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Conserved domains on  [gi|1528514379|ref|WP_124899006|]
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pyruvate dehydrogenase (acetyl-transferring) E1 component subunit alpha [Paenimyroides viscosum]

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 ...
 6-320 1.67e-158

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: 445.48  E-value: 1.67e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1528514379   6 KEVYLKWYEDMQFWRKFEDKLAALYIQQKVRGFLHLYNGQEAVLAGALHAMDlSKDKMITAYRNHVQPIGMGVDPRRVMA 85
Cdd:TIGR03182   1 KEELLELYRDMLLIRRFEEKAGQLYGMGKIGGFCHLYIGQEAVAVGLIAALK-PDDYVITSYRDHGHALARGVPPKEVMA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1528514379  86 ELLGKATGTSQGLGGSMHIFSKEHGFYGGHGIVGAQIPVGAGMAFADKYLETGGVSLTYFGDGAARQGSLHEAFNMAMLW 165
Cdd:TIGR03182  80 ELTGRETGCSKGKGGSMHMFDREKNFYGGHGIVGAQVPLATGLAFANKYRGNDNVTACFFGDGAANQGQFYESFNMAALW 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1528514379 166 KLPVVFICENNGYAMGTSVERTANHTDIWKLGLGYEMPSYAVDAMNPVKVAEAMFDAMERARRGEGPTFLEMKTYRYRGH 245
Cdd:TIGR03182 160 KLPVIFVIENNLYAMGTAVERSSSVTDLYKRGESFGIPGERVDGMDVLAVREAAKEAVERARSGKGPILLEMKTYRFRGH 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1528514379 246 SMSDAQHYRTKDEVEEYKKIDPITQVLNVIKENSWATDEEIETIDQRVRDLVSECEKFAEESPYPETNVMYDVVY 320
Cdd:TIGR03182 240 SMSDPAKYRSKEEVEEWRKRDPIEKLKARLIEQGIASEEELKEIDKEVRAEVEEAVEFAENSPEPPVEELYTDVY 314
 
Name Accession Description Interval E-value
PDH_E1_alph_y TIGR03182
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the ...
 6-320 1.67e-158

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: 445.48  E-value: 1.67e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1528514379   6 KEVYLKWYEDMQFWRKFEDKLAALYIQQKVRGFLHLYNGQEAVLAGALHAMDlSKDKMITAYRNHVQPIGMGVDPRRVMA 85
Cdd:TIGR03182   1 KEELLELYRDMLLIRRFEEKAGQLYGMGKIGGFCHLYIGQEAVAVGLIAALK-PDDYVITSYRDHGHALARGVPPKEVMA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1528514379  86 ELLGKATGTSQGLGGSMHIFSKEHGFYGGHGIVGAQIPVGAGMAFADKYLETGGVSLTYFGDGAARQGSLHEAFNMAMLW 165
Cdd:TIGR03182  80 ELTGRETGCSKGKGGSMHMFDREKNFYGGHGIVGAQVPLATGLAFANKYRGNDNVTACFFGDGAANQGQFYESFNMAALW 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1528514379 166 KLPVVFICENNGYAMGTSVERTANHTDIWKLGLGYEMPSYAVDAMNPVKVAEAMFDAMERARRGEGPTFLEMKTYRYRGH 245
Cdd:TIGR03182 160 KLPVIFVIENNLYAMGTAVERSSSVTDLYKRGESFGIPGERVDGMDVLAVREAAKEAVERARSGKGPILLEMKTYRFRGH 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1528514379 246 SMSDAQHYRTKDEVEEYKKIDPITQVLNVIKENSWATDEEIETIDQRVRDLVSECEKFAEESPYPETNVMYDVVY 320
Cdd:TIGR03182 240 SMSDPAKYRSKEEVEEWRKRDPIEKLKARLIEQGIASEEELKEIDKEVRAEVEEAVEFAENSPEPPVEELYTDVY 314
AcoA COG1071
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ...
 3-326 6.65e-153

