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Conserved domains on  [gi|2304497843|ref|WP_260465209|]
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thiamine pyrophosphate-dependent enzyme, partial [Stutzerimonas stutzeri]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AcoA super family cl43324
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ...
1-119 2.00e-46

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


The actual alignment was detected with superfamily member COG1071:

Pssm-ID: 440689 [Multi-domain]  Cd Length: 348  Bit Score: 152.60  E-value: 2.00e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304497843   1 PGVFVESNDPDGVFRAAGEAIERARAGGGPTLIEIETYRLAGHFMGD-GETYRPEGEKDGLMKKDPIPGYRQRLIDEGVM 79
Cdd:COG1071   214 PGVRVDGNDVLAVYAAVKEAVERARAGEGPTLIEAKTYRLGGHSTSDdPTRYRTKEEVEEWRERDPIERLRAYLLEEGLL 293
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2304497843  80 SEAQAQDIEARARGRIDEAVQFARESPYPRPEEALEHVFV 119
Cdd:COG1071   294 TEEELEAIEAEAKAEVEEAVEFAEASPEPDPEELFDDVYA 333
 
Name Accession Description Interval E-value
AcoA COG1071
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ...
1-119 2.00e-46

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: 152.60  E-value: 2.00e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304497843   1 PGVFVESNDPDGVFRAAGEAIERARAGGGPTLIEIETYRLAGHFMGD-GETYRPEGEKDGLMKKDPIPGYRQRLIDEGVM 79
Cdd:COG1071   214 PGVRVDGNDVLAVYAAVKEAVERARAGEGPTLIEAKTYRLGGHSTSDdPTRYRTKEEVEEWRERDPIERLRAYLLEEGLL 293
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2304497843  80 SEAQAQDIEARARGRIDEAVQFARESPYPRPEEALEHVFV 119
Cdd:COG1071   294 TEEELEAIEAEAKAEVEEAVEFAEASPEPDPEELFDDVYA 333
TPP_E1_PDC_ADC_BCADC cd02000
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ...
1-102 1.31e-38

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: 131.08  E-value: 1.31e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304497843   1 PGVFVESNDPDGVFRAAGEAIERARAGGGPTLIEIETYRLAGHFM-GDGETYRPEGEKDGLMKKDPIPGYRQRLIDEGVM 79
Cdd:cd02000   191 PGIRVDGNDVLAVYEAAKEAVERARAGGGPTLIEAVTYRLGGHSTsDDPSRYRTKEEVEEWKKRDPILRLRKYLIEAGIL 270
                          90       100
                  ....*....|....*....|...
gi 2304497843  80 SEAQAQDIEARARGRIDEAVQFA 102
Cdd:cd02000   271 TEEELAAIEAEVKAEVEEAVEFA 293
PDH_E1_alph_y TIGR03182
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the ...
1-119 2.09e-32

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: 274473 [Multi-domain]  Cd Length: 315  Bit Score: 115.36  E-value: 2.09e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304497843   1 PGVFVESNDPDGVFRAAGEAIERARAGGGPTLIEIETYRLAGHFMGDGETYRPEGEKDGLMKKDPIPGYRQRLIDEGVMS 80
Cdd:TIGR03182 197 PGERVDGMDVLAVREAAKEAVERARSGKGPILLEMKTYRFRGHSMSDPAKYRSKEEVEEWRKRDPIEKLKARLIEQGIAS 276
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2304497843  81 EAQAQDIEARARGRIDEAVQFARESPYPRPEEALEHVFV 119
Cdd:TIGR03182 277 EEELKEIDKEVRAEVEEAVEFAENSPEPPVEELYTDVYA 315
E1_dh pfam00676
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ...
1-111 3.47e-32

