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Conserved domains on  [gi|183396774|ref|NP_031559|]
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2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial isoform 2 [Mus musculus]

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 ...
81-430 2.04e-149

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: 2.04e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396774  81 RVMDRQGqiiNPSEDPHLPQEEVLKFYRSMTLLNTMDRILYESQRQGRISFYMTNYGEEGTHVGSAAALERTDLVFGQYR 160
Cdd:COG1071    3 QVLDPDG---TEAALPDLSKEELLELYRDMLLIRRFEERALALQRQGKIGFYHLSIGQEAAQVGAAAALRPGDWIFPTYR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396774 161 EAGVLMYRDYPLELFMSQCYGNVNDPGKGRQMPVHYGCKERHFVTISSPLATQIPQAVGAAYAAKRANANRIVICYFGEG 240
Cdd:COG1071   80 DHGHALARGVDPKELMAELFGKATGPSKGRGGSMHFFDKELNFLGGSGIVGGQLPHAVGAALAAKLRGEDEVAVAFFGDG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396774 241 AASEGDAHAGFNFAATLECPIIFFCRNNGYAISTPTSEQYRGDGIAARGPGYGIMSIRVDGNDVFAVYNATKEARRRAVA 320
Cdd:COG1071  160 ATSEGDFHEALNFAAVWKLPVVFVCENNGYAISTPVERQTAVETIADRAAGYGIPGVRVDGNDVLAVYAAVKEAVERARA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396774 321 ENQPFLIEAMTYRIGHHSTSDDSSAYRSVDEVNYWDKQDhPISRLRQYLLNQGWWDEEQEKAWRKQSRKKVMEAFEQAER 400
Cdd:COG1071  240 GEGPTLIEAKTYRLGGHSTSDDPTRYRTKEEVEEWRERD-PIERLRAYLLEEGLLTEEELEAIEAEAKAEVEEAVEFAEA 318
                        330       340       350
                 ....*....|....*....|....*....|
gi 183396774 401 KLKPNPSLLFSDVYQEMPAQLRRQQESLAR 430
Cdd:COG1071  319 SPEPDPEELFDDVYAEPPPHLAEQRAELAA 348
 
Name Accession Description Interval E-value
AcoA COG1071
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ...
81-430 2.04e-149

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: 2.04e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396774  81 RVMDRQGqiiNPSEDPHLPQEEVLKFYRSMTLLNTMDRILYESQRQGRISFYMTNYGEEGTHVGSAAALERTDLVFGQYR 160
Cdd:COG1071    3 QVLDPDG---TEAALPDLSKEELLELYRDMLLIRRFEERALALQRQGKIGFYHLSIGQEAAQVGAAAALRPGDWIFPTYR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396774 161 EAGVLMYRDYPLELFMSQCYGNVNDPGKGRQMPVHYGCKERHFVTISSPLATQIPQAVGAAYAAKRANANRIVICYFGEG 240
Cdd:COG1071   80 DHGHALARGVDPKELMAELFGKATGPSKGRGGSMHFFDKELNFLGGSGIVGGQLPHAVGAALAAKLRGEDEVAVAFFGDG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396774 241 AASEGDAHAGFNFAATLECPIIFFCRNNGYAISTPTSEQYRGDGIAARGPGYGIMSIRVDGNDVFAVYNATKEARRRAVA 320
Cdd:COG1071  160 ATSEGDFHEALNFAAVWKLPVVFVCENNGYAISTPVERQTAVETIADRAAGYGIPGVRVDGNDVLAVYAAVKEAVERARA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396774 321 ENQPFLIEAMTYRIGHHSTSDDSSAYRSVDEVNYWDKQDhPISRLRQYLLNQGWWDEEQEKAWRKQSRKKVMEAFEQAER 400
Cdd:COG1071  240 GEGPTLIEAKTYRLGGHSTSDDPTRYRTKEEVEEWRERD-PIERLRAYLLEEGLLTEEELEAIEAEAKAEVEEAVEFAEA 318
                        330       340       350
                 ....*....|....*....|....*....|
gi 183396774 401 KLKPNPSLLFSDVYQEMPAQLRRQQESLAR 430
Cdd:COG1071  319 SPEPDPEELFDDVYAEPPPHLAEQRAELAA 348
TPP_E1_PDC_ADC_BCADC cd02000
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ...
106-398 5.15e-148

