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Conserved domains on  [gi|2539597429|ref|WP_295815081|]
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pyruvate dehydrogenase (acetyl-transferring) E1 component subunit alpha, partial [uncultured Nitratireductor sp.]

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 ...
 1-267 6.32e-168

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: 466.66  E-value: 6.32e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539597429   1 ACLKDGDQVITGYRDHGHMLACGLDPRGVMAELTGRSGGLSKGKGGSMHMFSKEKNFYGGHGIVGAQVPIGTGLGFANKY 80
Cdd:TIGR03182  49 AALKPDDYVITSYRDHGHALARGVPPKEVMAELTGRETGCSKGKGGSMHMFDREKNFYGGHGIVGAQVPLATGLAFANKY 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539597429  81 RGNDNVSVAYFGDGASNQGQVYESFNMASLWDLPVVYVIENNMYAMGTSVDRASAETELFKRGISFEIEGEEVDGMDVLA 160
Cdd:TIGR03182 129 RGNDNVTACFFGDGAANQGQFYESFNMAALWKLPVIFVIENNLYAMGTAVERSSSVTDLYKRGESFGIPGERVDGMDVLA 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539597429 161 VREAAERAVKYARSGKGPYILEMKTYRYRGHSMSDPAKYRTKEEVNKMRqEHDPIDHLRATLLEAGV-EEEELKGIDKEI 239
Cdd:TIGR03182 209 VREAAKEAVERARSGKGPILLEMKTYRFRGHSMSDPAKYRSKEEVEEWR-KRDPIEKLKARLIEQGIaSEEELKEIDKEV 287

                         250       260
                  ....*....|....*....|....*...
gi 2539597429 240 KAIVTDAADFAQSSPEPDPSELYTDILV 267
Cdd:TIGR03182 288 RAEVEEAVEFAENSPEPPVEELYTDVYA 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 ...
 1-267 6.32e-168

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: 466.66  E-value: 6.32e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539597429   1 ACLKDGDQVITGYRDHGHMLACGLDPRGVMAELTGRSGGLSKGKGGSMHMFSKEKNFYGGHGIVGAQVPIGTGLGFANKY 80
Cdd:TIGR03182  49 AALKPDDYVITSYRDHGHALARGVPPKEVMAELTGRETGCSKGKGGSMHMFDREKNFYGGHGIVGAQVPLATGLAFANKY 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539597429  81 RGNDNVSVAYFGDGASNQGQVYESFNMASLWDLPVVYVIENNMYAMGTSVDRASAETELFKRGISFEIEGEEVDGMDVLA 160
Cdd:TIGR03182 129 RGNDNVTACFFGDGAANQGQFYESFNMAALWKLPVIFVIENNLYAMGTAVERSSSVTDLYKRGESFGIPGERVDGMDVLA 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539597429 161 VREAAERAVKYARSGKGPYILEMKTYRYRGHSMSDPAKYRTKEEVNKMRqEHDPIDHLRATLLEAGV-EEEELKGIDKEI 239
Cdd:TIGR03182 209 VREAAKEAVERARSGKGPILLEMKTYRFRGHSMSDPAKYRSKEEVEEWR-KRDPIEKLKARLIEQGIaSEEELKEIDKEV 287

                         250       260
                  ....*....|....*....|....*...
gi 2539597429 240 KAIVTDAADFAQSSPEPDPSELYTDILV 267
Cdd:TIGR03182 288 RAEVEEAVEFAENSPEPPVEELYTDVYA 315
AcoA COG1071
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ...
 1-268 6.68e-141

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: 399.52  E-value: 6.68e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539597429   1 ACLKDGDQVITGYRDHGHMLACGLDPRGVMAELTGRSGGLSKGKGGSMHMFSKEKNFYGGHGIVGAQVPIGTGLGFANKY 80
Cdd:COG1071    66 AALRPGDWIFPTYRDHGHALARGVDPKELMAELFGKATGPSKGRGGSMHFFDKELNFLGGSGIVGGQLPHAVGAALAAKL 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539597429  81 RGNDNVSVAYFGDGASNQGQVYESFNMASLWDLPVVYVIENNMYAMGTSVDRASAETELFKRGISFEIEGEEVDGMDVLA 160
Cdd:COG1071   146 RGEDEVAVAFFGDGATSEGDFHEALNFAAVWKLPVVFVCENNGYAISTPVERQTAVETIADRAAGYGIPGVRVDGNDVLA 225

