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Conserved domains on  [gi|548403|sp|P12694|]
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RecName: Full=2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial; AltName: Full=Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain; Short=BCKDE1A; Short=BCKDH E1-alpha; Flags: Precursor

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 ...
80-429 9.47e-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: 429.18  E-value: 9.47e-150
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548403    80 RVMDRQGqiiNPSEDPHLPKEKVLKLYKSMTLLNTMDRILYESQRQGRISFYMTNYGEEGTHVGSAAALDNTDLVFGQYR 159
Cdd:COG1071   3 QVLDPDG---TEAALPDLSKEELLELYRDMLLIRRFEERALALQRQGKIGFYHLSIGQEAAQVGAAAALRPGDWIFPTYR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548403   160 EAGVLMYRDYPLELFMAQCYGNISDLGKGRQMPVHYGCKERHFVTISSPLATQIPQAVGAAYAAKRANANRVVICYFGEG 239
Cdd:COG1071  80 DHGHALARGVDPKELMAELFGKATGPSKGRGGSMHFFDKELNFLGGSGIVGGQLPHAVGAALAAKLRGEDEVAVAFFGDG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548403   240 AASEGDAHAGFNFAATLECPIIFFCRNNGYAISTPTSEQYRGDGIAARGPGYGIMSIRVDGNDVFAVYNATKEARRRAVA 319
Cdd:COG1071 160 ATSEGDFHEALNFAAVWKLPVVFVCENNGYAISTPVERQTAVETIADRAAGYGIPGVRVDGNDVLAVYAAVKEAVERARA 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548403   320 ENQPFLIEAMTYRIGHHSTSDDSSAYRSVDEVNYWDKQDhPISRLRHYLLSQGWWDEEQEKAWRKQSRRKVMEAFEQAER 399
Cdd:COG1071 240 GEGPTLIEAKTYRLGGHSTSDDPTRYRTKEEVEEWRERD-PIERLRAYLLEEGLLTEEELEAIEAEAKAEVEEAVEFAEA 318
                       330       340       350
                ....*....|....*....|....*....|
gi 548403   400 KPKPNPNLLFSDVYQEMPAQLRKQQESLAR 429
Cdd:COG1071 319 SPEPDPEELFDDVYAEPPPHLAEQRAELAA 348
 
Name Accession Description Interval E-value
AcoA COG1071
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ...
80-429 9.47e-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: 429.18  E-value: 9.47e-150
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548403    80 RVMDRQGqiiNPSEDPHLPKEKVLKLYKSMTLLNTMDRILYESQRQGRISFYMTNYGEEGTHVGSAAALDNTDLVFGQYR 159
Cdd:COG1071   3 QVLDPDG---TEAALPDLSKEELLELYRDMLLIRRFEERALALQRQGKIGFYHLSIGQEAAQVGAAAALRPGDWIFPTYR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548403   160 EAGVLMYRDYPLELFMAQCYGNISDLGKGRQMPVHYGCKERHFVTISSPLATQIPQAVGAAYAAKRANANRVVICYFGEG 239
Cdd:COG1071  80 DHGHALARGVDPKELMAELFGKATGPSKGRGGSMHFFDKELNFLGGSGIVGGQLPHAVGAALAAKLRGEDEVAVAFFGDG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548403   240 AASEGDAHAGFNFAATLECPIIFFCRNNGYAISTPTSEQYRGDGIAARGPGYGIMSIRVDGNDVFAVYNATKEARRRAVA 319
Cdd:COG1071 160 ATSEGDFHEALNFAAVWKLPVVFVCENNGYAISTPVERQTAVETIADRAAGYGIPGVRVDGNDVLAVYAAVKEAVERARA 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548403   320 ENQPFLIEAMTYRIGHHSTSDDSSAYRSVDEVNYWDKQDhPISRLRHYLLSQGWWDEEQEKAWRKQSRRKVMEAFEQAER 399
Cdd:COG1071 240 GEGPTLIEAKTYRLGGHSTSDDPTRYRTKEEVEEWRERD-PIERLRAYLLEEGLLTEEELEAIEAEAKAEVEEAVEFAEA 318
                       330       340       350
                ....*....|....*....|....*....|
gi 548403   400 KPKPNPNLLFSDVYQEMPAQLRKQQESLAR 429
Cdd:COG1071 319 SPEPDPEELFDDVYAEPPPHLAEQRAELAA 348
TPP_E1_PDC_ADC_BCADC cd02000
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ...
105-397 2.01e-147

