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Conserved domains on  [gi|2282543696|ref|WP_256868291|]
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pyruvate dehydrogenase (acetyl-transferring) E1 component subunit alpha [Candidatus Entotheonella palauensis]

Protein Classification

thiamine pyrophosphate-dependent enzyme( domain architecture ID 22)

thiamine pyrophosphate (TPP)-dependent enzyme uses thiamine pyrophosphate as a cofactor to catalyze various reactions including reversible decarboxylation

CATH:  3.40.50.1220
Gene Ontology:  GO:0030976|GO:0003824
PubMed:  12735696|15514159
SCOP:  3001790

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TPP_enzymes super family cl01629
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ...
1-305 2.43e-162

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.


The actual alignment was detected with superfamily member TIGR03182:

Pssm-ID: 470272 [Multi-domain]  Cd Length: 315  Bit Score: 454.34  E-value: 2.43e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282543696   1 MIRIRRFEEKAAELYSATKIRGFLHLYDGEEAIAVGVMESLTPDDAVVATYREHGHALARGIDAGAIMAEMYGKQEGCSR 80
Cdd:TIGR03182  11 MLLIRRFEEKAGQLYGMGKIGGFCHLYIGQEAVAVGLIAALKPDDYVITSYRDHGHALARGVPPKEVMAELTGRETGCSK 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282543696  81 GRGGSMHLFDDKTRFYGGNAIVGGGLPVAVGLALADRIQGLPRVTCCFFGDGAVAEGEFHESMNLAALWRLPVLFVCENN 160
Cdd:TIGR03182  91 GKGGSMHMFDREKNFYGGHGIVGAQVPLATGLAFANKYRGNDNVTACFFGDGAANQGQFYESFNMAALWKLPVIFVIENN 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282543696 161 LYAMGTSLTRSESEIHLTTKAESYAVPALAVDGMDVLAVEQAAQNAAAAIRAGEGPYFLEYRTYRFRAHSMFDAQLYREK 240
Cdd:TIGR03182 171 LYAMGTAVERSSSVTDLYKRGESFGIPGERVDGMDVLAVREAAKEAVERARSGKGPILLEMKTYRFRGHSMSDPAKYRSK 250
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2282543696 241 AEVEAWKEHGPIVGFTQFLKGQGILDDADVQQLESQVAAEVEGAVAFAEKGTWEPVEDLTRFVYS 305
Cdd:TIGR03182 251 EEVEEWRKRDPIEKLKARLIEQGIASEEELKEIDKEVRAEVEEAVEFAENSPEPPVEELYTDVYA 315
 
Name Accession Description Interval E-value
PDH_E1_alph_y TIGR03182
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the ...
1-305 2.43e-162

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: 454.34  E-value: 2.43e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282543696   1 MIRIRRFEEKAAELYSATKIRGFLHLYDGEEAIAVGVMESLTPDDAVVATYREHGHALARGIDAGAIMAEMYGKQEGCSR 80
Cdd:TIGR03182  11 MLLIRRFEEKAGQLYGMGKIGGFCHLYIGQEAVAVGLIAALKPDDYVITSYRDHGHALARGVPPKEVMAELTGRETGCSK 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282543696  81 GRGGSMHLFDDKTRFYGGNAIVGGGLPVAVGLALADRIQGLPRVTCCFFGDGAVAEGEFHESMNLAALWRLPVLFVCENN 160
Cdd:TIGR03182  91 GKGGSMHMFDREKNFYGGHGIVGAQVPLATGLAFANKYRGNDNVTACFFGDGAANQGQFYESFNMAALWKLPVIFVIENN 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282543696 161 LYAMGTSLTRSESEIHLTTKAESYAVPALAVDGMDVLAVEQAAQNAAAAIRAGEGPYFLEYRTYRFRAHSMFDAQLYREK 240
Cdd:TIGR03182 171 LYAMGTAVERSSSVTDLYKRGESFGIPGERVDGMDVLAVREAAKEAVERARSGKGPILLEMKTYRFRGHSMSDPAKYRSK 250
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2282543696 241 AEVEAWKEHGPIVGFTQFLKGQGILDDADVQQLESQVAAEVEGAVAFAEKGTWEPVEDLTRFVYS 305
Cdd:TIGR03182 251 EEVEEWRKRDPIEKLKARLIEQGIASEEELKEIDKEVRAEVEEAVEFAENSPEPPVEELYTDVYA 315
AcoA COG1071
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ...
1-306 3.00e-140