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: 432.64  E-value: 6.65e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1528514379   3 AITKEVYLKWYEDMQFWRKFEDKLAALYIQQKVrGFLHLYNGQEAVLAGALHAMDlSKDKMITAYRNHVQPIGMGVDPRR 82
Cdd:COG1071    16 DLSKEELLELYRDMLLIRRFEERALALQRQGKI-GFYHLSIGQEAAQVGAAAALR-PGDWIFPTYRDHGHALARGVDPKE 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1528514379  83 VMAELLGKATGTSQGLGGSMHIFSKEHGFYGGHGIVGAQIPVGAGMAFADKYLETGGVSLTYFGDGAARQGSLHEAFNMA 162
Cdd:COG1071    94 LMAELFGKATGPSKGRGGSMHFFDKELNFLGGSGIVGGQLPHAVGAALAAKLRGEDEVAVAFFGDGATSEGDFHEALNFA 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1528514379 163 MLWKLPVVFICENNGYAMGTSVERTANHTDIWKLGLGYEMPSYAVDAMNPVKVAEAMFDAMERARRGEGPTFLEMKTYRY 242
Cdd:COG1071   174 AVWKLPVVFVCENNGYAISTPVERQTAVETIADRAAGYGIPGVRVDGNDVLAVYAAVKEAVERARAGEGPTLIEAKTYRL 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1528514379 243 RGHSMSD-AQHYRTKDEVEEYKKIDPITQVLNVIKENSWATDEEIETIDQRVRDLVSECEKFAEESPYPETNVMYDVVYD 321
Cdd:COG1071   254 GGHSTSDdPTRYRTKEEVEEWRERDPIERLRAYLLEEGLLTEEELEAIEAEAKAEVEEAVEFAEASPEPDPEELFDDVYA 333


                  ....*
gi 1528514379 322 QENYP 326
Cdd:COG1071   334 EPPPH 338
TPP_E1_PDC_ADC_BCADC cd02000
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ...
 12-304 7.46e-139

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: 394.94  E-value: 7.46e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1528514379  12 WYEDMQFWRKFEDKLAALYIQQKVRGFLHLYNGQEAVLAGALHAMDlSKDKMITAYRNHVQPIGMGVDPRRVMAELLGKA 91
Cdd:cd02000     1 LYRTMVLIRRFDERLLELYRQGKIGGFYHLSIGQEAVAVGVAAALR-PGDWVFPTYRDHGHALARGVDLKEMLAELFGKE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1528514379  92 TGTSQGLGGSMHIFSKEHGFYGGHGIVGAQIPVGAGMAFADKYLETGGVSLTYFGDGAARQGSLHEAFNMAMLWKLPVVF 171
Cdd:cd02000    80 TGPCKGRGGSMHIGDKEKNFFGGNGIVGGQVPLAAGAALALKYRGEDRVAVCFFGDGATNEGDFHEALNFAALWKLPVIF 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1528514379 172 ICENNGYAMGTSVERTANHTDIWKLGLGYEMPSYAVDAMNPVKVAEAMFDAMERARRGEGPTFLEMKTYRYRGHSMS-DA 250
Cdd:cd02000   160 VCENNGYAISTPTSRQTAGTSIADRAAAYGIPGIRVDGNDVLAVYEAAKEAVERARAGGGPTLIEAVTYRLGGHSTSdDP 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1528514379 251 QHYRTKDEVEEYKKIDPITQVLNVIKENSWATDEEIETIDQRVRDLVSECEKFA 304
Cdd:cd02000   240 SRYRTKEEVEEWKKRDPILRLRKYLIEAGILTEEELAAIEAEVKAEVEEAVEFA 293
PLN02269 PLN02269
Pyruvate dehydrogenase E1 component subunit alpha
 5-320 6.41e-109