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: 114.34  E-value: 3.47e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304497843   1 PGVFVESNDPDGVFRAAGEAIERARAGGGPTLIEIETYRLAGHFMGD-GETYRPEGEKDGLMK-KDPIPGYRQRLIDEGV 78
Cdd:pfam00676 188 PGLHVDGMDPLAVYQASKFAAERARTGKGPFLIELVTYRYGGHSMSDdPSTYRTRDEYEEVRKkKDPIQRFKEHLVSKGV 267
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2304497843  79 MSEAQAQDIEARARGRIDEAVQFARESPYPRPE 111
Cdd:pfam00676 268 WSEEELKAIEKEVRKEVEEAFKKAESAPEPHPE 300
PLN02374 PLN02374
pyruvate dehydrogenase (acetyl-transferring)
1-118 7.05e-26

pyruvate dehydrogenase (acetyl-transferring)


Pssm-ID: 215213 [Multi-domain]  Cd Length: 433  Bit Score: 99.63  E-value: 7.05e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304497843   1 PGVFVESNDPDGVFRAAGEAIERARAGGGPTLIEIETYRLAGHFMGDGETYRPEGEKDGLMKKDPIPGYRQRLIDEGVMS 80
Cdd:PLN02374  288 PGVHVDGMDVLKVREVAKEAIERARRGEGPTLVECETYRFRGHSLADPDELRDPAEKAHYAARDPIAALKKYLIENGLAT 367
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2304497843  81 EAQAQDIEARARGRIDEAVQFARESPYPRPEEALEHVF 118
Cdd:PLN02374  368 EAELKAIEKKIDEVVEDAVEFADASPLPPRSQLLENVF 405
 
Name Accession Description Interval E-value
AcoA COG1071
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ...
1-119 2.00e-46

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: 152.60  E-value: 2.00e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304497843   1 PGVFVESNDPDGVFRAAGEAIERARAGGGPTLIEIETYRLAGHFMGD-GETYRPEGEKDGLMKKDPIPGYRQRLIDEGVM 79
Cdd:COG1071   214 PGVRVDGNDVLAVYAAVKEAVERARAGEGPTLIEAKTYRLGGHSTSDdPTRYRTKEEVEEWRERDPIERLRAYLLEEGLL 293
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2304497843  80 SEAQAQDIEARARGRIDEAVQFARESPYPRPEEALEHVFV 119
Cdd:COG1071   294 TEEELEAIEAEAKAEVEEAVEFAEASPEPDPEELFDDVYA 333
TPP_E1_PDC_ADC_BCADC cd02000
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ...
1-102 1.31e-38

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: 131.08  E-value: 1.31e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304497843   1 PGVFVESNDPDGVFRAAGEAIERARAGGGPTLIEIETYRLAGHFM-GDGETYRPEGEKDGLMKKDPIPGYRQRLIDEGVM 79
Cdd:cd02000   191 PGIRVDGNDVLAVYEAAKEAVERARAGGGPTLIEAVTYRLGGHSTsDDPSRYRTKEEVEEWKKRDPILRLRKYLIEAGIL 270
                          90       100
                  ....*....|....*....|...
gi 2304497843  80 SEAQAQDIEARARGRIDEAVQFA 102
Cdd:cd02000   271 TEEELAAIEAEVKAEVEEAVEFA 293
PDH_E1_alph_y TIGR03182
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the ...
1-119 2.09e-32

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: 274473 [Multi-domain]  Cd Length: 315  Bit Score: 115.36  E-value: 2.09e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304497843   1 PGVFVESNDPDGVFRAAGEAIERARAGGGPTLIEIETYRLAGHFMGDGETYRPEGEKDGLMKKDPIPGYRQRLIDEGVMS 80
Cdd:TIGR03182 197 PGERVDGMDVLAVREAAKEAVERARSGKGPILLEMKTYRFRGHSMSDPAKYRSKEEVEEWRKRDPIEKLKARLIEQGIAS 276
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2304497843  81 EAQAQDIEARARGRIDEAVQFARESPYPRPEEALEHVFV 119
Cdd:TIGR03182 277 EEELKEIDKEVRAEVEEAVEFAENSPEPPVEELYTDVYA 315
E1_dh pfam00676
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ...
1-111 3.47e-32