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: 399.90  E-value: 3.00e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282543696   1 MIRIRRFEEKAAELYSATKIrGFLHLYDGEEAIAVGVMESLTPDDAVVATYREHGHALARGIDAGAIMAEMYGKQEGCSR 80
Cdd:COG1071    29 MLLIRRFEERALALQRQGKI-GFYHLSIGQEAAQVGAAAALRPGDWIFPTYRDHGHALARGVDPKELMAELFGKATGPSK 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282543696  81 GRGGSMHLFDDKTRFYGGNAIVGGGLPVAVGLALADRIQGLPRVTCCFFGDGAVAEGEFHESMNLAALWRLPVLFVCENN 160
Cdd:COG1071   108 GRGGSMHFFDKELNFLGGSGIVGGQLPHAVGAALAAKLRGEDEVAVAFFGDGATSEGDFHEALNFAAVWKLPVVFVCENN 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282543696 161 LYAMGTSLTRSESEIHLTTKAESYAVPALAVDGMDVLAVEQAAQNAAAAIRAGEGPYFLEYRTYRFRAHSMFD-AQLYRE 239
Cdd:COG1071   188 GYAISTPVERQTAVETIADRAAGYGIPGVRVDGNDVLAVYAAVKEAVERARAGEGPTLIEAKTYRLGGHSTSDdPTRYRT 267
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2282543696 240 KAEVEAWKEHGPIVGFTQFLKGQGILDDADVQQLESQVAAEVEGAVAFAEKGTWEPVEDLTRFVYSE 306
Cdd:COG1071   268 KEEVEEWRERDPIERLRAYLLEEGLLTEEELEAIEAEAKAEVEEAVEFAEASPEPDPEELFDDVYAE 334
TPP_E1_PDC_ADC_BCADC cd02000
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ...
1-288 1.37e-128

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: 367.98  E-value: 1.37e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282543696   1 MIRIRRFEEKAAELYSATKIRGFLHLYDGEEAIAVGVMESLTPDDAVVATYREHGHALARGIDAGAIMAEMYGKQEGCSR 80
Cdd:cd02000     5 MVLIRRFDERLLELYRQGKIGGFYHLSIGQEAVAVGVAAALRPGDWVFPTYRDHGHALARGVDLKEMLAELFGKETGPCK 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282543696  81 GRGGSMHLFDDKTRFYGGNAIVGGGLPVAVGLALADRIQGLPRVTCCFFGDGAVAEGEFHESMNLAALWRLPVLFVCENN 160
Cdd:cd02000    85 GRGGSMHIGDKEKNFFGGNGIVGGQVPLAAGAALALKYRGEDRVAVCFFGDGATNEGDFHEALNFAALWKLPVIFVCENN 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282543696 161 LYAMGTSLTRSESEIHLTTKAESYAVPALAVDGMDVLAVEQAAQNAAAAIRAGEGPYFLEYRTYRFRAHSMF-DAQLYRE 239
Cdd:cd02000   165 GYAISTPTSRQTAGTSIADRAAAYGIPGIRVDGNDVLAVYEAAKEAVERARAGGGPTLIEAVTYRLGGHSTSdDPSRYRT 244
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 2282543696 240 KAEVEAWKEHGPIVGFTQFLKGQGILDDADVQQLESQVAAEVEGAVAFA 288
Cdd:cd02000   245 KEEVEEWKKRDPILRLRKYLIEAGILTEEELAAIEAEVKAEVEEAVEFA 293
odpA CHL00149
pyruvate dehydrogenase E1 component alpha subunit; Reviewed
1-306 6.70e-93