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: 422.67  E-value: 5.15e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396774 106 FYRSMTLLNTMDRILYESQRQGRIS-FYMTNYGEEGTHVGSAAALERTDLVFGQYREAGVLMYRDYPLELFMSQCYGNVN 184
Cdd:cd02000    1 LYRTMVLIRRFDERLLELYRQGKIGgFYHLSIGQEAVAVGVAAALRPGDWVFPTYRDHGHALARGVDLKEMLAELFGKET 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396774 185 DPGKGRQMPVHYGCKERHFVTISSPLATQIPQAVGAAYAAKRANANRIVICYFGEGAASEGDAHAGFNFAATLECPIIFF 264
Cdd:cd02000   81 GPCKGRGGSMHIGDKEKNFFGGNGIVGGQVPLAAGAALALKYRGEDRVAVCFFGDGATNEGDFHEALNFAALWKLPVIFV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396774 265 CRNNGYAISTPTSEQYRGDGIAARGPGYGIMSIRVDGNDVFAVYNATKEARRRAVAENQPFLIEAMTYRIGHHSTSDDSS 344
Cdd:cd02000  161 CENNGYAISTPTSRQTAGTSIADRAAAYGIPGIRVDGNDVLAVYEAAKEAVERARAGGGPTLIEAVTYRLGGHSTSDDPS 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 183396774 345 AYRSVDEVNYWDKQDhPISRLRQYLLNQGWWDEEQEKAWRKQSRKKVMEAFEQA 398
Cdd:cd02000  241 RYRTKEEVEEWKKRD-PILRLRKYLIEAGILTEEELAAIEAEVKAEVEEAVEFA 293
E1_dh pfam00676
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ...
107-407 3.41e-139

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: 400.93  E-value: 3.41e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396774  107 YRSMTLLNTMDRILYESQRQGRISFYMTNYGEEGTHVGSAAALERTDLVFGQYREAGVLMYRDYPLELFMSQCYGNV-ND 185
Cdd:pfam00676   1 RRMMTLRRMEDARDALYKRQGIRGFYHLYAGQEAAQVGIAAALEPGDYIIPGYRDHGNLLARGLSLEEIFAELYGRVaKG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396774  186 PGKGRQMpvHYGCKERHFVTISSPLATQIPQAVGAAYAAKRANANRIVICYFGEGAASEGDAHAGFNFAATLECPIIFFC 265
Cdd:pfam00676  81 KGGSMHG--YYGAKGNRFYGGNGILGAQVPLGAGIALAAKYRGKKEVAITLYGDGAANQGDFFEGLNFAALWKLPVIFVC 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396774  266 RNNGYAISTPTSEQYRGDGIAARGPGYGIMSIRVDGNDVFAVYNATKEARRRAVAENQPFLIEAMTYRIGHHSTSDDSSA 345
Cdd:pfam00676 159 ENNQYGISTPAERASASTTYADRARGYGIPGLHVDGMDPLAVYQASKFAAERARTGKGPFLIELVTYRYGGHSMSDDPST 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 183396774  346 YRSVDEVNYWDKQDHPISRLRQYLLNQGWWDEEQEKAWRKQSRKKVMEAFEQAERKLKPNPS 407
Cdd:pfam00676 239 YRTRDEYEEVRKKKDPIQRFKEHLVSKGVWSEEELKAIEKEVRKEVEEAFKKAESAPEPHPE 300
PDH_E1_alph_x TIGR03181
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the ...
78-428 2.51e-121