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539597429 161 VREAAERAVKYARSGKGPYILEMKTYRYRGHSMSD-PAKYRTKEEVNKMRqEHDPIDHLRATLLEAGV-EEEELKGIDKE 238
Cdd:COG1071   226 VYAAVKEAVERARAGEGPTLIEAKTYRLGGHSTSDdPTRYRTKEEVEEWR-ERDPIERLRAYLLEEGLlTEEELEAIEAE 304

                         250       260       270
                  ....*....|....*....|....*....|
gi 2539597429 239 IKAIVTDAADFAQSSPEPDPSELYTDILVE 268
Cdd:COG1071   305 AKAEVEEAVEFAEASPEPDPEELFDDVYAE 334
TPP_E1_PDC_ADC_BCADC cd02000
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ...
 1-250 4.18e-123

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: 352.57  E-value: 4.18e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539597429   1 ACLKDGDQVITGYRDHGHMLACGLDPRGVMAELTGRSGGLSKGKGGSMHMFSKEKNFYGGHGIVGAQVPIGTGLGFANKY 80
Cdd:cd02000    43 AALRPGDWVFPTYRDHGHALARGVDLKEMLAELFGKETGPCKGRGGSMHIGDKEKNFFGGNGIVGGQVPLAAGAALALKY 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539597429  81 RGNDNVSVAYFGDGASNQGQVYESFNMASLWDLPVVYVIENNMYAMGTSVDRASAETELFKRGISFEIEGEEVDGMDVLA 160
Cdd:cd02000   123 RGEDRVAVCFFGDGATNEGDFHEALNFAALWKLPVIFVCENNGYAISTPTSRQTAGTSIADRAAAYGIPGIRVDGNDVLA 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539597429 161 VREAAERAVKYARSGKGPYILEMKTYRYRGHSMS-DPAKYRTKEEVNKmRQEHDPIDHLRATLLEAGV-EEEELKGIDKE 238
Cdd:cd02000   203 VYEAAKEAVERARAGGGPTLIEAVTYRLGGHSTSdDPSRYRTKEEVEE-WKKRDPILRLRKYLIEAGIlTEEELAAIEAE 281

                         250
                  ....*....|..
gi 2539597429 239 IKAIVTDAADFA 250
Cdd:cd02000   282 VKAEVEEAVEFA 293
PLN02269 PLN02269
Pyruvate dehydrogenase E1 component subunit alpha
 1-269 7.29e-116

Pyruvate dehydrogenase E1 component subunit alpha


Pssm-ID: 215152 [Multi-domain]  Cd Length: 362  Bit Score: 336.69  E-value: 7.29e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539597429   1 ACLKDGDQVITGYRDHGHMLACGLDPRGVMAELTGRSGGLSKGKGGSMHMFSKEKNFYGGHGIVGAQVPIGTGLGFANKY 80
Cdd:PLN02269   77 AAITKEDAIITAYRDHCTHLGRGGTVLEVFAELMGRKDGCSRGKGGSMHFYKKDANFYGGHGIVGAQVPLGAGLAFAQKY 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539597429  81 RGNDNVSVAYFGDGASNQGQVYESFNMASLWDLPVVYVIENNMYAMGTSVDRASAETELFKRGISfeIEGEEVDGMDVLA 160
Cdd:PLN02269  157 NKEENVAFALYGDGAANQGQLFEALNIAALWDLPVIFVCENNHYGMGTAEWRAAKSPAYYKRGDY--VPGLKVDGMDVLA 234