Pyruvate dehydrogenase E1 component subunit alpha


Pssm-ID: 215152 [Multi-domain]  Cd Length: 362  Bit Score: 321.66  E-value: 6.41e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1528514379   5 TKEVYLKWYEDMQFWRKFEDKLAALYIQQKVRGFLHLYNGQEAVLAGALHAMDLsKDKMITAYRNHVQPIGMGVDPRRVM 84
Cdd:PLN02269   28 SKQELVDFFRDMYLMRRMEIAADSLYKAKLIRGFCHLYDGQEAVAVGMEAAITK-EDAIITAYRDHCTHLGRGGTVLEVF 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1528514379  85 AELLGKATGTSQGLGGSMHIFSKEHGFYGGHGIVGAQIPVGAGMAFADKYLETGGVSLTYFGDGAARQGSLHEAFNMAML 164
Cdd:PLN02269  107 AELMGRKDGCSRGKGGSMHFYKKDANFYGGHGIVGAQVPLGAGLAFAQKYNKEENVAFALYGDGAANQGQLFEALNIAAL 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1528514379 165 WKLPVVFICENNGYAMGTSVERTANHTDIWKLGlGYeMPSYAVDAMNPVKVAEAMFDAMERARRgEGPTFLEMKTYRYRG 244
Cdd:PLN02269  187 WDLPVIFVCENNHYGMGTAEWRAAKSPAYYKRG-DY-VPGLKVDGMDVLAVKQACKFAKEHALS-NGPIVLEMDTYRYHG 263

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1528514379 245 HSMSD-AQHYRTKDEVEEYKKI-DPITQVLNVIKENSWATDEEIETIDQRVRDLVSECEKFAEESPYPETNVMYDVVY 320
Cdd:PLN02269  264 HSMSDpGSTYRTRDEISGVRQErDPIERVRKLLLAHELATEAELKDIEKEIRKEVDDAVAKAKESPMPDPSELFTNVY 341
E1_dh pfam00676
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ...
 14-311 2.28e-100

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: 297.70  E-value: 2.28e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1528514379  14 EDMQFWRKFEDKLAALYIQQKVRGFLHLYNGQEAVLAGALHAMDLsKDKMITAYRNHVQPIGMGVDPRRVMAELLGKAtg 93
Cdd:pfam00676   1 RRMMTLRRMEDARDALYKRQGIRGFYHLYAGQEAAQVGIAAALEP-GDYIIPGYRDHGNLLARGLSLEEIFAELYGRV-- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1528514379  94 tSQGLGGSMHIF--SKEHGFYGGHGIVGAQIPVGAGMAFADKYLETGGVSLTYFGDGAARQGSLHEAFNMAMLWKLPVVF 171
Cdd:pfam00676  78 -AKGKGGSMHGYygAKGNRFYGGNGILGAQVPLGAGIALAAKYRGKKEVAITLYGDGAANQGDFFEGLNFAALWKLPVIF 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1528514379 172 ICENNGYAMGTSVERTANHTDIWKLGLGYEMPSYAVDAMNPVKVAEAMFDAMERARRGEGPTFLEMKTYRYRGHSMSD-A 250
Cdd:pfam00676 157 VCENNQYGISTPAERASASTTYADRARGYGIPGLHVDGMDPLAVYQASKFAAERARTGKGPFLIELVTYRYGGHSMSDdP 236

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1528514379 251 QHYRTKDEVEEY-KKIDPITQVLNVIKENSWATDEEIETIDQRVRDLVSECEKFAEESPYPE 311
Cdd:pfam00676 237 STYRTRDEYEEVrKKKDPIQRFKEHLVSKGVWSEEELKAIEKEVRKEVEEAFKKAESAPEPH 298
 
Name Accession Description Interval E-value
PDH_E1_alph_y TIGR03182
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the ...
 6-320 1.67e-158