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: 356.84  E-value: 2.51e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396774   78 PIYRVMDRQGQIINPSEDPHLPQEEVLKFYRSMTLLNTMDRILYESQRQGRISFYMTNYGEEGTHVGSAAALERTDLVFG 157
Cdd:TIGR03181   1 ELVQVLDEDGNVVDPEPAPDLSDEELVELYRDMVLTRRFDTKALALQRQGRLGTYAPNLGQEAAQVGSALALRKDDWVFP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396774  158 QYREAGVLMYRDYPLELFMSQCYGNVndpgKGRQMPVhygckERHFVTISSPLATQIPQAVGAAYAAKRANANRIVICYF 237
Cdd:TIGR03181  81 SYRDHAAMLARGVPLVEILLYWRGDE----RGSWDPE-----GVNILPPNIPIGTQYLHAAGVAYALKLRGEDNVAVTYF 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396774  238 GEGAASEGDAHAGFNFAATLECPIIFFCRNNGYAISTPTSEQYRGDGIAARGPGYGIMSIRVDGNDVFAVYNATKEARRR 317
Cdd:TIGR03181 152 GDGGTSEGDFYEALNFAGVFKAPVVFFVQNNQWAISVPRSKQTAAPTLAQKAIAYGIPGVQVDGNDVLAVYAVTKEAVER 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396774  318 AVAENQPFLIEAMTYRIGHHSTSDDSSAYRSVDEVNYWDKQDhPISRLRQYLLNQGWWDEEQEKAWRKQSRKKVMEAFEQ 397
Cdd:TIGR03181 232 ARSGGGPTLIEAVTYRLGPHTTADDPTRYRTKEEEEEWRKKD-PILRLRKYLERKGLWDEEQEEALEEEAEAEVAEAVAE 310
                         330       340       350
                  ....*....|....*....|....*....|.
gi 183396774  398 AERKLKPNPSLLFSDVYQEMPAQLRRQQESL 428
Cdd:TIGR03181 311 ALALPPPPVDDIFDHVYAELPPELEEQRAEL 341
PLN02269 PLN02269
Pyruvate dehydrogenase E1 component subunit alpha
92-415 1.16e-41

Pyruvate dehydrogenase E1 component subunit alpha


Pssm-ID: 215152 [Multi-domain]  Cd Length: 362  Bit Score: 151.40  E-value: 1.16e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396774  92 PSEDPHLPQEEVLKFYRSMTLLNTMD---RILYESQR-QGRISFYMtnyGEEGTHVGSAAALERTDLVFGQYREAGVLMY 167
Cdd:PLN02269  21 PSRTVETSKQELVDFFRDMYLMRRMEiaaDSLYKAKLiRGFCHLYD---GQEAVAVGMEAAITKEDAIITAYRDHCTHLG 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396774 168 RD-YPLELFmSQCYGNVNDPGKGRQMPVHYGCKERHFVTISSPLATQIPQAVGAAYAAKRANANRIVICYFGEGAASEGD 246
Cdd:PLN02269  98 RGgTVLEVF-AELMGRKDGCSRGKGGSMHFYKKDANFYGGHGIVGAQVPLGAGLAFAQKYNKEENVAFALYGDGAANQGQ 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396774 247 AHAGFNFAATLECPIIFFCRNNGYAISTPT------SEQY-RGDGIaargPGygimsIRVDGNDVFAVYNATKEARRRAV 319
Cdd:PLN02269 177 LFEALNIAALWDLPVIFVCENNHYGMGTAEwraaksPAYYkRGDYV----PG-----LKVDGMDVLAVKQACKFAKEHAL 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396774 320 AeNQPFLIEAMTYRIGHHSTSDDSSAYRSVDEVNYWDKQDHPISRLRQYLLNQGWWDEEQEKAWRKQSRKKVMEAFEQAE 399
Cdd:PLN02269 248 S-NGPIVLEMDTYRYHGHSMSDPGSTYRTRDEISGVRQERDPIERVRKLLLAHELATEAELKDIEKEIRKEVDDAVAKAK 326
                        330
                 ....*....|....*.
gi 183396774 400 RKLKPNPSLLFSDVYQ 415
Cdd:PLN02269 327 ESPMPDPSELFTNVYV 342
 
Name Accession Description Interval E-value
AcoA COG1071
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ...
81-430 2.04e-149