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539597429 161 VREAAERAVKYARSgKGPYILEMKTYRYRGHSMSDP-AKYRTKEEVNKMRQEHDPIDHLRATLLEAGV-EEEELKGIDKE 238
Cdd:PLN02269  235 VKQACKFAKEHALS-NGPIVLEMDTYRYHGHSMSDPgSTYRTRDEISGVRQERDPIERVRKLLLAHELaTEAELKDIEKE 313

                         250       260       270
                  ....*....|....*....|....*....|.
gi 2539597429 239 IKAIVTDAADFAQSSPEPDPSELYTDILVES 269
Cdd:PLN02269  314 IRKEVDDAVAKAKESPMPDPSELFTNVYVKG 344
E1_dh pfam00676
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ...
 1-259 2.96e-102

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: 300.01  E-value: 2.96e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539597429   1 ACLKDGDQVITGYRDHGHMLACGLDPRGVMAELTGRSGGLSKGKggsMHMF--SKEKNFYGGHGIVGAQVPIGTGLGFAN 78
Cdd:pfam00676  41 AALEPGDYIIPGYRDHGNLLARGLSLEEIFAELYGRVAKGKGGS---MHGYygAKGNRFYGGNGILGAQVPLGAGIALAA 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539597429  79 KYRGNDNVSVAYFGDGASNQGQVYESFNMASLWDLPVVYVIENNMYAMGTSVDRASAETELFKRGISFEIEGEEVDGMDV 158
Cdd:pfam00676 118 KYRGKKEVAITLYGDGAANQGDFFEGLNFAALWKLPVIFVCENNQYGISTPAERASASTTYADRARGYGIPGLHVDGMDP 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539597429 159 LAVREAAERAVKYARSGKGPYILEMKTYRYRGHSMSDPA-KYRTKEEVNKMRQEHDPIDHLRATLLEAGV-EEEELKGID 236
Cdd:pfam00676 198 LAVYQASKFAAERARTGKGPFLIELVTYRYGGHSMSDDPsTYRTRDEYEEVRKKKDPIQRFKEHLVSKGVwSEEELKAIE 277

                         250       260
                  ....*....|....*....|...
gi 2539597429 237 KEIKAIVTDAADFAQSSPEPDPS 259
Cdd:pfam00676 278 KEVRKEVEEAFKKAESAPEPHPE 300
 
Name Accession Description Interval E-value
PDH_E1_alph_y TIGR03182
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the ...
 1-267 6.32e-168

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: 466.66  E-value: 6.32e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539597429   1 ACLKDGDQVITGYRDHGHMLACGLDPRGVMAELTGRSGGLSKGKGGSMHMFSKEKNFYGGHGIVGAQVPIGTGLGFANKY 80
Cdd:TIGR03182  49 AALKPDDYVITSYRDHGHALARGVPPKEVMAELTGRETGCSKGKGGSMHMFDREKNFYGGHGIVGAQVPLATGLAFANKY 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539597429  81 RGNDNVSVAYFGDGASNQGQVYESFNMASLWDLPVVYVIENNMYAMGTSVDRASAETELFKRGISFEIEGEEVDGMDVLA 160
Cdd:TIGR03182 129 RGNDNVTACFFGDGAANQGQFYESFNMAALWKLPVIFVIENNLYAMGTAVERSSSVTDLYKRGESFGIPGERVDGMDVLA 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539597429 161 VREAAERAVKYARSGKGPYILEMKTYRYRGHSMSDPAKYRTKEEVNKMRqEHDPIDHLRATLLEAGV-EEEELKGIDKEI 239
Cdd:TIGR03182 209 VREAAKEAVERARSGKGPILLEMKTYRFRGHSMSDPAKYRSKEEVEEWR-KRDPIEKLKARLIEQGIaSEEELKEIDKEV 287

                         250       260
                  ....*....|....*....|....*...
gi 2539597429 240 KAIVTDAADFAQSSPEPDPSELYTDILV 267
Cdd:TIGR03182 288 RAEVEEAVEFAENSPEPPVEELYTDVYA 315
AcoA COG1071
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ...
 1-268 6.68e-141