pyruvate dehydrogenase E1 component alpha subunit; Reviewed


Pssm-ID: 177069 [Multi-domain]  Cd Length: 341  Bit Score: 279.06  E-value: 6.70e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282543696   1 MIRIRRFEEKAAELYSATKIRGFLHLYDGEEAIAVGVMESLTPDDAVVATYREHGHALARGIDAGAIMAEMYGKQEGCSR 80
Cdd:CHL00149   29 MLLGRNFEDMCAQMYYRGKMFGFVHLYNGQEAVSTGVIKLLAETDYVCSTYRDHVHALSKGVPPKNVMAELFGKETGCSR 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282543696  81 GRGGSMHLFDDKTRFYGGNAIVGGGLPVAVGLALAD--RIQGLP-----RVTCCFFGDGAVAEGEFHESMNLAALWRLPV 153
Cdd:CHL00149  109 GRGGSMHIFSAPHNFLGGFAFIGEGIPIALGAAFQSiyRQQVLKevqplRVTACFFGDGTTNNGQFFECLNMAVLWKLPI 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282543696 154 LFVCENNLYAMGTSLTRSESEIHLTTKAESYAVPALAVDGMDVLAVEQAAQNAAAAIRAGEGPYFLEYRTYRFRAHSMFD 233
Cdd:CHL00149  189 IFVVENNQWAIGMAHHRSTSIPEIHKKAEAFGLPGIEVDGMDVLAVREVAKEAVERARQGDGPTLIEALTYRFRGHSLAD 268
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2282543696 234 AQLYREKAEVEAWKEHGPIVGFTQFLKGQGILDDADVQQLESQVAAEVEGAVAFAEKGTWEPVEDLTRFVYSE 306
Cdd:CHL00149  269 PDELRSKQEKEAWVARDPIKKLKSYIIDNELASQKELNKIQREVKIEIEQAVQFAISSPEPNISDLKKYLFAD 341
E1_dh pfam00676
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ...
1-289 4.75e-86

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: 260.34  E-value: 4.75e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282543696   1 MIRIRRFEEKAAELYSATKIRGFLHLYDGEEAIAVGVMESLTPDDAVVATYREHGHALARGIDAGAIMAEMYGKQEgcsR 80
Cdd:pfam00676   3 MMTLRRMEDARDALYKRQGIRGFYHLYAGQEAAQVGIAAALEPGDYIIPGYRDHGNLLARGLSLEEIFAELYGRVA---K 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282543696  81 GRGGSMHLFDD--KTRFYGGNAIVGGGLPVAVGLALADRIQGLPRVTCCFFGDGAVAEGEFHESMNLAALWRLPVLFVCE 158
Cdd:pfam00676  80 GKGGSMHGYYGakGNRFYGGNGILGAQVPLGAGIALAAKYRGKKEVAITLYGDGAANQGDFFEGLNFAALWKLPVIFVCE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282543696 159 NNLYAMGTSLTRSESEIHLTTKAESYAVPALAVDGMDVLAVEQAAQNAAAAIRAGEGPYFLEYRTYRFRAHSMFD-AQLY 237
Cdd:pfam00676 160 NNQYGISTPAERASASTTYADRARGYGIPGLHVDGMDPLAVYQASKFAAERARTGKGPFLIELVTYRYGGHSMSDdPSTY 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2282543696 238 REKAEVEA-WKEHGPIVGFTQFLKGQGILDDADVQQLESQVAAEVEGAVAFAE 289
Cdd:pfam00676 240 RTRDEYEEvRKKKDPIQRFKEHLVSKGVWSEEELKAIEKEVRKEVEEAFKKAE 292
 