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: 2.04e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396774  81 RVMDRQGqiiNPSEDPHLPQEEVLKFYRSMTLLNTMDRILYESQRQGRISFYMTNYGEEGTHVGSAAALERTDLVFGQYR 160
Cdd:COG1071    3 QVLDPDG---TEAALPDLSKEELLELYRDMLLIRRFEERALALQRQGKIGFYHLSIGQEAAQVGAAAALRPGDWIFPTYR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396774 161 EAGVLMYRDYPLELFMSQCYGNVNDPGKGRQMPVHYGCKERHFVTISSPLATQIPQAVGAAYAAKRANANRIVICYFGEG 240
Cdd:COG1071   80 DHGHALARGVDPKELMAELFGKATGPSKGRGGSMHFFDKELNFLGGSGIVGGQLPHAVGAALAAKLRGEDEVAVAFFGDG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396774 241 AASEGDAHAGFNFAATLECPIIFFCRNNGYAISTPTSEQYRGDGIAARGPGYGIMSIRVDGNDVFAVYNATKEARRRAVA 320
Cdd:COG1071  160 ATSEGDFHEALNFAAVWKLPVVFVCENNGYAISTPVERQTAVETIADRAAGYGIPGVRVDGNDVLAVYAAVKEAVERARA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396774 321 ENQPFLIEAMTYRIGHHSTSDDSSAYRSVDEVNYWDKQDhPISRLRQYLLNQGWWDEEQEKAWRKQSRKKVMEAFEQAER 400
Cdd:COG1071  240 GEGPTLIEAKTYRLGGHSTSDDPTRYRTKEEVEEWRERD-PIERLRAYLLEEGLLTEEELEAIEAEAKAEVEEAVEFAEA 318
                        330       340       350
                 ....*....|....*....|....*....|
gi 183396774 401 KLKPNPSLLFSDVYQEMPAQLRRQQESLAR 430
Cdd:COG1071  319 SPEPDPEELFDDVYAEPPPHLAEQRAELAA 348
TPP_E1_PDC_ADC_BCADC cd02000
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ...
106-398 5.15e-148

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: 422.67  E-value: 5.15e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396774 106 FYRSMTLLNTMDRILYESQRQGRIS-FYMTNYGEEGTHVGSAAALERTDLVFGQYREAGVLMYRDYPLELFMSQCYGNVN 184
Cdd:cd02000    1 LYRTMVLIRRFDERLLELYRQGKIGgFYHLSIGQEAVAVGVAAALRPGDWVFPTYRDHGHALARGVDLKEMLAELFGKET 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396774 185 DPGKGRQMPVHYGCKERHFVTISSPLATQIPQAVGAAYAAKRANANRIVICYFGEGAASEGDAHAGFNFAATLECPIIFF 264
Cdd:cd02000   81 GPCKGRGGSMHIGDKEKNFFGGNGIVGGQVPLAAGAALALKYRGEDRVAVCFFGDGATNEGDFHEALNFAALWKLPVIFV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396774 265 CRNNGYAISTPTSEQYRGDGIAARGPGYGIMSIRVDGNDVFAVYNATKEARRRAVAENQPFLIEAMTYRIGHHSTSDDSS 344
Cdd:cd02000  161 CENNGYAISTPTSRQTAGTSIADRAAAYGIPGIRVDGNDVLAVYEAAKEAVERARAGGGPTLIEAVTYRLGGHSTSDDPS 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 183396774 345 AYRSVDEVNYWDKQDhPISRLRQYLLNQGWWDEEQEKAWRKQSRKKVMEAFEQA 398
Cdd:cd02000  241 RYRTKEEVEEWKKRD-PILRLRKYLIEAGILTEEELAAIEAEVKAEVEEAVEFA 293
E1_dh pfam00676
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ...
107-407 3.41e-139

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: 400.93  E-value: 3.41e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396774  107 YRSMTLLNTMDRILYESQRQGRISFYMTNYGEEGTHVGSAAALERTDLVFGQYREAGVLMYRDYPLELFMSQCYGNV-ND 185
Cdd:pfam00676   1 RRMMTLRRMEDARDALYKRQGIRGFYHLYAGQEAAQVGIAAALEPGDYIIPGYRDHGNLLARGLSLEEIFAELYGRVaKG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396774  186 PGKGRQMpvHYGCKERHFVTISSPLATQIPQAVGAAYAAKRANANRIVICYFGEGAASEGDAHAGFNFAATLECPIIFFC 265
Cdd:pfam00676  81 KGGSMHG--YYGAKGNRFYGGNGILGAQVPLGAGIALAAKYRGKKEVAITLYGDGAANQGDFFEGLNFAALWKLPVIFVC 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396774  266 RNNGYAISTPTSEQYRGDGIAARGPGYGIMSIRVDGNDVFAVYNATKEARRRAVAENQPFLIEAMTYRIGHHSTSDDSSA 345
Cdd:pfam00676 159 ENNQYGISTPAERASASTTYADRARGYGIPGLHVDGMDPLAVYQASKFAAERARTGKGPFLIELVTYRYGGHSMSDDPST 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 183396774  346 YRSVDEVNYWDKQDHPISRLRQYLLNQGWWDEEQEKAWRKQSRKKVMEAFEQAERKLKPNPS 407
Cdd:pfam00676 239 YRTRDEYEEVRKKKDPIQRFKEHLVSKGVWSEEELKAIEKEVRKEVEEAFKKAESAPEPHPE 300
PDH_E1_alph_x TIGR03181
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the ...
78-428 2.51e-121