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: 445.48  E-value: 1.67e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1528514379   6 KEVYLKWYEDMQFWRKFEDKLAALYIQQKVRGFLHLYNGQEAVLAGALHAMDlSKDKMITAYRNHVQPIGMGVDPRRVMA 85
Cdd:TIGR03182   1 KEELLELYRDMLLIRRFEEKAGQLYGMGKIGGFCHLYIGQEAVAVGLIAALK-PDDYVITSYRDHGHALARGVPPKEVMA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1528514379  86 ELLGKATGTSQGLGGSMHIFSKEHGFYGGHGIVGAQIPVGAGMAFADKYLETGGVSLTYFGDGAARQGSLHEAFNMAMLW 165
Cdd:TIGR03182  80 ELTGRETGCSKGKGGSMHMFDREKNFYGGHGIVGAQVPLATGLAFANKYRGNDNVTACFFGDGAANQGQFYESFNMAALW 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1528514379 166 KLPVVFICENNGYAMGTSVERTANHTDIWKLGLGYEMPSYAVDAMNPVKVAEAMFDAMERARRGEGPTFLEMKTYRYRGH 245
Cdd:TIGR03182 160 KLPVIFVIENNLYAMGTAVERSSSVTDLYKRGESFGIPGERVDGMDVLAVREAAKEAVERARSGKGPILLEMKTYRFRGH 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1528514379 246 SMSDAQHYRTKDEVEEYKKIDPITQVLNVIKENSWATDEEIETIDQRVRDLVSECEKFAEESPYPETNVMYDVVY 320
Cdd:TIGR03182 240 SMSDPAKYRSKEEVEEWRKRDPIEKLKARLIEQGIASEEELKEIDKEVRAEVEEAVEFAENSPEPPVEELYTDVY 314
AcoA COG1071
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ...
 3-326 6.65e-153

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: 432.64  E-value: 6.65e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1528514379   3 AITKEVYLKWYEDMQFWRKFEDKLAALYIQQKVrGFLHLYNGQEAVLAGALHAMDlSKDKMITAYRNHVQPIGMGVDPRR 82
Cdd:COG1071    16 DLSKEELLELYRDMLLIRRFEERALALQRQGKI-GFYHLSIGQEAAQVGAAAALR-PGDWIFPTYRDHGHALARGVDPKE 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1528514379  83 VMAELLGKATGTSQGLGGSMHIFSKEHGFYGGHGIVGAQIPVGAGMAFADKYLETGGVSLTYFGDGAARQGSLHEAFNMA 162
Cdd:COG1071    94 LMAELFGKATGPSKGRGGSMHFFDKELNFLGGSGIVGGQLPHAVGAALAAKLRGEDEVAVAFFGDGATSEGDFHEALNFA 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1528514379 163 MLWKLPVVFICENNGYAMGTSVERTANHTDIWKLGLGYEMPSYAVDAMNPVKVAEAMFDAMERARRGEGPTFLEMKTYRY 242
Cdd:COG1071   174 AVWKLPVVFVCENNGYAISTPVERQTAVETIADRAAGYGIPGVRVDGNDVLAVYAAVKEAVERARAGEGPTLIEAKTYRL 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1528514379 243 RGHSMSD-AQHYRTKDEVEEYKKIDPITQVLNVIKENSWATDEEIETIDQRVRDLVSECEKFAEESPYPETNVMYDVVYD 321
Cdd:COG1071   254 GGHSTSDdPTRYRTKEEVEEWRERDPIERLRAYLLEEGLLTEEELEAIEAEAKAEVEEAVEFAEASPEPDPEELFDDVYA 333


                  ....*
gi 1528514379 322 QENYP 326
Cdd:COG1071   334 EPPPH 338
TPP_E1_PDC_ADC_BCADC cd02000
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ...
 12-304 7.46e-139