Name Accession Description Interval E-value
PDH_E1_alph_y TIGR03182
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the ...
1-305 2.43e-162

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: 454.34  E-value: 2.43e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282543696   1 MIRIRRFEEKAAELYSATKIRGFLHLYDGEEAIAVGVMESLTPDDAVVATYREHGHALARGIDAGAIMAEMYGKQEGCSR 80
Cdd:TIGR03182  11 MLLIRRFEEKAGQLYGMGKIGGFCHLYIGQEAVAVGLIAALKPDDYVITSYRDHGHALARGVPPKEVMAELTGRETGCSK 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282543696  81 GRGGSMHLFDDKTRFYGGNAIVGGGLPVAVGLALADRIQGLPRVTCCFFGDGAVAEGEFHESMNLAALWRLPVLFVCENN 160
Cdd:TIGR03182  91 GKGGSMHMFDREKNFYGGHGIVGAQVPLATGLAFANKYRGNDNVTACFFGDGAANQGQFYESFNMAALWKLPVIFVIENN 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282543696 161 LYAMGTSLTRSESEIHLTTKAESYAVPALAVDGMDVLAVEQAAQNAAAAIRAGEGPYFLEYRTYRFRAHSMFDAQLYREK 240
Cdd:TIGR03182 171 LYAMGTAVERSSSVTDLYKRGESFGIPGERVDGMDVLAVREAAKEAVERARSGKGPILLEMKTYRFRGHSMSDPAKYRSK 250
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2282543696 241 AEVEAWKEHGPIVGFTQFLKGQGILDDADVQQLESQVAAEVEGAVAFAEKGTWEPVEDLTRFVYS 305
Cdd:TIGR03182 251 EEVEEWRKRDPIEKLKARLIEQGIASEEELKEIDKEVRAEVEEAVEFAENSPEPPVEELYTDVYA 315
AcoA COG1071
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ...
1-306 3.00e-140

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: 399.90  E-value: 3.00e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282543696   1 MIRIRRFEEKAAELYSATKIrGFLHLYDGEEAIAVGVMESLTPDDAVVATYREHGHALARGIDAGAIMAEMYGKQEGCSR 80
Cdd:COG1071    29 MLLIRRFEERALALQRQGKI-GFYHLSIGQEAAQVGAAAALRPGDWIFPTYRDHGHALARGVDPKELMAELFGKATGPSK 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282543696  81 GRGGSMHLFDDKTRFYGGNAIVGGGLPVAVGLALADRIQGLPRVTCCFFGDGAVAEGEFHESMNLAALWRLPVLFVCENN 160
Cdd:COG1071   108 GRGGSMHFFDKELNFLGGSGIVGGQLPHAVGAALAAKLRGEDEVAVAFFGDGATSEGDFHEALNFAAVWKLPVVFVCENN 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282543696 161 LYAMGTSLTRSESEIHLTTKAESYAVPALAVDGMDVLAVEQAAQNAAAAIRAGEGPYFLEYRTYRFRAHSMFD-AQLYRE 239
Cdd:COG1071   188 GYAISTPVERQTAVETIADRAAGYGIPGVRVDGNDVLAVYAAVKEAVERARAGEGPTLIEAKTYRLGGHSTSDdPTRYRT 267
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2282543696 240 KAEVEAWKEHGPIVGFTQFLKGQGILDDADVQQLESQVAAEVEGAVAFAEKGTWEPVEDLTRFVYSE 306
Cdd:COG1071   268 KEEVEEWRERDPIERLRAYLLEEGLLTEEELEAIEAEAKAEVEEAVEFAEASPEPDPEELFDDVYAE 334
TPP_E1_PDC_ADC_BCADC cd02000
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ...
1-288 1.37e-128