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: 356.84  E-value: 2.51e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396774   78 PIYRVMDRQGQIINPSEDPHLPQEEVLKFYRSMTLLNTMDRILYESQRQGRISFYMTNYGEEGTHVGSAAALERTDLVFG 157
Cdd:TIGR03181   1 ELVQVLDEDGNVVDPEPAPDLSDEELVELYRDMVLTRRFDTKALALQRQGRLGTYAPNLGQEAAQVGSALALRKDDWVFP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396774  158 QYREAGVLMYRDYPLELFMSQCYGNVndpgKGRQMPVhygckERHFVTISSPLATQIPQAVGAAYAAKRANANRIVICYF 237
Cdd:TIGR03181  81 SYRDHAAMLARGVPLVEILLYWRGDE----RGSWDPE-----GVNILPPNIPIGTQYLHAAGVAYALKLRGEDNVAVTYF 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396774  238 GEGAASEGDAHAGFNFAATLECPIIFFCRNNGYAISTPTSEQYRGDGIAARGPGYGIMSIRVDGNDVFAVYNATKEARRR 317
Cdd:TIGR03181 152 GDGGTSEGDFYEALNFAGVFKAPVVFFVQNNQWAISVPRSKQTAAPTLAQKAIAYGIPGVQVDGNDVLAVYAVTKEAVER 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396774  318 AVAENQPFLIEAMTYRIGHHSTSDDSSAYRSVDEVNYWDKQDhPISRLRQYLLNQGWWDEEQEKAWRKQSRKKVMEAFEQ 397
Cdd:TIGR03181 232 ARSGGGPTLIEAVTYRLGPHTTADDPTRYRTKEEEEEWRKKD-PILRLRKYLERKGLWDEEQEEALEEEAEAEVAEAVAE 310
                         330       340       350
                  ....*....|....*....|....*....|.
gi 183396774  398 AERKLKPNPSLLFSDVYQEMPAQLRRQQESL 428
Cdd:TIGR03181 311 ALALPPPPVDDIFDHVYAELPPELEEQRAEL 341
PLN02269 PLN02269
Pyruvate dehydrogenase E1 component subunit alpha
92-415 1.16e-41

Pyruvate dehydrogenase E1 component subunit alpha


Pssm-ID: 215152 [Multi-domain]  Cd Length: 362  Bit Score: 151.40  E-value: 1.16e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396774  92 PSEDPHLPQEEVLKFYRSMTLLNTMD---RILYESQR-QGRISFYMtnyGEEGTHVGSAAALERTDLVFGQYREAGVLMY 167
Cdd:PLN02269  21 PSRTVETSKQELVDFFRDMYLMRRMEiaaDSLYKAKLiRGFCHLYD---GQEAVAVGMEAAITKEDAIITAYRDHCTHLG 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396774 168 RD-YPLELFmSQCYGNVNDPGKGRQMPVHYGCKERHFVTISSPLATQIPQAVGAAYAAKRANANRIVICYFGEGAASEGD 246
Cdd:PLN02269  98 RGgTVLEVF-AELMGRKDGCSRGKGGSMHFYKKDANFYGGHGIVGAQVPLGAGLAFAQKYNKEENVAFALYGDGAANQGQ 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396774 247 AHAGFNFAATLECPIIFFCRNNGYAISTPT------SEQY-RGDGIaargPGygimsIRVDGNDVFAVYNATKEARRRAV 319
Cdd:PLN02269 177 LFEALNIAALWDLPVIFVCENNHYGMGTAEwraaksPAYYkRGDYV----PG-----LKVDGMDVLAVKQACKFAKEHAL 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396774 320 AeNQPFLIEAMTYRIGHHSTSDDSSAYRSVDEVNYWDKQDHPISRLRQYLLNQGWWDEEQEKAWRKQSRKKVMEAFEQAE 399
Cdd:PLN02269 248 S-NGPIVLEMDTYRYHGHSMSDPGSTYRTRDEISGVRQERDPIERVRKLLLAHELATEAELKDIEKEIRKEVDDAVAKAK 326
                        330
                 ....*....|....*.
gi 183396774 400 RKLKPNPSLLFSDVYQ 415
Cdd:PLN02269 327 ESPMPDPSELFTNVYV 342
PLN02374 PLN02374
pyruvate dehydrogenase (acetyl-transferring)
36-414 2.41e-27