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: 399.52  E-value: 6.68e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539597429   1 ACLKDGDQVITGYRDHGHMLACGLDPRGVMAELTGRSGGLSKGKGGSMHMFSKEKNFYGGHGIVGAQVPIGTGLGFANKY 80
Cdd:COG1071    66 AALRPGDWIFPTYRDHGHALARGVDPKELMAELFGKATGPSKGRGGSMHFFDKELNFLGGSGIVGGQLPHAVGAALAAKL 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539597429  81 RGNDNVSVAYFGDGASNQGQVYESFNMASLWDLPVVYVIENNMYAMGTSVDRASAETELFKRGISFEIEGEEVDGMDVLA 160
Cdd:COG1071   146 RGEDEVAVAFFGDGATSEGDFHEALNFAAVWKLPVVFVCENNGYAISTPVERQTAVETIADRAAGYGIPGVRVDGNDVLA 225

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539597429 161 VREAAERAVKYARSGKGPYILEMKTYRYRGHSMSD-PAKYRTKEEVNKMRqEHDPIDHLRATLLEAGV-EEEELKGIDKE 238
Cdd:COG1071   226 VYAAVKEAVERARAGEGPTLIEAKTYRLGGHSTSDdPTRYRTKEEVEEWR-ERDPIERLRAYLLEEGLlTEEELEAIEAE 304

                         250       260       270
                  ....*....|....*....|....*....|
gi 2539597429 239 IKAIVTDAADFAQSSPEPDPSELYTDILVE 268
Cdd:COG1071   305 AKAEVEEAVEFAEASPEPDPEELFDDVYAE 334
TPP_E1_PDC_ADC_BCADC cd02000
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ...
 1-250 4.18e-123

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: 352.57  E-value: 4.18e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539597429   1 ACLKDGDQVITGYRDHGHMLACGLDPRGVMAELTGRSGGLSKGKGGSMHMFSKEKNFYGGHGIVGAQVPIGTGLGFANKY 80
Cdd:cd02000    43 AALRPGDWVFPTYRDHGHALARGVDLKEMLAELFGKETGPCKGRGGSMHIGDKEKNFFGGNGIVGGQVPLAAGAALALKY 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539597429  81 RGNDNVSVAYFGDGASNQGQVYESFNMASLWDLPVVYVIENNMYAMGTSVDRASAETELFKRGISFEIEGEEVDGMDVLA 160
Cdd:cd02000   123 RGEDRVAVCFFGDGATNEGDFHEALNFAALWKLPVIFVCENNGYAISTPTSRQTAGTSIADRAAAYGIPGIRVDGNDVLA 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539597429 161 VREAAERAVKYARSGKGPYILEMKTYRYRGHSMS-DPAKYRTKEEVNKmRQEHDPIDHLRATLLEAGV-EEEELKGIDKE 238
Cdd:cd02000   203 VYEAAKEAVERARAGGGPTLIEAVTYRLGGHSTSdDPSRYRTKEEVEE-WKKRDPILRLRKYLIEAGIlTEEELAAIEAE 281

                         250
                  ....*....|..
gi 2539597429 239 IKAIVTDAADFA 250
Cdd:cd02000   282 VKAEVEEAVEFA 293
PLN02269 PLN02269
Pyruvate dehydrogenase E1 component subunit alpha
 1-269 7.29e-116

Pyruvate dehydrogenase E1 component subunit alpha


Pssm-ID: 215152 [Multi-domain]  Cd Length: 362  Bit Score: 336.69  E-value: 7.29e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539597429   1 ACLKDGDQVITGYRDHGHMLACGLDPRGVMAELTGRSGGLSKGKGGSMHMFSKEKNFYGGHGIVGAQVPIGTGLGFANKY 80
Cdd:PLN02269   77 AAITKEDAIITAYRDHCTHLGRGGTVLEVFAELMGRKDGCSRGKGGSMHFYKKDANFYGGHGIVGAQVPLGAGLAFAQKY 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539597429  81 RGNDNVSVAYFGDGASNQGQVYESFNMASLWDLPVVYVIENNMYAMGTSVDRASAETELFKRGISfeIEGEEVDGMDVLA 160
Cdd:PLN02269  157 NKEENVAFALYGDGAANQGQLFEALNIAALWDLPVIFVCENNHYGMGTAEWRAAKSPAYYKRGDY--VPGLKVDGMDVLA 234