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: 367.98  E-value: 1.37e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282543696   1 MIRIRRFEEKAAELYSATKIRGFLHLYDGEEAIAVGVMESLTPDDAVVATYREHGHALARGIDAGAIMAEMYGKQEGCSR 80
Cdd:cd02000     5 MVLIRRFDERLLELYRQGKIGGFYHLSIGQEAVAVGVAAALRPGDWVFPTYRDHGHALARGVDLKEMLAELFGKETGPCK 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282543696  81 GRGGSMHLFDDKTRFYGGNAIVGGGLPVAVGLALADRIQGLPRVTCCFFGDGAVAEGEFHESMNLAALWRLPVLFVCENN 160
Cdd:cd02000    85 GRGGSMHIGDKEKNFFGGNGIVGGQVPLAAGAALALKYRGEDRVAVCFFGDGATNEGDFHEALNFAALWKLPVIFVCENN 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282543696 161 LYAMGTSLTRSESEIHLTTKAESYAVPALAVDGMDVLAVEQAAQNAAAAIRAGEGPYFLEYRTYRFRAHSMF-DAQLYRE 239
Cdd:cd02000   165 GYAISTPTSRQTAGTSIADRAAAYGIPGIRVDGNDVLAVYEAAKEAVERARAGGGPTLIEAVTYRLGGHSTSdDPSRYRT 244
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 2282543696 240 KAEVEAWKEHGPIVGFTQFLKGQGILDDADVQQLESQVAAEVEGAVAFA 288
Cdd:cd02000   245 KEEVEEWKKRDPILRLRKYLIEAGILTEEELAAIEAEVKAEVEEAVEFA 293
odpA CHL00149
pyruvate dehydrogenase E1 component alpha subunit; Reviewed
1-306 6.70e-93

pyruvate dehydrogenase E1 component alpha subunit; Reviewed


Pssm-ID: 177069 [Multi-domain]  Cd Length: 341  Bit Score: 279.06  E-value: 6.70e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282543696   1 MIRIRRFEEKAAELYSATKIRGFLHLYDGEEAIAVGVMESLTPDDAVVATYREHGHALARGIDAGAIMAEMYGKQEGCSR 80
Cdd:CHL00149   29 MLLGRNFEDMCAQMYYRGKMFGFVHLYNGQEAVSTGVIKLLAETDYVCSTYRDHVHALSKGVPPKNVMAELFGKETGCSR 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282543696  81 GRGGSMHLFDDKTRFYGGNAIVGGGLPVAVGLALAD--RIQGLP-----RVTCCFFGDGAVAEGEFHESMNLAALWRLPV 153
Cdd:CHL00149  109 GRGGSMHIFSAPHNFLGGFAFIGEGIPIALGAAFQSiyRQQVLKevqplRVTACFFGDGTTNNGQFFECLNMAVLWKLPI 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282543696 154 LFVCENNLYAMGTSLTRSESEIHLTTKAESYAVPALAVDGMDVLAVEQAAQNAAAAIRAGEGPYFLEYRTYRFRAHSMFD 233
Cdd:CHL00149  189 IFVVENNQWAIGMAHHRSTSIPEIHKKAEAFGLPGIEVDGMDVLAVREVAKEAVERARQGDGPTLIEALTYRFRGHSLAD 268
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2282543696 234 AQLYREKAEVEAWKEHGPIVGFTQFLKGQGILDDADVQQLESQVAAEVEGAVAFAEKGTWEPVEDLTRFVYSE 306
Cdd:CHL00149  269 PDELRSKQEKEAWVARDPIKKLKSYIIDNELASQKELNKIQREVKIEIEQAVQFAISSPEPNISDLKKYLFAD 341
PLN02269 PLN02269
Pyruvate dehydrogenase E1 component subunit alpha
1-305 1.71e-87