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: 114.34  E-value: 3.47e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304497843   1 PGVFVESNDPDGVFRAAGEAIERARAGGGPTLIEIETYRLAGHFMGD-GETYRPEGEKDGLMK-KDPIPGYRQRLIDEGV 78
Cdd:pfam00676 188 PGLHVDGMDPLAVYQASKFAAERARTGKGPFLIELVTYRYGGHSMSDdPSTYRTRDEYEEVRKkKDPIQRFKEHLVSKGV 267
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2304497843  79 MSEAQAQDIEARARGRIDEAVQFARESPYPRPE 111
Cdd:pfam00676 268 WSEEELKAIEKEVRKEVEEAFKKAESAPEPHPE 300
PLN02374 PLN02374
pyruvate dehydrogenase (acetyl-transferring)
1-118 7.05e-26

pyruvate dehydrogenase (acetyl-transferring)


Pssm-ID: 215213 [Multi-domain]  Cd Length: 433  Bit Score: 99.63  E-value: 7.05e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304497843   1 PGVFVESNDPDGVFRAAGEAIERARAGGGPTLIEIETYRLAGHFMGDGETYRPEGEKDGLMKKDPIPGYRQRLIDEGVMS 80
Cdd:PLN02374  288 PGVHVDGMDVLKVREVAKEAIERARRGEGPTLVECETYRFRGHSLADPDELRDPAEKAHYAARDPIAALKKYLIENGLAT 367
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2304497843  81 EAQAQDIEARARGRIDEAVQFARESPYPRPEEALEHVF 118
Cdd:PLN02374  368 EAELKAIEKKIDEVVEDAVEFADASPLPPRSQLLENVF 405
odpA CHL00149
pyruvate dehydrogenase E1 component alpha subunit; Reviewed
1-118 1.05e-23

pyruvate dehydrogenase E1 component alpha subunit; Reviewed


Pssm-ID: 177069 [Multi-domain]  Cd Length: 341  Bit Score: 93.01  E-value: 1.05e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304497843   1 PGVFVESNDPDGVFRAAGEAIERARAGGGPTLIEIETYRLAGHFMGDGETYRPEGEKDGLMKKDPIPGYRQRLIDEGVMS 80
Cdd:CHL00149  222 PGIEVDGMDVLAVREVAKEAVERARQGDGPTLIEALTYRFRGHSLADPDELRSKQEKEAWVARDPIKKLKSYIIDNELAS 301
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2304497843  81 EAQAQDIEARARGRIDEAVQFARESPYPRPEEALEHVF 118
Cdd:CHL00149  302 QKELNKIQREVKIEIEQAVQFAISSPEPNISDLKKYLF 339
PLN02269 PLN02269
Pyruvate dehydrogenase E1 component subunit alpha
1-119 2.33e-19

Pyruvate dehydrogenase E1 component subunit alpha


Pssm-ID: 215152 [Multi-domain]  Cd Length: 362  Bit Score: 81.30  E-value: 2.33e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304497843   1 PGVFVESNDPDGVFRAAGEAIERARAGGgPTLIEIETYRLAGHFMGD-GETYRPEGEKDGL-MKKDPIPGYRQRLIDEGV 78
Cdd:PLN02269  223 PGLKVDGMDVLAVKQACKFAKEHALSNG-PIVLEMDTYRYHGHSMSDpGSTYRTRDEISGVrQERDPIERVRKLLLAHEL 301
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2304497843  79 MSEAQAQDIEARARGRIDEAVQFARESPYPRPEEALEHVFV 119
Cdd:PLN02269  302 ATEAELKDIEKEIRKEVDDAVAKAKESPMPDPSELFTNVYV 342
 
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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