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539597429 161 VREAAERAVKYARSgKGPYILEMKTYRYRGHSMSDP-AKYRTKEEVNKMRQEHDPIDHLRATLLEAGV-EEEELKGIDKE 238
Cdd:PLN02269  235 VKQACKFAKEHALS-NGPIVLEMDTYRYHGHSMSDPgSTYRTRDEISGVRQERDPIERVRKLLLAHELaTEAELKDIEKE 313

                         250       260       270
                  ....*....|....*....|....*....|.
gi 2539597429 239 IKAIVTDAADFAQSSPEPDPSELYTDILVES 269
Cdd:PLN02269  314 IRKEVDDAVAKAKESPMPDPSELFTNVYVKG 344
E1_dh pfam00676
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ...
 1-259 2.96e-102

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: 300.01  E-value: 2.96e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539597429   1 ACLKDGDQVITGYRDHGHMLACGLDPRGVMAELTGRSGGLSKGKggsMHMF--SKEKNFYGGHGIVGAQVPIGTGLGFAN 78
Cdd:pfam00676  41 AALEPGDYIIPGYRDHGNLLARGLSLEEIFAELYGRVAKGKGGS---MHGYygAKGNRFYGGNGILGAQVPLGAGIALAA 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539597429  79 KYRGNDNVSVAYFGDGASNQGQVYESFNMASLWDLPVVYVIENNMYAMGTSVDRASAETELFKRGISFEIEGEEVDGMDV 158
Cdd:pfam00676 118 KYRGKKEVAITLYGDGAANQGDFFEGLNFAALWKLPVIFVCENNQYGISTPAERASASTTYADRARGYGIPGLHVDGMDP 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539597429 159 LAVREAAERAVKYARSGKGPYILEMKTYRYRGHSMSDPA-KYRTKEEVNKMRQEHDPIDHLRATLLEAGV-EEEELKGID 236
Cdd:pfam00676 198 LAVYQASKFAAERARTGKGPFLIELVTYRYGGHSMSDDPsTYRTRDEYEEVRKKKDPIQRFKEHLVSKGVwSEEELKAIE 277

                         250       260
                  ....*....|....*....|...
gi 2539597429 237 KEIKAIVTDAADFAQSSPEPDPS 259
Cdd:pfam00676 278 KEVRKEVEEAFKKAESAPEPHPE 300
PLN02374 PLN02374
pyruvate dehydrogenase (acetyl-transferring)
 3-268 7.85e-85

pyruvate dehydrogenase (acetyl-transferring)


Pssm-ID: 215213 [Multi-domain]  Cd Length: 433  Bit Score: 259.87  E-value: 7.85e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539597429   3 LKDGDQVITGYRDHGHMLACGLDPRGVMAELTGRSGGLSKGKGGSMHMFSKEKNFYGGHGIVGAQVPIGTGLGFANKYR- 81
Cdd:PLN02374  135 LKKDDSVVSTYRDHVHALSKGVPARAVMSELFGKATGCCRGQGGSMHMFSKEHNLLGGFAFIGEGIPVATGAAFSSKYRr 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539597429  82 ------GNDNVSVAYFGDGASNQGQVYESFNMASLWDLPVVYVIENNMYAMGTSVDRASAETELFKRGISFEIEGEEVDG 155
Cdd:PLN02374  215 evlkeeSCDDVTLAFFGDGTCNNGQFFECLNMAALWKLPIVFVVENNLWAIGMSHLRATSDPEIWKKGPAFGMPGVHVDG 294