Pyruvate dehydrogenase E1 component subunit alpha


Pssm-ID: 215152 [Multi-domain]  Cd Length: 362  Bit Score: 266.19  E-value: 1.71e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282543696   1 MIRIRRFEEKAAELYSATKIRGFLHLYDGEEAIAVGVMESLTPDDAVVATYREHGHALARGIDAGAIMAEMYGKQEGCSR 80
Cdd:PLN02269   39 MYLMRRMEIAADSLYKAKLIRGFCHLYDGQEAVAVGMEAAITKEDAIITAYRDHCTHLGRGGTVLEVFAELMGRKDGCSR 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282543696  81 GRGGSMHLFDDKTRFYGGNAIVGGGLPVAVGLALADRIQGLPRVTCCFFGDGAVAEGEFHESMNLAALWRLPVLFVCENN 160
Cdd:PLN02269  119 GKGGSMHFYKKDANFYGGHGIVGAQVPLGAGLAFAQKYNKEENVAFALYGDGAANQGQLFEALNIAALWDLPVIFVCENN 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282543696 161 LYAMGTSLTRSeSEIHLTTKAESYaVPALAVDGMDVLAVEQAAQNAAAAIRAgEGPYFLEYRTYRFRAHSMFD-AQLYRE 239
Cdd:PLN02269  199 HYGMGTAEWRA-AKSPAYYKRGDY-VPGLKVDGMDVLAVKQACKFAKEHALS-NGPIVLEMDTYRYHGHSMSDpGSTYRT 275
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2282543696 240 KAEVEAWK-EHGPIVGFTQFLKGQGILDDADVQQLESQVAAEVEGAVAFAEKGTWEPVEDLTRFVYS 305
Cdd:PLN02269  276 RDEISGVRqERDPIERVRKLLLAHELATEAELKDIEKEIRKEVDDAVAKAKESPMPDPSELFTNVYV 342
PLN02374 PLN02374
pyruvate dehydrogenase (acetyl-transferring)
1-306 3.08e-86

pyruvate dehydrogenase (acetyl-transferring)


Pssm-ID: 215213 [Multi-domain]  Cd Length: 433  Bit Score: 265.27  E-value: 3.08e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282543696   1 MIRIRRFEEKAAELYSATKIRGFLHLYDGEEAIAVGVMESLTPDDAVVATYREHGHALARGIDAGAIMAEMYGKQEGCSR 80
Cdd:PLN02374   95 MVLGRSFEDMCAQMYYRGKMFGFVHLYNGQEAVSTGFIKLLKKDDSVVSTYRDHVHALSKGVPARAVMSELFGKATGCCR 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282543696  81 GRGGSMHLFDDKTRFYGGNAIVGGGLPVAVGLALADRIQ-------GLPRVTCCFFGDGAVAEGEFHESMNLAALWRLPV 153
Cdd:PLN02374  175 GQGGSMHMFSKEHNLLGGFAFIGEGIPVATGAAFSSKYRrevlkeeSCDDVTLAFFGDGTCNNGQFFECLNMAALWKLPI 254
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282543696 154 LFVCENNLYAMGTSLTRSESEIHLTTKAESYAVPALAVDGMDVLAVEQAAQNAAAAIRAGEGPYFLEYRTYRFRAHSMFD 233
Cdd:PLN02374  255 VFVVENNLWAIGMSHLRATSDPEIWKKGPAFGMPGVHVDGMDVLKVREVAKEAIERARRGEGPTLVECETYRFRGHSLAD 334
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2282543696 234 AQLYREKAEVEAWKEHGPIVGFTQFLKGQGILDDADVQQLESQVAAEVEGAVAFAEKGTWEPVEDLTRFVYSE 306
Cdd:PLN02374  335 PDELRDPAEKAHYAARDPIAALKKYLIENGLATEAELKAIEKKIDEVVEDAVEFADASPLPPRSQLLENVFAD 407
E1_dh pfam00676
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ...
1-289 4.75e-86