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: 421.13  E-value: 2.01e-147
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548403   105 LYKSMTLLNTMDRILYESQRQGRIS-FYMTNYGEEGTHVGSAAALDNTDLVFGQYREAGVLMYRDYPLELFMAQCYGNIS 183
Cdd:cd02000   1 LYRTMVLIRRFDERLLELYRQGKIGgFYHLSIGQEAVAVGVAAALRPGDWVFPTYRDHGHALARGVDLKEMLAELFGKET 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548403   184 DLGKGRQMPVHYGCKERHFVTISSPLATQIPQAVGAAYAAKRANANRVVICYFGEGAASEGDAHAGFNFAATLECPIIFF 263
Cdd:cd02000  81 GPCKGRGGSMHIGDKEKNFFGGNGIVGGQVPLAAGAALALKYRGEDRVAVCFFGDGATNEGDFHEALNFAALWKLPVIFV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548403   264 CRNNGYAISTPTSEQYRGDGIAARGPGYGIMSIRVDGNDVFAVYNATKEARRRAVAENQPFLIEAMTYRIGHHSTSDDSS 343
Cdd:cd02000 161 CENNGYAISTPTSRQTAGTSIADRAAAYGIPGIRVDGNDVLAVYEAAKEAVERARAGGGPTLIEAVTYRLGGHSTSDDPS 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 548403   344 AYRSVDEVNYWDKQDhPISRLRHYLLSQGWWDEEQEKAWRKQSRRKVMEAFEQA 397
Cdd:cd02000 241 RYRTKEEVEEWKKRD-PILRLRKYLIEAGILTEEELAAIEAEVKAEVEEAVEFA 293
E1_dh pfam00676
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ...
106-405 5.75e-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: 400.16  E-value: 5.75e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548403     106 YKSMTLLNTMDRILYESQRQGRISFYMTNYGEEGTHVGSAAALDNTDLVFGQYREAGVLMYRDYPLELFMAQCYGNISDl 185
Cdd:pfam00676   1 RRMMTLRRMEDARDALYKRQGIRGFYHLYAGQEAAQVGIAAALEPGDYIIPGYRDHGNLLARGLSLEEIFAELYGRVAK- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548403     186 GKGRQMPVHYGCKERHFVTISSPLATQIPQAVGAAYAAKRANANRVVICYFGEGAASEGDAHAGFNFAATLECPIIFFCR 265
Cdd:pfam00676  80 GKGGSMHGYYGAKGNRFYGGNGILGAQVPLGAGIALAAKYRGKKEVAITLYGDGAANQGDFFEGLNFAALWKLPVIFVCE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548403     266 NNGYAISTPTSEQYRGDGIAARGPGYGIMSIRVDGNDVFAVYNATKEARRRAVAENQPFLIEAMTYRIGHHSTSDDSSAY 345
Cdd:pfam00676 160 NNQYGISTPAERASASTTYADRARGYGIPGLHVDGMDPLAVYQASKFAAERARTGKGPFLIELVTYRYGGHSMSDDPSTY 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 548403     346 RSVDEVNYWDKQDHPISRLRHYLLSQGWWDEEQEKAWRKQSRRKVMEAFEQAERKPKPNP 405
Cdd:pfam00676 240 RTRDEYEEVRKKKDPIQRFKEHLVSKGVWSEEELKAIEKEVRKEVEEAFKKAESAPEPHP 299
PDH_E1_alph_x TIGR03181
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the ...
77-427 2.47e-122