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: 394.94  E-value: 7.46e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1528514379  12 WYEDMQFWRKFEDKLAALYIQQKVRGFLHLYNGQEAVLAGALHAMDlSKDKMITAYRNHVQPIGMGVDPRRVMAELLGKA 91
Cdd:cd02000     1 LYRTMVLIRRFDERLLELYRQGKIGGFYHLSIGQEAVAVGVAAALR-PGDWVFPTYRDHGHALARGVDLKEMLAELFGKE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1528514379  92 TGTSQGLGGSMHIFSKEHGFYGGHGIVGAQIPVGAGMAFADKYLETGGVSLTYFGDGAARQGSLHEAFNMAMLWKLPVVF 171
Cdd:cd02000    80 TGPCKGRGGSMHIGDKEKNFFGGNGIVGGQVPLAAGAALALKYRGEDRVAVCFFGDGATNEGDFHEALNFAALWKLPVIF 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1528514379 172 ICENNGYAMGTSVERTANHTDIWKLGLGYEMPSYAVDAMNPVKVAEAMFDAMERARRGEGPTFLEMKTYRYRGHSMS-DA 250
Cdd:cd02000   160 VCENNGYAISTPTSRQTAGTSIADRAAAYGIPGIRVDGNDVLAVYEAAKEAVERARAGGGPTLIEAVTYRLGGHSTSdDP 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1528514379 251 QHYRTKDEVEEYKKIDPITQVLNVIKENSWATDEEIETIDQRVRDLVSECEKFA 304
Cdd:cd02000   240 SRYRTKEEVEEWKKRDPILRLRKYLIEAGILTEEELAAIEAEVKAEVEEAVEFA 293
PLN02269 PLN02269
Pyruvate dehydrogenase E1 component subunit alpha
 5-320 6.41e-109

Pyruvate dehydrogenase E1 component subunit alpha


Pssm-ID: 215152 [Multi-domain]  Cd Length: 362  Bit Score: 321.66  E-value: 6.41e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1528514379   5 TKEVYLKWYEDMQFWRKFEDKLAALYIQQKVRGFLHLYNGQEAVLAGALHAMDLsKDKMITAYRNHVQPIGMGVDPRRVM 84
Cdd:PLN02269   28 SKQELVDFFRDMYLMRRMEIAADSLYKAKLIRGFCHLYDGQEAVAVGMEAAITK-EDAIITAYRDHCTHLGRGGTVLEVF 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1528514379  85 AELLGKATGTSQGLGGSMHIFSKEHGFYGGHGIVGAQIPVGAGMAFADKYLETGGVSLTYFGDGAARQGSLHEAFNMAML 164
Cdd:PLN02269  107 AELMGRKDGCSRGKGGSMHFYKKDANFYGGHGIVGAQVPLGAGLAFAQKYNKEENVAFALYGDGAANQGQLFEALNIAAL 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1528514379 165 WKLPVVFICENNGYAMGTSVERTANHTDIWKLGlGYeMPSYAVDAMNPVKVAEAMFDAMERARRgEGPTFLEMKTYRYRG 244
Cdd:PLN02269  187 WDLPVIFVCENNHYGMGTAEWRAAKSPAYYKRG-DY-VPGLKVDGMDVLAVKQACKFAKEHALS-NGPIVLEMDTYRYHG 263

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1528514379 245 HSMSD-AQHYRTKDEVEEYKKI-DPITQVLNVIKENSWATDEEIETIDQRVRDLVSECEKFAEESPYPETNVMYDVVY 320
Cdd:PLN02269  264 HSMSDpGSTYRTRDEISGVRQErDPIERVRKLLLAHELATEAELKDIEKEIRKEVDDAVAKAKESPMPDPSELFTNVY 341
PLN02374 PLN02374
pyruvate dehydrogenase (acetyl-transferring)
 3-320 2.57e-108

pyruvate dehydrogenase (acetyl-transferring)


Pssm-ID: 215213 [Multi-domain]  Cd Length: 433  Bit Score: 322.66  E-value: 2.57e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1528514379   3 AITKEVYLKWYEDMQFWRKFEDKLAALYIQQKVRGFLHLYNGQEAVLAGALHAMDlSKDKMITAYRNHVQPIGMGVDPRR 82
Cdd:PLN02374   82 LVTREEGLELYEDMVLGRSFEDMCAQMYYRGKMFGFVHLYNGQEAVSTGFIKLLK-KDDSVVSTYRDHVHALSKGVPARA 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1528514379  83 VMAELLGKATGTSQGLGGSMHIFSKEHGFYGGHGIVGAQIPVGAGMAFADKY-------LETGGVSLTYFGDGAARQGSL 155
Cdd:PLN02374  161 VMSELFGKATGCCRGQGGSMHMFSKEHNLLGGFAFIGEGIPVATGAAFSSKYrrevlkeESCDDVTLAFFGDGTCNNGQF 240

