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Conserved domains on  [gi|488286560|ref|WP_002357768|]
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MULTISPECIES: pyruvate dehydrogenase (acetyl-transferring) E1 component subunit alpha [Enterococcus]

Protein Classification

thiamine pyrophosphate-dependent dehydrogenase E1 component subunit alpha( domain architecture ID 10799054)

thiamine pyrophosphate-dependent dehydrogenase E1 component subunit alpha is part of the E1 component of a multi-enzyme dehydrogenase complex such as pyruvate dehydrogenase, which catalyzes the overall conversion of pyruvate to acetyl-CoA and carbon dioxide

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PDH_E1_alph_x TIGR03181
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the ...
 24-365 0e+00

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: 534.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286560   24 PTFQILDQDGKIVNEDLVPDLSDEELVELMTRMVWSRVLDQRSTALNRQGRLGFFAPTAGQEASQLASQFAMEKEDYLLP 103
Cdd:TIGR03181   1 ELVQVLDEDGNVVDPEPAPDLSDEELVELYRDMVLTRRFDTKALALQRQGRLGTYAPNLGQEAAQVGSALALRKDDWVFP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286560  104 GYRDVPQLVQHGLPLREAFLWSRGHVAGNYYAEDLNALPPQIIIGAQYIQAAGVALGLKKRGKENVVFTYTGDGGSSQGD 183
Cdd:TIGR03181  81 SYRDHAAMLARGVPLVEILLYWRGDERGSWDPEGVNILPPNIPIGTQYLHAAGVAYALKLRGEDNVAVTYFGDGGTSEGD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286560  184 FYEAINFAGAYQANGVFIIQNNGFAISTPREKQTAAKTLAQKAVAAGIPGIQVDGMDPLAVYAIAKEARDWSAAGNGPVL 263
Cdd:TIGR03181 161 FYEALNFAGVFKAPVVFFVQNNQWAISVPRSKQTAAPTLAQKAIAYGIPGVQVDGNDVLAVYAVTKEAVERARSGGGPTL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286560  264 IETLTYRYGPHTLSgDDPTRYRSKEMDDEWVQKDPLTRFRKYLTDKGLWSEAKEEEIIEKTKEEIKVAIAEADKAPKQKV 343
Cdd:TIGR03181 241 IEAVTYRLGPHTTA-DDPTRYRTKEEEEEWRKKDPILRLRKYLERKGLWDEEQEEALEEEAEAEVAEAVAEALALPPPPV 319

                         330       340
                  ....*....|....*....|..
gi 488286560  344 SDFLKNMFEVQPQTIKEQIAFY 365
Cdd:TIGR03181 320 DDIFDHVYAELPPELEEQRAEL 341
 
Name Accession Description Interval E-value
PDH_E1_alph_x TIGR03181
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the ...
 24-365 0e+00

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: 534.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286560   24 PTFQILDQDGKIVNEDLVPDLSDEELVELMTRMVWSRVLDQRSTALNRQGRLGFFAPTAGQEASQLASQFAMEKEDYLLP 103
Cdd:TIGR03181   1 ELVQVLDEDGNVVDPEPAPDLSDEELVELYRDMVLTRRFDTKALALQRQGRLGTYAPNLGQEAAQVGSALALRKDDWVFP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286560  104 GYRDVPQLVQHGLPLREAFLWSRGHVAGNYYAEDLNALPPQIIIGAQYIQAAGVALGLKKRGKENVVFTYTGDGGSSQGD 183
Cdd:TIGR03181  81 SYRDHAAMLARGVPLVEILLYWRGDERGSWDPEGVNILPPNIPIGTQYLHAAGVAYALKLRGEDNVAVTYFGDGGTSEGD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286560  184 FYEAINFAGAYQANGVFIIQNNGFAISTPREKQTAAKTLAQKAVAAGIPGIQVDGMDPLAVYAIAKEARDWSAAGNGPVL 263
Cdd:TIGR03181 161 FYEALNFAGVFKAPVVFFVQNNQWAISVPRSKQTAAPTLAQKAIAYGIPGVQVDGNDVLAVYAVTKEAVERARSGGGPTL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286560  264 IETLTYRYGPHTLSgDDPTRYRSKEMDDEWVQKDPLTRFRKYLTDKGLWSEAKEEEIIEKTKEEIKVAIAEADKAPKQKV 343
Cdd:TIGR03181 241 IEAVTYRLGPHTTA-DDPTRYRTKEEEEEWRKKDPILRLRKYLERKGLWDEEQEEALEEEAEAEVAEAVAEALALPPPPV 319