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539597429 156 MDVLAVREAAERAVKYARSGKGPYILEMKTYRYRGHSMSDPAKYRTKEEVNKMrQEHDPIDHLRATLLEAGV-EEEELKG 234
Cdd:PLN02374  295 MDVLKVREVAKEAIERARRGEGPTLVECETYRFRGHSLADPDELRDPAEKAHY-AARDPIAALKKYLIENGLaTEAELKA 373

                         250       260       270
                  ....*....|....*....|....*....|....
gi 2539597429 235 IDKEIKAIVTDAADFAQSSPEPDPSELYTDILVE 268
Cdd:PLN02374  374 IEKKIDEVVEDAVEFADASPLPPRSQLLENVFAD 407
odpA CHL00149
pyruvate dehydrogenase E1 component alpha subunit; Reviewed
 3-262 6.61e-78

pyruvate dehydrogenase E1 component alpha subunit; Reviewed


Pssm-ID: 177069 [Multi-domain]  Cd Length: 341  Bit Score: 239.38  E-value: 6.61e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539597429   3 LKDGDQVITGYRDHGHMLACGLDPRGVMAELTGRSGGLSKGKGGSMHMFSKEKNFYGGHGIVGAQVPIGTGLGFANKYR- 81
Cdd:CHL00149   69 LAETDYVCSTYRDHVHALSKGVPPKNVMAELFGKETGCSRGRGGSMHIFSAPHNFLGGFAFIGEGIPIALGAAFQSIYRq 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539597429  82 ------GNDNVSVAYFGDGASNQGQVYESFNMASLWDLPVVYVIENNMYAMGTSVDRASAETELFKRGISFEIEGEEVDG 155
Cdd:CHL00149  149 qvlkevQPLRVTACFFGDGTTNNGQFFECLNMAVLWKLPIIFVVENNQWAIGMAHHRSTSIPEIHKKAEAFGLPGIEVDG 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539597429 156 MDVLAVREAAERAVKYARSGKGPYILEMKTYRYRGHSMSDPAKYRTKEEvNKMRQEHDPIDHLRATLLEAG-VEEEELKG 234
Cdd:CHL00149  229 MDVLAVREVAKEAVERARQGDGPTLIEALTYRFRGHSLADPDELRSKQE-KEAWVARDPIKKLKSYIIDNElASQKELNK 307

                         250       260
                  ....*....|....*....|....*...
gi 2539597429 235 IDKEIKAIVTDAADFAQSSPEPDPSELY 262
Cdd:CHL00149  308 IQREVKIEIEQAVQFAISSPEPNISDLK 335
TPP_TK cd02012
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ...
 60-205 2.09e-08

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: 53.66  E-value: 2.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539597429  60 GHGIvgaqvPIGTGLGFANKYRGNDNVSVAYFGDGASNQGQVYESFNMASLWDL-PVVYVIENNMYAMGTSVDRASAETE 138
Cdd:cd02012   108 GQGL-----SVAVGMALAEKLLGFDYRVYVLLGDGELQEGSVWEAASFAGHYKLdNLIAIVDSNRIQIDGPTDDILFTED 182

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2539597429 139 LFKRGISFEIEGEEVDGMDVlavrEAAERAVKYARSGKG-PYILEMKTYRYRG-HSMSDPAKYR----TKEEV 205
Cdd:cd02012   183 LAKKFEAFGWNVIEVDGHDV----EEILAALEEAKKSKGkPTLIIAKTIKGKGvPFMENTAKWHgkplGEEEV 251
TPP_enzyme_C pfam02775
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
57-182 3.85e-04

Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;


Pssm-ID: 460689 [Multi-domain]  Cd Length: 151  Bit Score: 39.88  E-value: 3.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539597429  57 FYGGHGIVGAQVPIGTGLGFANKYRgndNVsVAYFGDGASnqgqvyeSFNMASLW-----DLPVVYVIENNM-YAM---- 126
Cdd:pfam02775  23 TSGGLGTMGYGLPAAIGAKLARPDR---PV-VAIAGDGGF-------QMNLQELAtavryNLPITVVVLNNGgYGMtrgq 91