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1528514379 156 HEAFNMAMLWKLPVVFICENNGYAMGTSVERTANHTDIWKLGLGYEMPSYAVDAMNPVKVAEAMFDAMERARRGEGPTFL 235
Cdd:PLN02374  241 FECLNMAALWKLPIVFVVENNLWAIGMSHLRATSDPEIWKKGPAFGMPGVHVDGMDVLKVREVAKEAIERARRGEGPTLV 320

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1528514379 236 EMKTYRYRGHSMSDAQHYRTKDEVEEYKKIDPITQVLNVIKENSWATDEEIETIDQRVRDLVSECEKFAEESPYPETNVM 315
Cdd:PLN02374  321 ECETYRFRGHSLADPDELRDPAEKAHYAARDPIAALKKYLIENGLATEAELKAIEKKIDEVVEDAVEFADASPLPPRSQL 400


                  ....*
gi 1528514379 316 YDVVY 320
Cdd:PLN02374  401 LENVF 405
E1_dh pfam00676
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ...
 14-311 2.28e-100

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: 297.70  E-value: 2.28e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1528514379  14 EDMQFWRKFEDKLAALYIQQKVRGFLHLYNGQEAVLAGALHAMDLsKDKMITAYRNHVQPIGMGVDPRRVMAELLGKAtg 93
Cdd:pfam00676   1 RRMMTLRRMEDARDALYKRQGIRGFYHLYAGQEAAQVGIAAALEP-GDYIIPGYRDHGNLLARGLSLEEIFAELYGRV-- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1528514379  94 tSQGLGGSMHIF--SKEHGFYGGHGIVGAQIPVGAGMAFADKYLETGGVSLTYFGDGAARQGSLHEAFNMAMLWKLPVVF 171
Cdd:pfam00676  78 -AKGKGGSMHGYygAKGNRFYGGNGILGAQVPLGAGIALAAKYRGKKEVAITLYGDGAANQGDFFEGLNFAALWKLPVIF 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1528514379 172 ICENNGYAMGTSVERTANHTDIWKLGLGYEMPSYAVDAMNPVKVAEAMFDAMERARRGEGPTFLEMKTYRYRGHSMSD-A 250
Cdd:pfam00676 157 VCENNQYGISTPAERASASTTYADRARGYGIPGLHVDGMDPLAVYQASKFAAERARTGKGPFLIELVTYRYGGHSMSDdP 236

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1528514379 251 QHYRTKDEVEEY-KKIDPITQVLNVIKENSWATDEEIETIDQRVRDLVSECEKFAEESPYPE 311
Cdd:pfam00676 237 STYRTRDEYEEVrKKKDPIQRFKEHLVSKGVWSEEELKAIEKEVRKEVEEAFKKAESAPEPH 298
odpA CHL00149
pyruvate dehydrogenase E1 component alpha subunit; Reviewed
 4-320 9.82e-93