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: 359.54  E-value: 2.47e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548403      77 PIYRVMDRQGQIINPSEDPHLPKEKVLKLYKSMTLLNTMDRILYESQRQGRISFYMTNYGEEGTHVGSAAALDNTDLVFG 156
Cdd:TIGR03181   1 ELVQVLDEDGNVVDPEPAPDLSDEELVELYRDMVLTRRFDTKALALQRQGRLGTYAPNLGQEAAQVGSALALRKDDWVFP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548403     157 QYREAGVLMYRDYPLELFMAQCYGNIsdlgKGRQMPVhygckERHFVTISSPLATQIPQAVGAAYAAKRANANRVVICYF 236
Cdd:TIGR03181  81 SYRDHAAMLARGVPLVEILLYWRGDE----RGSWDPE-----GVNILPPNIPIGTQYLHAAGVAYALKLRGEDNVAVTYF 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548403     237 GEGAASEGDAHAGFNFAATLECPIIFFCRNNGYAISTPTSEQYRGDGIAARGPGYGIMSIRVDGNDVFAVYNATKEARRR 316
Cdd:TIGR03181 152 GDGGTSEGDFYEALNFAGVFKAPVVFFVQNNQWAISVPRSKQTAAPTLAQKAIAYGIPGVQVDGNDVLAVYAVTKEAVER 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548403     317 AVAENQPFLIEAMTYRIGHHSTSDDSSAYRSVDEVNYWDKQDhPISRLRHYLLSQGWWDEEQEKAWRKQSRRKVMEAFEQ 396
Cdd:TIGR03181 232 ARSGGGPTLIEAVTYRLGPHTTADDPTRYRTKEEEEEWRKKD-PILRLRKYLERKGLWDEEQEEALEEEAEAEVAEAVAE 310
                         330       340       350
                  ....*....|....*....|....*....|.
gi 548403     397 AERKPKPNPNLLFSDVYQEMPAQLRKQQESL 427
Cdd:TIGR03181 311 ALALPPPPVDDIFDHVYAELPPELEEQRAEL 341
PLN02269 PLN02269
Pyruvate dehydrogenase E1 component subunit alpha
91-414 4.44e-42

Pyruvate dehydrogenase E1 component subunit alpha


Pssm-ID: 215152 [Multi-domain]  Cd Length: 362  Bit Score: 152.56  E-value: 4.44e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548403     91 PSEDPHLPKEKVLKLYKSMTLLNTMD---RILYESQR-QGRISFYMtnyGEEGTHVGSAAALDNTDLVFGQYREAGVLMY 166
Cdd:PLN02269  21 PSRTVETSKQELVDFFRDMYLMRRMEiaaDSLYKAKLiRGFCHLYD---GQEAVAVGMEAAITKEDAIITAYRDHCTHLG 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548403    167 RD-YPLELFmAQCYGNIS--DLGKGRQMpvHYGCKERHFVTISSPLATQIPQAVGAAYAAKRANANRVVICYFGEGAASE 243
Cdd:PLN02269  98 RGgTVLEVF-AELMGRKDgcSRGKGGSM--HFYKKDANFYGGHGIVGAQVPLGAGLAFAQKYNKEENVAFALYGDGAANQ 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548403    244 GDAHAGFNFAATLECPIIFFCRNNGYAISTPT------SEQY-RGDGIaargPGygimsIRVDGNDVFAVYNATKEARRR 316
Cdd:PLN02269 175 GQLFEALNIAALWDLPVIFVCENNHYGMGTAEwraaksPAYYkRGDYV----PG-----LKVDGMDVLAVKQACKFAKEH 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548403    317 AVAeNQPFLIEAMTYRIGHHSTSDDSSAYRSVDEVNYWDKQDHPISRLRHYLLSQGWWDEEQEKAWRKQSRRKVMEAFEQ 396
Cdd:PLN02269 246 ALS-NGPIVLEMDTYRYHGHSMSDPGSTYRTRDEISGVRQERDPIERVRKLLLAHELATEAELKDIEKEIRKEVDDAVAK 324
                        330
                 ....*....|....*...
gi 548403    397 AERKPKPNPNLLFSDVYQ 414
Cdd:PLN02269 325 AKESPMPDPSELFTNVYV 342
 