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: 260.34  E-value: 4.75e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282543696   1 MIRIRRFEEKAAELYSATKIRGFLHLYDGEEAIAVGVMESLTPDDAVVATYREHGHALARGIDAGAIMAEMYGKQEgcsR 80
Cdd:pfam00676   3 MMTLRRMEDARDALYKRQGIRGFYHLYAGQEAAQVGIAAALEPGDYIIPGYRDHGNLLARGLSLEEIFAELYGRVA---K 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282543696  81 GRGGSMHLFDD--KTRFYGGNAIVGGGLPVAVGLALADRIQGLPRVTCCFFGDGAVAEGEFHESMNLAALWRLPVLFVCE 158
Cdd:pfam00676  80 GKGGSMHGYYGakGNRFYGGNGILGAQVPLGAGIALAAKYRGKKEVAITLYGDGAANQGDFFEGLNFAALWKLPVIFVCE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282543696 159 NNLYAMGTSLTRSESEIHLTTKAESYAVPALAVDGMDVLAVEQAAQNAAAAIRAGEGPYFLEYRTYRFRAHSMFD-AQLY 237
Cdd:pfam00676 160 NNQYGISTPAERASASTTYADRARGYGIPGLHVDGMDPLAVYQASKFAAERARTGKGPFLIELVTYRYGGHSMSDdPSTY 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2282543696 238 REKAEVEA-WKEHGPIVGFTQFLKGQGILDDADVQQLESQVAAEVEGAVAFAE 289
Cdd:pfam00676 240 RTRDEYEEvRKKKDPIQRFKEHLVSKGVWSEEELKAIEKEVRKEVEEAFKKAE 292
PDH_E1_alph_x TIGR03181
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the ...
1-306 6.05e-73

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: 228.18  E-value: 6.05e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282543696   1 MIRIRRFEEKAAELYSATKIRGFLHLYdGEEAIAVGVMESLTPDDAVVATYREHGHALARGIDAGAIMAEMYGKQEGCsr 80
Cdd:TIGR03181  33 MVLTRRFDTKALALQRQGRLGTYAPNL-GQEAAQVGSALALRKDDWVFPSYRDHAAMLARGVPLVEILLYWRGDERGS-- 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282543696  81 grggsmhLFDDKTRFYGGNAIVGGGLPVAVGLALADRIQGLPRVTCCFFGDGAVAEGEFHESMNLAALWRLPVLFVCENN 160
Cdd:TIGR03181 110 -------WDPEGVNILPPNIPIGTQYLHAAGVAYALKLRGEDNVAVTYFGDGGTSEGDFYEALNFAGVFKAPVVFFVQNN 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282543696 161 LYAMGTSLTRSESEIHLTTKAESYAVPALAVDGMDVLAVEQAAQNAAAAIRAGEGPYFLEYRTYRFRAHSMFD-AQLYRE 239
Cdd:TIGR03181 183 QWAISVPRSKQTAAPTLAQKAIAYGIPGVQVDGNDVLAVYAVTKEAVERARSGGGPTLIEAVTYRLGPHTTADdPTRYRT 262
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2282543696 240 KAEVEAWKEHGPIVGFTQFLKGQGILDDADVQQLESQVAAEVEGAVAFAEKGTWEPVEDLTRFVYSE 306
Cdd:TIGR03181 263 KEEEEEWRKKDPILRLRKYLERKGLWDEEQEEALEEEAEAEVAEAVAEALALPPPPVDDIFDHVYAE 329
TPP_TK cd02012
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ...
103-196 4.29e-10

