEYEEVRKKKDPIQRFKEHLVSKGVWSEEELKAIEKEVRKEVEEAFKKAESAPEPHP 299
PDH_E1_alph_x TIGR03181
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the ...
77-426 1.51e-120

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: 354.91  E-value: 1.51e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258645172   77 PIYRVMDRQGQIINPSEDPHLPKEKVLKLYKSMTLLNTMDRILYESQRQGRISFYMTNYGEEGTHVGSAAALDNTDLVFG 156
Cdd:TIGR03181   1 ELVQVLDEDGNVVDPEPAPDLSDEELVELYRDMVLTRRFDTKALALQRQGRLGTYAPNLGQEAAQVGSALALRKDDWVFP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258645172  157 QYREAGVLMYRDYPLELFMAQCYGNIsdlgKGRQMPVhygckERHFVTISSPLATQIPQAVGAAYAAKRANANRVVICYF 236
Cdd:TIGR03181  81 SYRDHAAMLARGVPLVEILLYWRGDE----RGSWDPE-----GVNILPPNIPIGTQYLHAAGVAYALKLRGEDNVAVTYF 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258645172  237 GEGAASEGDAHAGFNFAATLECPIIFFCRNNGYAISTPTSEQYRGDGIA-RGPGYGIMSIRVDGNDVFAVYNATKEARRR 315
Cdd:TIGR03181 152 GDGGTSEGDFYEALNFAGVFKAPVVFFVQNNQWAISVPRSKQTAAPTLAqKAIAYGIPGVQVDGNDVLAVYAVTKEAVER 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258645172  316 AVAENQPFLIEAMTYRIGHHSTSDDSSAYRSVDEVNYWDKQDhPISRLRHYLLSQGWWDEEQEKAWRKQSRRKVMEAFEQ 395
Cdd:TIGR03181 232 ARSGGGPTLIEAVTYRLGPHTTADDPTRYRTKEEEEEWRKKD-PILRLRKYLERKGLWDEEQEEALEEEAEAEVAEAVAE 310
                         330       340       350
                  ....*....|....*....|....*....|.
gi 258645172  396 AERKPKPNPNLLFSDVYQEMPAQLRKQQESL 426
Cdd:TIGR03181 311 ALALPPPPVDDIFDHVYAELPPELEEQRAEL 341
PLN02269 PLN02269
Pyruvate dehydrogenase E1 component subunit alpha
91-413 2.60e-42

Pyruvate dehydrogenase E1 component subunit alpha


Pssm-ID: 215152 [Multi-domain]  Cd Length: 362  Bit Score: 152.95  E-value: 2.60e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258645172  91 PSEDPHLPKEKVLKLYKSMTLLNTMD---RILYESQR-QGRISFYMtnyGEEGTHVGSAAALDNTDLVFGQYREAGVLMY 166
Cdd:PLN02269  21 PSRTVETSKQELVDFFRDMYLMRRMEiaaDSLYKAKLiRGFCHLYD---GQEAVAVGMEAAITKEDAIITAYRDHCTHLG 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258645172 167 RD-YPLELFmAQCYGNIS--DLGKGRQMpvHYGCKERHFVTISSPLATQIPQAVGAAYAAKRANANRVVICYFGEGAASE 243
Cdd:PLN02269  98 RGgTVLEVF-AELMGRKDgcSRGKGGSM--HFYKKDANFYGGHGIVGAQVPLGAGLAFAQKYNKEENVAFALYGDGAANQ 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258645172 244 GDAHAGFNFAATLECPIIFFCRNNGYAISTPT------SEQY-RGDGIargPGygimsIRVDGNDVFAVYNATKEARRRA 316
Cdd:PLN02269 175 GQLFEALNIAALWDLPVIFVCENNHYGMGTAEwraaksPAYYkRGDYV---PG-----LKVDGMDVLAVKQACKFAKEHA 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258645172 317 VAeNQPFLIEAMTYRIGHHSTSDDSSAYRSVDEVNYWDKQDHPISRLRHYLLSQGWWDEEQEKAWRKQSRRKVMEAFEQA 396
Cdd:PLN02269 247 LS-NGPIVLEMDTYRYHGHSMSDPGSTYRTRDEISGVRQERDPIERVRKLLLAHELATEAELKDIEKEIRKEVDDAVAKA 325
                        330
                 ....*....|....*..
gi 258645172 397 ERKPKPNPNLLFSDVYQ 413
Cdd:PLN02269 326 KESPMPDPSELFTNVYV 342
odpA CHL00149
pyruvate dehydrogenase E1 component alpha subunit; Reviewed
97-412 2.61e-30