Name Accession Description Interval E-value
AcoA COG1071
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ...
80-429 9.47e-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: 429.18  E-value: 9.47e-150
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548403    80 RVMDRQGqiiNPSEDPHLPKEKVLKLYKSMTLLNTMDRILYESQRQGRISFYMTNYGEEGTHVGSAAALDNTDLVFGQYR 159
Cdd:COG1071   3 QVLDPDG---TEAALPDLSKEELLELYRDMLLIRRFEERALALQRQGKIGFYHLSIGQEAAQVGAAAALRPGDWIFPTYR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548403   160 EAGVLMYRDYPLELFMAQCYGNISDLGKGRQMPVHYGCKERHFVTISSPLATQIPQAVGAAYAAKRANANRVVICYFGEG 239
Cdd:COG1071  80 DHGHALARGVDPKELMAELFGKATGPSKGRGGSMHFFDKELNFLGGSGIVGGQLPHAVGAALAAKLRGEDEVAVAFFGDG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548403   240 AASEGDAHAGFNFAATLECPIIFFCRNNGYAISTPTSEQYRGDGIAARGPGYGIMSIRVDGNDVFAVYNATKEARRRAVA 319
Cdd:COG1071 160 ATSEGDFHEALNFAAVWKLPVVFVCENNGYAISTPVERQTAVETIADRAAGYGIPGVRVDGNDVLAVYAAVKEAVERARA 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548403   320 ENQPFLIEAMTYRIGHHSTSDDSSAYRSVDEVNYWDKQDhPISRLRHYLLSQGWWDEEQEKAWRKQSRRKVMEAFEQAER 399
Cdd:COG1071 240 GEGPTLIEAKTYRLGGHSTSDDPTRYRTKEEVEEWRERD-PIERLRAYLLEEGLLTEEELEAIEAEAKAEVEEAVEFAEA 318
                       330       340       350
                ....*....|....*....|....*....|
gi 548403   400 KPKPNPNLLFSDVYQEMPAQLRKQQESLAR 429
Cdd:COG1071 319 SPEPDPEELFDDVYAEPPPHLAEQRAELAA 348
TPP_E1_PDC_ADC_BCADC cd02000
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ...
105-397 2.01e-147

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: 421.13  E-value: 2.01e-147
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548403   105 LYKSMTLLNTMDRILYESQRQGRIS-FYMTNYGEEGTHVGSAAALDNTDLVFGQYREAGVLMYRDYPLELFMAQCYGNIS 183
Cdd:cd02000   1 LYRTMVLIRRFDERLLELYRQGKIGgFYHLSIGQEAVAVGVAAALRPGDWVFPTYRDHGHALARGVDLKEMLAELFGKET 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548403   184 DLGKGRQMPVHYGCKERHFVTISSPLATQIPQAVGAAYAAKRANANRVVICYFGEGAASEGDAHAGFNFAATLECPIIFF 263
Cdd:cd02000  81 GPCKGRGGSMHIGDKEKNFFGGNGIVGGQVPLAAGAALALKYRGEDRVAVCFFGDGATNEGDFHEALNFAALWKLPVIFV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548403   264 CRNNGYAISTPTSEQYRGDGIAARGPGYGIMSIRVDGNDVFAVYNATKEARRRAVAENQPFLIEAMTYRIGHHSTSDDSS 343
Cdd:cd02000 161 CENNGYAISTPTSRQTAGTSIADRAAAYGIPGIRVDGNDVLAVYEAAKEAVERARAGGGPTLIEAVTYRLGGHSTSDDPS 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 548403   344 AYRSVDEVNYWDKQDhPISRLRHYLLSQGWWDEEQEKAWRKQSRRKVMEAFEQA 397
Cdd:cd02000 241 RYRTKEEVEEWKKRD-PILRLRKYLIEAGILTEEELAAIEAEVKAEVEEAVEFA 293
E1_dh pfam00676
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ...
106-405 5.75e-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: 400.16  E-value: 5.75e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548403     106 YKSMTLLNTMDRILYESQRQGRISFYMTNYGEEGTHVGSAAALDNTDLVFGQYREAGVLMYRDYPLELFMAQCYGNISDl 185
Cdd:pfam00676   1 RRMMTLRRMEDARDALYKRQGIRGFYHLYAGQEAAQVGIAAALEPGDYIIPGYRDHGNLLARGLSLEEIFAELYGRVAK- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548403     186 GKGRQMPVHYGCKERHFVTISSPLATQIPQAVGAAYAAKRANANRVVICYFGEGAASEGDAHAGFNFAATLECPIIFFCR 265
Cdd:pfam00676  80 GKGGSMHGYYGAKGNRFYGGNGILGAQVPLGAGIALAAKYRGKKEVAITLYGDGAANQGDFFEGLNFAALWKLPVIFVCE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548403     266 NNGYAISTPTSEQYRGDGIAARGPGYGIMSIRVDGNDVFAVYNATKEARRRAVAENQPFLIEAMTYRIGHHSTSDDSSAY 345
Cdd:pfam00676 160 NNQYGISTPAERASASTTYADRARGYGIPGLHVDGMDPLAVYQASKFAAERARTGKGPFLIELVTYRYGGHSMSDDPSTY 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 548403     346 RSVDEVNYWDKQDHPISRLRHYLLSQGWWDEEQEKAWRKQSRRKVMEAFEQAERKPKPNP 405
Cdd:pfam00676 240 RTRDEYEEVRKKKDPIQRFKEHLVSKGVWSEEELKAIEKEVRKEVEEAFKKAESAPEPHP 299
PDH_E1_alph_x TIGR03181
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the ...
77-427 2.47e-122