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


Pssm-ID: 238970 [Multi-domain]  Cd Length: 255  Bit Score: 59.05  E-value: 4.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282543696 103 GGGLPVAVGLALADRIQGLPRVTCCFFGDGAVAEGEFHESMNLAALWRLP--VLFVCENNLYAMGTSLTRSESEIhLTTK 180
Cdd:cd02012   108 GQGLSVAVGMALAEKLLGFDYRVYVLLGDGELQEGSVWEAASFAGHYKLDnlIAIVDSNRIQIDGPTDDILFTED-LAKK 186
                          90
                  ....*....|....*.
gi 2282543696 181 AESYAVPALAVDGMDV 196
Cdd:cd02012   187 FEAFGWNVIEVDGHDV 202
TPP_BFDC cd02002
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ...
103-192 1.38e-04

Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins similar to Pseudomonas putida benzoylformate decarboxylase (BFDC). P. putida BFDC plays a role in the mandelate pathway, catalyzing the conversion of benzoylformate to benzaldehyde and carbon dioxide. This enzyme is dependent on TPP and a divalent metal cation as cofactors.


Pssm-ID: 238960 [Multi-domain]  Cd Length: 178  Bit Score: 41.81  E-value: 1.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282543696 103 GGGLPVAVGLALADRiqglPRVTCCFFGDGAvaegeFHesMNLAALW-----RLPVLFVCENN------------LYAMG 165
Cdd:cd02002    52 GWGLPAAVGAALANP----DRKVVAIIGDGS-----FM--YTIQALWtaaryGLPVTVVILNNrgygalrsflkrVGPEG 120
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2282543696 166 TS------LTRSESEIHLTTKAESYAVPALAVD 192
Cdd:cd02002   121 PGenapdgLDLLDPGIDFAAIAKAFGVEAERVE 153
PRK05899 PRK05899
transketolase; Reviewed
103-196 1.01e-03

transketolase; Reviewed


Pssm-ID: 235639 [Multi-domain]  Cd Length: 586  Bit Score: 40.50  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282543696 103 GGGLPVAVGLALADRIQG----------LPRVTCCFFGDGAVAEGEFHESMNLAALWRLpvlfvceNNLYAM----GTSL 168
Cdd:PRK05899  121 GQGLANAVGMALAEKYLAalfnrpgldiVDHYTYVLCGDGDLMEGISHEACSLAGHLKL-------GNLIVIyddnRISI 193
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2282543696 169 tRSESEIHLTT----KAESYAVPALAVDGMDV 196
Cdd:PRK05899  194 -DGPTEGWFTEdvkkRFEAYGWHVIEVDGHDV 224
TPP_enzyme_C pfam02775
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
77-164 1.37e-03

Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;


Pssm-ID: 460689 [Multi-domain]  Cd Length: 151  Bit Score: 38.34  E-value: 1.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282543696  77 GCSRGRGGSMHLFDDKTRFY--GGNAIVGGGLPVAVGLALADRiqglPRVTCCFFGDGAVAegefhesMNLAALW----- 149
Cdd:pfam02775   3 GCHQMWAAQYYRFRPPRRYLtsGGLGTMGYGLPAAIGAKLARP----DRPVVAIAGDGGFQ-------MNLQELAtavry 71
                          90
                  ....*....|....*.
gi 2282543696 150 RLPVLFVCENN-LYAM 164
Cdd:pfam02775  72 NLPITVVVLNNgGYGM 87
TPP_enzymes cd00568
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ...
77-192 2.15e-03

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: 38.01  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282543696  77 GCSRGRGGSMHLFDDKTRFY--GGNAIVGGGLPVAVGLALADRiqglPRVTCCFFGDGAVAEGefHESMNLAALWRLPVL 154
Cdd:cd00568    21 GNSAYWAYRYLPLRRGRRFLtsTGFGAMGYGLPAAIGAALAAP----DRPVVCIAGDGGFMMT--GQELATAVRYGLPVI 94
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2282543696 155 FVC-ENNLYAMG-------TSLTRSESEIH---LTTKAESYAVPALAVD 192
Cdd:cd00568    95 VVVfNNGGYGTIrmhqeafYGGRVSGTDLSnpdFAALAEAYGAKGVRVE 143
 
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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