pyruvate dehydrogenase (acetyl-transferring)


Pssm-ID: 215213 [Multi-domain]  Cd Length: 433  Bit Score: 113.11  E-value: 2.41e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396774  36 SHPSRQQQQQFPSLDDKPQFPGASAEFVDKLEFIQPNVISGIPIYRVMD--RQGQIINPSEDPHLPQEEVLKFYRSMTLL 113
Cdd:PLN02374  19 SRDDAPSSPLRGALKRSSAFTGSTSKLSSLRGLNAANGRRRSTVVAVSAvvKEKNSKASASDLLVTREEGLELYEDMVLG 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396774 114 NTMDRILYESQRQGRISFYMTNY-GEEGTHVGSAAALERTDLVFGQYREAGVLMYRDYPLELFMSQCYGNVNDPGKGRQM 192
Cdd:PLN02374  99 RSFEDMCAQMYYRGKMFGFVHLYnGQEAVSTGFIKLLKKDDSVVSTYRDHVHALSKGVPARAVMSELFGKATGCCRGQGG 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396774 193 PVHYGCKERHFVTISSPLATQIPQAVGAAYAA-------KRANANRIVICYFGEGAASEGDAHAGFNFAATLECPIIFFC 265
Cdd:PLN02374 179 SMHMFSKEHNLLGGFAFIGEGIPVATGAAFSSkyrrevlKEESCDDVTLAFFGDGTCNNGQFFECLNMAALWKLPIVFVV 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396774 266 RNNGYAISTPTSEQYRGDGIAARGPGYGIMSIRVDGNDVFAVYNATKEARRRAVAENQPFLIEAMTYRIGHHSTSDDSSa 345
Cdd:PLN02374 259 ENNLWAIGMSHLRATSDPEIWKKGPAFGMPGVHVDGMDVLKVREVAKEAIERARRGEGPTLVECETYRFRGHSLADPDE- 337
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 183396774 346 YRSVDEVNYWDKQDhPISRLRQYLLNQGWWDEEQEKAWRKQSRKKVMEAFEQAERKLKPNPSLLFSDVY 414
Cdd:PLN02374 338 LRDPAEKAHYAARD-PIAALKKYLIENGLATEAELKAIEKKIDEVVEDAVEFADASPLPPRSQLLENVF 405
odpA CHL00149
pyruvate dehydrogenase E1 component alpha subunit; Reviewed
103-414 4.82e-27