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539597429 127 --GTSVDRASAETELFKRGISFE--IEGEEVDGMDVlAVREAAERAVKYARSGKGPYILE 182
Cdd:pfam02775  92 qtPFGGGRYSGPSGKILPPVDFAklAEAYGAKGARV-ESPEELEEALKEALEHDGPALID 150
PRK12571 PRK12571
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
 66-195 5.57e-04

1-deoxy-D-xylulose-5-phosphate synthase; Provisional


Pssm-ID: 183601 [Multi-domain]  Cd Length: 641  Bit Score: 41.25  E-value: 5.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539597429  66 AQVPIGTGLGFA--NKYRGNDNVSVAYFGDGASNQGQVYESFNMASLWDLPVVYVIENNMYAMGTSVDRASAETELFKRG 143
Cdd:PRK12571  121 SSTSISAALGFAkaRALGQPDGDVVAVIGDGSLTAGMAYEALNNAGAADRRLIVILNDNEMSIAPPVGALAAYLSTLRSS 200

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539597429 144 ISFEIEGEEVDGMDVL---AVREAAERAVKYARS-GKGPYILEMKTYRY----RGHSMSD 195
Cdd:PRK12571  201 DPFARLRAIAKGVEERlpgPLRDGARRARELVTGmIGGGTLFEELGFTYvgpiDGHDMEA 260
PLN02234 PLN02234
1-deoxy-D-xylulose-5-phosphate synthase
 52-122 1.80e-03

1-deoxy-D-xylulose-5-phosphate synthase


Pssm-ID: 177878 [Multi-domain]  Cd Length: 641  Bit Score: 39.31  E-value: 1.80e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2539597429  52 SKEKNFYGGHGivGAQVPIGTGLGFANKYRGNDNVSVAYFGDGASNQGQVYESFNMASLWDLPVVYVIENN 122
Cdd:PLN02234  169 SEHDSFGTGHS--STTLSAGLGMAVGRDLKGMNNSVVSVIGDGAMTAGQAYEAMNNAGYLHSNMIVILNDN 237
PLN02582 PLN02582
1-deoxy-D-xylulose-5-phosphate synthase
 52-122 2.91e-03

1-deoxy-D-xylulose-5-phosphate synthase


Pssm-ID: 178194 [Multi-domain]  Cd Length: 677  Bit Score: 38.73  E-value: 2.91e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2539597429  52 SKEKNFYGGHgivgAQVPIGTGLGFA--NKYRGNDNVSVAYFGDGASNQGQVYESFNMASLWDLPVVYVIENN 122
Cdd:PLN02582  136 SEYDCFGTGH----SSTTISAGLGMAvgRDLKGKKNNVVAVIGDGAMTAGQAYEAMNNAGYLDSDMIVILNDN 204
TPP_E1_OGDC_like cd02016
Thiamine pyrophosphate (TPP) family, E1 of OGDC-like subfamily, TPP-binding module; composed ...
 92-195 3.95e-03

Thiamine pyrophosphate (TPP) family, E1 of OGDC-like subfamily, TPP-binding module; composed of proteins similar to the E1 component of the 2-oxoglutarate dehydrogenase multienzyme complex (OGDC). OGDC catalyzes the oxidative decarboxylation of 2-oxoglutarate to succinyl-CoA and carbon dioxide, a key reaction of the tricarboxylic acid cycle.


Pssm-ID: 238974 [Multi-domain]  Cd Length: 265  Bit Score: 37.89  E-value: 3.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2539597429  92 GDGA-SNQGQVYESFNMaslWDLP------VVYVIENNMYAMGTSVDRASAE---TELFKrgiSFEIEGEEVDGMDVLAV 161
Cdd:cd02016   148 GDAAfAGQGVVYETLNL---SNLPgyttggTIHIVVNNQIGFTTDPRDSRSSpycTDVAK---MIGAPIFHVNGDDPEAV 221

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2539597429 162 REAAERAVKYARSGKGPYILEMKTYRYRGHSMSD 195
Cdd:cd02016   222 VRATRLALEYRQKFKKDVVIDLVCYRRHGHNELD 255
 
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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