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: 359.54  E-value: 2.47e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548403      77 PIYRVMDRQGQIINPSEDPHLPKEKVLKLYKSMTLLNTMDRILYESQRQGRISFYMTNYGEEGTHVGSAAALDNTDLVFG 156
Cdd:TIGR03181   1 ELVQVLDEDGNVVDPEPAPDLSDEELVELYRDMVLTRRFDTKALALQRQGRLGTYAPNLGQEAAQVGSALALRKDDWVFP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548403     157 QYREAGVLMYRDYPLELFMAQCYGNIsdlgKGRQMPVhygckERHFVTISSPLATQIPQAVGAAYAAKRANANRVVICYF 236
Cdd:TIGR03181  81 SYRDHAAMLARGVPLVEILLYWRGDE----RGSWDPE-----GVNILPPNIPIGTQYLHAAGVAYALKLRGEDNVAVTYF 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548403     237 GEGAASEGDAHAGFNFAATLECPIIFFCRNNGYAISTPTSEQYRGDGIAARGPGYGIMSIRVDGNDVFAVYNATKEARRR 316
Cdd:TIGR03181 152 GDGGTSEGDFYEALNFAGVFKAPVVFFVQNNQWAISVPRSKQTAAPTLAQKAIAYGIPGVQVDGNDVLAVYAVTKEAVER 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548403     317 AVAENQPFLIEAMTYRIGHHSTSDDSSAYRSVDEVNYWDKQDhPISRLRHYLLSQGWWDEEQEKAWRKQSRRKVMEAFEQ 396
Cdd:TIGR03181 232 ARSGGGPTLIEAVTYRLGPHTTADDPTRYRTKEEEEEWRKKD-PILRLRKYLERKGLWDEEQEEALEEEAEAEVAEAVAE 310
                         330       340       350
                  ....*....|....*....|....*....|.
gi 548403     397 AERKPKPNPNLLFSDVYQEMPAQLRKQQESL 427
Cdd:TIGR03181 311 ALALPPPPVDDIFDHVYAELPPELEEQRAEL 341
PLN02269 PLN02269
Pyruvate dehydrogenase E1 component subunit alpha
91-414 4.44e-42