pyruvate dehydrogenase E1 component alpha subunit; Reviewed


Pssm-ID: 177069 [Multi-domain]  Cd Length: 341  Bit Score: 119.97  E-value: 2.61e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258645172  97 LPKEKVLKLYKSMTLLNTMDRILYESQRQGRISFYMTNY-GEEGTHVGSAAALDNTDLVFGQYREAGVLMYRDYPLELFM 175
Cdd:CHL00149  17 INSMWLLVLYEDMLLGRNFEDMCAQMYYRGKMFGFVHLYnGQEAVSTGVIKLLAETDYVCSTYRDHVHALSKGVPPKNVM 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258645172 176 AQCYGNISDLGKGRQMPVHYGCKERHFVTISSPLATQIPQAVGAAYAA-------KRANANRVVICYFGEGAASEGDAHA 248
Cdd:CHL00149  97 AELFGKETGCSRGRGGSMHIFSAPHNFLGGFAFIGEGIPIALGAAFQSiyrqqvlKEVQPLRVTACFFGDGTTNNGQFFE 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258645172 249 GFNFAATLECPIIFFCRNNGYAI------STPTSEQYRgdgiaRGPGYGIMSIRVDGNDVFAVYNATKEARRRAVAENQP 322
Cdd:CHL00149 177 CLNMAVLWKLPIIFVVENNQWAIgmahhrSTSIPEIHK-----KAEAFGLPGIEVDGMDVLAVREVAKEAVERARQGDGP 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258645172 323 FLIEAMTYRIGHHSTSDDSSaYRSVDEVNYWDKQDhPISRLRHYLLSQGWWDEEQEKAWRKQSRRKVMEAFEQAERKPKP 402
Cdd:CHL00149 252 TLIEALTYRFRGHSLADPDE-LRSKQEKEAWVARD-PIKKLKSYIIDNELASQKELNKIQREVKIEIEQAVQFAISSPEP 329
                        330
                 ....*....|
gi 258645172 403 NPNLLFSDVY 412
Cdd:CHL00149 330 NISDLKKYLF 339
PLN02374 PLN02374
pyruvate dehydrogenase (acetyl-transferring)
17-412 7.55e-29

pyruvate dehydrogenase (acetyl-transferring)