pyruvate dehydrogenase E1 component alpha subunit; Reviewed


Pssm-ID: 177069 [Multi-domain]  Cd Length: 341  Bit Score: 279.83  E-value: 9.82e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1528514379   4 ITKEVYLKWYEDMQFWRKFEDKLAALYIQQKVRGFLHLYNGQEAVLAGALHAMDlSKDKMITAYRNHVQPIGMGVDPRRV 83
Cdd:CHL00149   17 INSMWLLVLYEDMLLGRNFEDMCAQMYYRGKMFGFVHLYNGQEAVSTGVIKLLA-ETDYVCSTYRDHVHALSKGVPPKNV 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1528514379  84 MAELLGKATGTSQGLGGSMHIFSKEHGFYGGHGIVGAQIPVGAGMAFADKY-------LETGGVSLTYFGDGAARQGSLH 156
Cdd:CHL00149   96 MAELFGKETGCSRGRGGSMHIFSAPHNFLGGFAFIGEGIPIALGAAFQSIYrqqvlkeVQPLRVTACFFGDGTTNNGQFF 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1528514379 157 EAFNMAMLWKLPVVFICENNGYAMGTSVERTANHTDIWKLGLGYEMPSYAVDAMNPVKVAEAMFDAMERARRGEGPTFLE 236
Cdd:CHL00149  176 ECLNMAVLWKLPIIFVVENNQWAIGMAHHRSTSIPEIHKKAEAFGLPGIEVDGMDVLAVREVAKEAVERARQGDGPTLIE 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1528514379 237 MKTYRYRGHSMSDAQHYRTKDEVEEYKKIDPITQVLNVIKENSWATDEEIETIDQRVRDLVSECEKFAEESPYPETNVMY 316
Cdd:CHL00149  256 ALTYRFRGHSLADPDELRSKQEKEAWVARDPIKKLKSYIIDNELASQKELNKIQREVKIEIEQAVQFAISSPEPNISDLK 335


                  ....
gi 1528514379 317 DVVY 320
Cdd:CHL00149  336 KYLF 339
TPP_enzyme_C pfam02775
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
91-236 1.90e-07

Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;


Pssm-ID: 460689 [Multi-domain]  Cd Length: 151  Bit Score: 49.89  E-value: 1.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1528514379  91 ATGTSQGLGGSMHIFSKEHGFY--GGHGIVGAQIPVGAGMAFADKYLETggVSLTyfGDGAArQGSLHEAFNMAMLwKLP 168
Cdd:pfam02775   1 DIGCHQMWAAQYYRFRPPRRYLtsGGLGTMGYGLPAAIGAKLARPDRPV--VAIA--GDGGF-QMNLQELATAVRY-NLP 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1528514379 169 VVFICENNG-YAMgtsverTANHTDIWKLGLGYEMPSYAVDAMNPVKVAEAM-------------FDAMERARRGEGPTF 234
Cdd:pfam02775  75 ITVVVLNNGgYGM------TRGQQTPFGGGRYSGPSGKILPPVDFAKLAEAYgakgarvespeelEEALKEALEHDGPAL 148


                  ..
gi 1528514379 235 LE 236
Cdd:pfam02775 149 ID 150
TPP_TK cd02012
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ...
 114-261 3.09e-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: 3.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1528514379 114 GHGIvgaqiPVGAGMAFADKYLETGGVSLTYFGDGAARQGSLHEAFNMAMLWKL-PVVFICENNGYAMGTSVERTANHTD 192
Cdd:cd02012   108 GQGL-----SVAVGMALAEKLLGFDYRVYVLLGDGELQEGSVWEAASFAGHYKLdNLIAIVDSNRIQIDGPTDDILFTED 182

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1528514379 193 I---WKlGLGYEmpSYAVDAMNpvkvAEAMFDAMERARRGEG-PTFLEMKTYRYRG-HSMSD--AQHYR--TKDEVEE 261
Cdd:cd02012   183 LakkFE-AFGWN--VIEVDGHD----VEEILAALEEAKKSKGkPTLIIAKTIKGKGvPFMENtaKWHGKplGEEEVEL 253
IlvB COG0028
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ...
 60-239 1.63e-05

Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis


Pssm-ID: 439799 [Multi-domain]  Cd Length: 548  Bit Score: 46.31  E-value: 1.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1528514379  60 KDKMITAYRNHVQPIgmgvDPRRVMAELlGKAT----------GTSQGLGGSMHIFSKEHGFY--GGHGIVGAQIP--VG 125
Cdd:COG0028   349 RAEYLAAYAADDGPI----KPQRVIAAL-REALpddaivvtdvGQHQMWAARYLRFRRPRRFLtsGGLGTMGYGLPaaIG 423

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1528514379 126 AGMAFADKYLetggVSLTyfGDGAarqgslheaFNMAM--LW-----KLPVVFICENNG-YAMgtsvERtanhtdiWKLG 197
Cdd:COG0028   424 AKLARPDRPV----VAIT--GDGG---------FQMNLqeLAtavryGLPVKVVVLNNGgLGM----VR-------QWQE 477