Pyruvate dehydrogenase E1 component subunit alpha


Pssm-ID: 215152 [Multi-domain]  Cd Length: 362  Bit Score: 152.56  E-value: 4.44e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548403     91 PSEDPHLPKEKVLKLYKSMTLLNTMD---RILYESQR-QGRISFYMtnyGEEGTHVGSAAALDNTDLVFGQYREAGVLMY 166
Cdd:PLN02269  21 PSRTVETSKQELVDFFRDMYLMRRMEiaaDSLYKAKLiRGFCHLYD---GQEAVAVGMEAAITKEDAIITAYRDHCTHLG 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548403    167 RD-YPLELFmAQCYGNIS--DLGKGRQMpvHYGCKERHFVTISSPLATQIPQAVGAAYAAKRANANRVVICYFGEGAASE 243
Cdd:PLN02269  98 RGgTVLEVF-AELMGRKDgcSRGKGGSM--HFYKKDANFYGGHGIVGAQVPLGAGLAFAQKYNKEENVAFALYGDGAANQ 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548403    244 GDAHAGFNFAATLECPIIFFCRNNGYAISTPT------SEQY-RGDGIaargPGygimsIRVDGNDVFAVYNATKEARRR 316
Cdd:PLN02269 175 GQLFEALNIAALWDLPVIFVCENNHYGMGTAEwraaksPAYYkRGDYV----PG-----LKVDGMDVLAVKQACKFAKEH 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548403    317 AVAeNQPFLIEAMTYRIGHHSTSDDSSAYRSVDEVNYWDKQDHPISRLRHYLLSQGWWDEEQEKAWRKQSRRKVMEAFEQ 396
Cdd:PLN02269 246 ALS-NGPIVLEMDTYRYHGHSMSDPGSTYRTRDEISGVRQERDPIERVRKLLLAHELATEAELKDIEKEIRKEVDDAVAK 324
                        330
                 ....*....|....*...
gi 548403    397 AERKPKPNPNLLFSDVYQ 414
Cdd:PLN02269 325 AKESPMPDPSELFTNVYV 342
odpA CHL00149
pyruvate dehydrogenase E1 component alpha subunit; Reviewed
97-413 2.64e-30

pyruvate dehydrogenase E1 component alpha subunit; Reviewed


Pssm-ID: 177069 [Multi-domain]  Cd Length: 341  Bit Score: 119.97  E-value: 2.64e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548403     97 LPKEKVLKLYKSMTLLNTMDRILYESQRQGRISFYMTNY-GEEGTHVGSAAALDNTDLVFGQYREAGVLMYRDYPLELFM 175
Cdd:CHL00149  17 INSMWLLVLYEDMLLGRNFEDMCAQMYYRGKMFGFVHLYnGQEAVSTGVIKLLAETDYVCSTYRDHVHALSKGVPPKNVM 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548403    176 AQCYGNISDLGKGRQMPVHYGCKERHFVTISSPLATQIPQAVGAAYAA-------KRANANRVVICYFGEGAASEGDAHA 248
Cdd:CHL00149  97 AELFGKETGCSRGRGGSMHIFSAPHNFLGGFAFIGEGIPIALGAAFQSiyrqqvlKEVQPLRVTACFFGDGTTNNGQFFE 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548403    249 GFNFAATLECPIIFFCRNNGYAISTPTSEQYRGDGIAARGPGYGIMSIRVDGNDVFAVYNATKEARRRAVAENQPFLIEA 328
Cdd:CHL00149 177 CLNMAVLWKLPIIFVVENNQWAIGMAHHRSTSIPEIHKKAEAFGLPGIEVDGMDVLAVREVAKEAVERARQGDGPTLIEA 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548403    329 MTYRIGHHSTSDDSSaYRSVDEVNYWDKQDhPISRLRHYLLSQGWWDEEQEKAWRKQSRRKVMEAFEQAERKPKPNPNLL 408
Cdd:CHL00149 257 LTYRFRGHSLADPDE-LRSKQEKEAWVARD-PIKKLKSYIIDNELASQKELNKIQREVKIEIEQAVQFAISSPEPNISDL 334

                 ....*
gi 548403    409 FSDVY 413
Cdd:CHL00149 335 KKYLF 339
PLN02374 PLN02374
pyruvate dehydrogenase (acetyl-transferring)
17-413 4.84e-29

pyruvate dehydrogenase (acetyl-transferring)