Pssm-ID: 215213 [Multi-domain]  Cd Length: 433  Bit Score: 117.74  E-value: 7.55e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258645172  17 LSQAALLLLRQPGARGLARSHPPRQQQqFSSLDDKPQFPGASAEFIDKLEFIQPNVISGIPIYRVMD--RQGQIINPSED 94
Cdd:PLN02374   2 AAAFAATSLLVPVPARSSRDDAPSSPL-RGALKRSSAFTGSTSKLSSLRGLNAANGRRRSTVVAVSAvvKEKNSKASASD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258645172  95 PHLPKEKVLKLYKSMTLLNTMDRILYESQRQGRISFYMTNY-GEEGTHVGSAAALDNTDLVFGQYREAGVLMYRDYPLEL 173
Cdd:PLN02374  81 LLVTREEGLELYEDMVLGRSFEDMCAQMYYRGKMFGFVHLYnGQEAVSTGFIKLLKKDDSVVSTYRDHVHALSKGVPARA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258645172 174 FMAQCYGNISDLGKGRQMPVHYGCKERHFVTISSPLATQIPQAVGAAYAA-------KRANANRVVICYFGEGAASEGDA 246
Cdd:PLN02374 161 VMSELFGKATGCCRGQGGSMHMFSKEHNLLGGFAFIGEGIPVATGAAFSSkyrrevlKEESCDDVTLAFFGDGTCNNGQF 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258645172 247 HAGFNFAATLECPIIFFCRNNGYAI------STPTSEQYRgdgiaRGPGYGIMSIRVDGNDVFAVYNATKEARRRAVAEN 320
Cdd:PLN02374 241 FECLNMAALWKLPIVFVVENNLWAIgmshlrATSDPEIWK-----KGPAFGMPGVHVDGMDVLKVREVAKEAIERARRGE 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258645172 321 QPFLIEAMTYRIGHHSTSDDSSaYRSVDEVNYWDKQDhPISRLRHYLLSQGWWDEEQEKAWRKQSRRKVMEAFEQAERKP 400
Cdd:PLN02374 316 GPTLVECETYRFRGHSLADPDE-LRDPAEKAHYAARD-PIAALKKYLIENGLATEAELKAIEKKIDEVVEDAVEFADASP 393
                        410
                 ....*....|..
gi 258645172 401 KPNPNLLFSDVY 412
Cdd:PLN02374 394 LPPRSQLLENVF 405
TPP_enzymes cd00568
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ...
188-329 1.40e-12

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: 65.35  E-value: 1.40e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258645172 188 GRQMPVHYGCKERHFVTISSPLATQIPQAVGAAYAAKranaNRVVICYFGEGAASEGdaHAGFNFAATLECPIIFFCRNN 267
Cdd:cd00568   27 AYRYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAAP----DRPVVCIAGDGGFMMT--GQELATAVRYGLPVIVVVFNN 100
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 258645172 268 GYAISTPTSEQYRGDG------------IARGPGYGIMSIRVDGNDVFavynatKEARRRAVAENQPFLIEAMT 329
Cdd:cd00568  101 GGYGTIRMHQEAFYGGrvsgtdlsnpdfAALAEAYGAKGVRVEDPEDL------EAALAEALAAGGPALIEVKT 168
PRK05899 PRK05899
transketolase; Reviewed
232-334 8.73e-05

transketolase; Reviewed


Pssm-ID: 235639 [Multi-domain]  Cd Length: 586  Bit Score: 44.74  E-value: 8.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258645172 232 VICyfGEGAASEGDAHAGFNFAATLEC-PIIFFCRNNGYAISTPTSEQYRGDGIARGPGYGIMSIRVDGNDVFAVYNATK 310
Cdd:PRK05899 155 VLC--GDGDLMEGISHEACSLAGHLKLgNLIVIYDDNRISIDGPTEGWFTEDVKKRFEAYGWHVIEVDGHDVEAIDAAIE 232
                         90       100
                 ....*....|....*....|....
gi 258645172 311 EARrravAENQPFLIEAMTyRIGH 334
Cdd:PRK05899 233 EAK----ASTKPTLIIAKT-IIGK 251
TPP_TK cd02012
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ...
179-336 1.00e-04

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: 43.65  E-value: 1.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258645172 179 YGNISDLGKGRQ----MPVHYGCKERHFVTISS-PLATQIPQAVGAAYAAKRANANRVVICYFGEGAASEGDAHAGFNFA 253
Cdd:cd02012   72 YLPEEDLKTFRQlgsrLPGHPEYGLTPGVEVTTgSLGQGLSVAVGMALAEKLLGFDYRVYVLLGDGELQEGSVWEAASFA 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258645172 254 ATLEC-PIIFFCRNNGYAISTPTSEQYRGDGIA-RGPGYGIMSIRVDGNDVFAVYNATKEARRravAENQPFLIEAMTyR 331
Cdd:cd02012  152 GHYKLdNLIAIVDSNRIQIDGPTDDILFTEDLAkKFEAFGWNVIEVDGHDVEEILAALEEAKK---SKGKPTLIIAKT-I 227

                 ....*
gi 258645172 332 IGHHS 336
Cdd:cd02012  228 KGKGV 232
 
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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