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1528514379 198 LGYEMPSYAVDAMNP--VKVAEAM------------FD-AMERARRGEGPTFLEMKT 239
Cdd:COG0028   478 LFYGGRYSGTDLPNPdfAKLAEAFgakgervetpeeLEaALEEALASDGPALIDVRV 534
TPP_enzymes cd00568
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ...
 109-239 1.20e-04

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: 41.86  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1528514379 109 HGFYGGHGIVGAQIPVGAGMAFADKylETGGVSLTyfGDGAArQGSLHEaFNMAMLWKLPVVFICENNGY------AMGT 182
Cdd:cd00568    39 FLTSTGFGAMGYGLPAAIGAALAAP--DRPVVCIA--GDGGF-MMTGQE-LATAVRYGLPVIVVVFNNGGygtirmHQEA 112

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1528514379 183 SVERTANHT-----DIWKLGLGYEMPSYAVDAmnpvkvAEAMFDAMERARRGEGPTFLEMKT 239
Cdd:cd00568   113 FYGGRVSGTdlsnpDFAALAEAYGAKGVRVED------PEDLEAALAEALAAGGPALIEVKT 168
PRK13679 PRK13679
hypothetical protein; Provisional
 262-330 1.14e-03

hypothetical protein; Provisional


Pssm-ID: 184236  Cd Length: 168  Bit Score: 39.15  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1528514379 262 YKKIDP-ITqvlnvIKENSWATDEEIETIDQRVRDLVSECEKFAEE-----SPYPETNVMY------------------D 317
Cdd:PRK13679   28 YALIPPhIT-----LKEPFEISDEQLDSIVEELRAIASETKPFTLHvtkvsSFAPTNNVIYfkvekteeleelherlhsG 102

                          90
                  ....*....|...
gi 1528514379 318 VVYDQENYPFIPH 330
Cdd:PRK13679  103 DFYGEAEYAFVPH 115
PRK05899 PRK05899
transketolase; Reviewed
 122-239 4.64e-03

transketolase; Reviewed


Pssm-ID: 235639 [Multi-domain]  Cd Length: 586  Bit Score: 38.58  E-value: 4.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1528514379 122 IPVGAGMAFADKYL-----ETGGVSLTYF-----GDGAARQGSLHEAFNMAMLWKLP--VVFICENN----GYAMGTSVE 185
Cdd:PRK05899  124 LANAVGMALAEKYLaalfnRPGLDIVDHYtyvlcGDGDLMEGISHEACSLAGHLKLGnlIVIYDDNRisidGPTEGWFTE 203

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1528514379 186 RTANHtdiwklglgYEmpSY-----AVDAMNPvkvaEAMFDAMERARRGEGPTFLEMKT 239
Cdd:PRK05899  204 DVKKR---------FE--AYgwhviEVDGHDV----EAIDAAIEEAKASTKPTLIIAKT 247
TPP_BFDC cd02002
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ...
 105-239 4.64e-03

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: 37.57  E-value: 4.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1528514379 105 FSKEHGFYG--GHGIvGAQIPVGAGMAFADKyletGGVSLTYFGDGAarqgslheaFNMAM--LW-----KLPVVFICEN 175
Cdd:cd02002    37 LTRPGSYFTlrGGGL-GWGLPAAVGAALANP----DRKVVAIIGDGS---------FMYTIqaLWtaaryGLPVTVVILN 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1528514379 176 NG--YAMGTSVERtanhtdIWKLGLG---YEMPSYAVDAMNPVKVAEAM------------FD-AMERARRGEGPTFLEM 237
Cdd:cd02002   103 NRgyGALRSFLKR------VGPEGPGenaPDGLDLLDPGIDFAAIAKAFgveaervetpeeLDeALREALAEGGPALIEV 176


                  ..
gi 1528514379 238 KT 239
Cdd:cd02002   177 VV 178
 
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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