Pssm-ID: 215213 [Multi-domain]  Cd Length: 433  Bit Score: 118.12  E-value: 4.84e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548403     17 LSQAALLLLRQPGARGLARSHPPRQQQqFSSLDDKPQFPGASAEFIDKLEFIQPNVISGIPIYRVMD--RQGQIINPSED 94
Cdd:PLN02374   2 AAAFAATSLLVPVPARSSRDDAPSSPL-RGALKRSSAFTGSTSKLSSLRGLNAANGRRRSTVVAVSAvvKEKNSKASASD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548403     95 PHLPKEKVLKLYKSMTLLNTMDRILYESQRQGRISFYMTNY-GEEGTHVGSAAALDNTDLVFGQYREAGVLMYRDYPLEL 173
Cdd:PLN02374  81 LLVTREEGLELYEDMVLGRSFEDMCAQMYYRGKMFGFVHLYnGQEAVSTGFIKLLKKDDSVVSTYRDHVHALSKGVPARA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548403    174 FMAQCYGNISDLGKGRQMPVHYGCKERHFVTISSPLATQIPQAVGAAYAA-------KRANANRVVICYFGEGAASEGDA 246
Cdd:PLN02374 161 VMSELFGKATGCCRGQGGSMHMFSKEHNLLGGFAFIGEGIPVATGAAFSSkyrrevlKEESCDDVTLAFFGDGTCNNGQF 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548403    247 HAGFNFAATLECPIIFFCRNNGYAISTPTSEQYRGDGIAARGPGYGIMSIRVDGNDVFAVYNATKEARRRAVAENQPFLI 326
Cdd:PLN02374 241 FECLNMAALWKLPIVFVVENNLWAIGMSHLRATSDPEIWKKGPAFGMPGVHVDGMDVLKVREVAKEAIERARRGEGPTLV 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548403    327 EAMTYRIGHHSTSDDSSaYRSVDEVNYWDKQDhPISRLRHYLLSQGWWDEEQEKAWRKQSRRKVMEAFEQAERKPKPNPN 406
Cdd:PLN02374 321 ECETYRFRGHSLADPDE-LRDPAEKAHYAARD-PIAALKKYLIENGLATEAELKAIEKKIDEVVEDAVEFADASPLPPRS 398

                 ....*..
gi 548403    407 LLFSDVY 413
Cdd:PLN02374 399 QLLENVF 405
TPP_enzymes cd00568
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ...
188-330 1.92e-13

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: 68.05  E-value: 1.92e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548403   188 GRQMPVHYGCKERHFVTISSPLATQIPQAVGAAYAAKranaNRVVICYFGEGAASEGdaHAGFNFAATLECPIIFFCRNN 267
Cdd:cd00568  27 AYRYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAAP----DRPVVCIAGDGGFMMT--GQELATAVRYGLPVIVVVFNN 100
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 548403   268 GYAISTPTSEQYRGDG-----------IAARGPGYGIMSIRVDGNDVFavynatKEARRRAVAENQPFLIEAMT 330
Cdd:cd00568 101 GGYGTIRMHQEAFYGGrvsgtdlsnpdFAALAEAYGAKGVRVEDPEDL------EAALAEALAAGGPALIEVKT 168
TPP_TK cd02012
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ...
179-337 2.05e-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: 49.04  E-value: 2.05e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548403   179 YGNISDLGKGRQ----MPVHYGCKERHFVTISS-PLATQIPQAVGAAYAAKRANANRVVICYFGEGAASEGDAHAGFNFA 253
Cdd:cd02012  72 YLPEEDLKTFRQlgsrLPGHPEYGLTPGVEVTTgSLGQGLSVAVGMALAEKLLGFDYRVYVLLGDGELQEGSVWEAASFA 151
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548403   254 ATLEC-PIIFFCRNNGYAISTPTSEQYRGDGIAARGPGYGIMSIRVDGNDVFAVYNATKEARRravAENQPFLIEAMTyR 332
Cdd:cd02012 152 GHYKLdNLIAIVDSNRIQIDGPTDDILFTEDLAKKFEAFGWNVIEVDGHDVEEILAALEEAKK---SKGKPTLIIAKT-I 227

                ....*
gi 548403   333 IGHHS 337
Cdd:cd02012 228 KGKGV 232
PRK05899 PRK05899
transketolase; Reviewed
232-335 3.46e-05

transketolase; Reviewed


Pssm-ID: 235639 [Multi-domain]  Cd Length: 586  Bit Score: 46.28  E-value: 3.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548403    232 VICyfGEGAASEGDAHAGFNFAATLEC-PIIFFCRNNGYAISTPTSEQYRGDgIAARGPGYGIMSIRVDGNDVFAVYNAT 310
Cdd:PRK05899 155 VLC--GDGDLMEGISHEACSLAGHLKLgNLIVIYDDNRISIDGPTEGWFTED-VKKRFEAYGWHVIEVDGHDVEAIDAAI 231
                         90       100
                 ....*....|....*....|....*
gi 548403    311 KEARrravAENQPFLIEAMTyRIGH 335
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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