pyruvate dehydrogenase E1 component alpha subunit; Reviewed


Pssm-ID: 177069 [Multi-domain]  Cd Length: 341  Bit Score: 110.73  E-value: 4.82e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396774 103 VLKFYRSMTLLNTMDRILYESQRQGRISFYMTNY-GEEGTHVGSAAALERTDLVFGQYREAGVLMYRDYPLELFMSQCYG 181
Cdd:CHL00149  22 LLVLYEDMLLGRNFEDMCAQMYYRGKMFGFVHLYnGQEAVSTGVIKLLAETDYVCSTYRDHVHALSKGVPPKNVMAELFG 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396774 182 NVNDPGKGRQMPVHYGCKERHFVTISSPLATQIPQAVGAAYAA-------KRANANRIVICYFGEGAASEGDAHAGFNFA 254
Cdd:CHL00149 102 KETGCSRGRGGSMHIFSAPHNFLGGFAFIGEGIPIALGAAFQSiyrqqvlKEVQPLRVTACFFGDGTTNNGQFFECLNMA 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396774 255 ATLECPIIFFCRNNGYAISTPTSEQYRGDGIAARGPGYGIMSIRVDGNDVFAVYNATKEARRRAVAENQPFLIEAMTYRI 334
Cdd:CHL00149 182 VLWKLPIIFVVENNQWAIGMAHHRSTSIPEIHKKAEAFGLPGIEVDGMDVLAVREVAKEAVERARQGDGPTLIEALTYRF 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396774 335 GHHSTSDDSSaYRSVDEVNYWDKQDhPISRLRQYLLNQGWWDEEQEKAWRKQSRKKVMEAFEQAERKLKPNPSLLFSDVY 414
Cdd:CHL00149 262 RGHSLADPDE-LRSKQEKEAWVARD-PIKKLKSYIIDNELASQKELNKIQREVKIEIEQAVQFAISSPEPNISDLKKYLF 339
TPP_enzymes cd00568
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ...
183-331 1.26e-11

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: 62.66  E-value: 1.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396774 183 VNDPGK----GRQMPVHYGCKERHFVTISSPLATQIPQAVgaayAAKRANANRIVICYFGEGAASEGdaHAGFNFAATLE 258
Cdd:cd00568   17 VNDAGNsaywAYRYLPLRRGRRFLTSTGFGAMGYGLPAAI----GAALAAPDRPVVCIAGDGGFMMT--GQELATAVRYG 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396774 259 CPIIFFCRNNGYAISTPTSEQYRGDG-----------IAARGPGYGIMSIRVDGNDVFavynatKEARRRAVAENQPFLI 327
Cdd:cd00568   91 LPVIVVVFNNGGYGTIRMHQEAFYGGrvsgtdlsnpdFAALAEAYGAKGVRVEDPEDL------EAALAEALAAGGPALI 164

                 ....
gi 183396774 328 EAMT 331
Cdd:cd00568  165 EVKT 168
TPP_TK cd02012
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ...
192-338 4.27e-06

Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK catalyzes the transfer of a two-carbon unit from ketose phosphates to aldose phosphates. In heterotrophic organisms, TK provides a link between glycolysis and the pentose phosphate pathway and provides precursors for nucleotide, aromatic amino acid and vitamin biosynthesis. In addition, the enzyme plays a central role in the Calvin cycle in plants. Typically, TKs are homodimers. They require TPP and divalent cations, such as magnesium ions, for activity.


Pssm-ID: 238970 [Multi-domain]  Cd Length: 255  Bit Score: 47.88  E-value: 4.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396774 192 MPVHYGCKERHFVTISS-PLATQIPQAVGAAYAAKRANANRIVICYFGEGAASEGDAHAGFNFAATLEC-PIIFFCRNNG 269
Cdd:cd02012   88 LPGHPEYGLTPGVEVTTgSLGQGLSVAVGMALAEKLLGFDYRVYVLLGDGELQEGSVWEAASFAGHYKLdNLIAIVDSNR 167
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 183396774 270 YAISTPTSEQYRGDGIAARGPGYGIMSIRVDGNDVFAVYNATKEARRravAENQPFLIEAMTyRIGHHS 338
Cdd:cd02012  168 IQIDGPTDDILFTEDLAKKFEAFGWNVIEVDGHDVEEILAALEEAKK---SKGKPTLIIAKT-IKGKGV 232
PRK05899 PRK05899
transketolase; Reviewed
233-336 3.12e-05

transketolase; Reviewed


Pssm-ID: 235639 [Multi-domain]  Cd Length: 586  Bit Score: 46.28  E-value: 3.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396774 233 VICyfGEGAASEGDAHAGFNFAATLEC-PIIFFCRNNGYAISTPTSEQYRGDgIAARGPGYGIMSIRVDGNDVFAVYNAT 311
Cdd:PRK05899 155 VLC--GDGDLMEGISHEACSLAGHLKLgNLIVIYDDNRISIDGPTEGWFTED-VKKRFEAYGWHVIEVDGHDVEAIDAAI 231
                         90       100
                 ....*....|....*....|....*
gi 183396774 312 KEARrravAENQPFLIEAMTyRIGH 336
Cdd:PRK05899 232 EEAK----ASTKPTLIIAKT-IIGK 251
 
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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