                         330       340
                  ....*....|....*....|..
gi 488286560  344 SDFLKNMFEVQPQTIKEQIAFY 365
Cdd:TIGR03181 320 DDIFDHVYAELPPELEEQRAEL 341
AcoA COG1071
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ...
 25-367 7.83e-147

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: 418.78  E-value: 7.83e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286560  25 TFQILDQDGKivnEDLVPDLSDEELVELMTRMVWSRVLDQRSTALNRQGRLGFFAPTAGQEASQLASQFAMEKEDYLLPG 104
Cdd:COG1071    1 LVQVLDPDGT---EAALPDLSKEELLELYRDMLLIRRFEERALALQRQGKIGFYHLSIGQEAAQVGAAAALRPGDWIFPT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286560 105 YRDVPQLVQHGLPLREAFLWSRGHVAGN---------YYAEDLNALPPQIIIGAQYIQAAGVALGLKKRGKENVVFTYTG 175
Cdd:COG1071   78 YRDHGHALARGVDPKELMAELFGKATGPskgrggsmhFFDKELNFLGGSGIVGGQLPHAVGAALAAKLRGEDEVAVAFFG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286560 176 DGGSSQGDFYEAINFAGAYQANGVFIIQNNGFAISTPREKQTAAKTLAQKAVAAGIPGIQVDGMDPLAVYAIAKEARDWS 255
Cdd:COG1071  158 DGATSEGDFHEALNFAAVWKLPVVFVCENNGYAISTPVERQTAVETIADRAAGYGIPGVRVDGNDVLAVYAAVKEAVERA 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286560 256 AAGNGPVLIETLTYRYGPHTLSgDDPTRYRSKEMDDEWVQKDPLTRFRKYLTDKGLWSEAKEEEIIEKTKEEIKVAIAEA 335
Cdd:COG1071  238 RAGEGPTLIEAKTYRLGGHSTS-DDPTRYRTKEEVEEWRERDPIERLRAYLLEEGLLTEEELEAIEAEAKAEVEEAVEFA 316

                        330       340       350
                 ....*....|....*....|....*....|..
gi 488286560 336 DKAPKQKVSDFLKNMFEVQPQTIKEQIAFYEA 367
Cdd:COG1071  317 EASPEPDPEELFDDVYAEPPPHLAEQRAELAA 348
TPP_E1_PDC_ADC_BCADC cd02000
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ...
 52-313 3.26e-112

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: 329.07  E-value: 3.26e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286560  52 LMTRMVWSRVLDQRSTALNRQGRLGFF-APTAGQEASQLASQFAMEKEDYLLPGYRDVPQLVQHGLPLREAFLWSRGHVA 130
Cdd:cd02000    1 LYRTMVLIRRFDERLLELYRQGKIGGFyHLSIGQEAVAVGVAAALRPGDWVFPTYRDHGHALARGVDLKEMLAELFGKET 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286560 131 GN---------YYAEDLNALPPQIIIGAQYIQAAGVALGLKKRGKENVVFTYTGDGGSSQGDFYEAINFAGAYQANGVFI 201
Cdd:cd02000   81 GPckgrggsmhIGDKEKNFFGGNGIVGGQVPLAAGAALALKYRGEDRVAVCFFGDGATNEGDFHEALNFAALWKLPVIFV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286560 202 IQNNGFAISTPREKQTAAKTLAQKAVAAGIPGIQVDGMDPLAVYAIAKEARDWSAAGNGPVLIETLTYRYGPHTLSgDDP 281
Cdd:cd02000  161 CENNGYAISTPTSRQTAGTSIADRAAAYGIPGIRVDGNDVLAVYEAAKEAVERARAGGGPTLIEAVTYRLGGHSTS-DDP 239

                        250       260       270
                 ....*....|....*....|....*....|..
gi 488286560 282 TRYRSKEMDDEWVQKDPLTRFRKYLTDKGLWS 313
Cdd:cd02000  240 SRYRTKEEVEEWKKRDPILRLRKYLIEAGILT 271
E1_dh pfam00676
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ...
 53-344 5.36e-108

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: 318.50  E-value: 5.36e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286560   53 MTRMVWSRVLDQRSTALNRQGRLGFFAPTAGQEASQLASQFAMEKEDYLLPGYRDVPQLVQHGLPLREAFLWSRGHVA-- 130
Cdd:pfam00676   1 RRMMTLRRMEDARDALYKRQGIRGFYHLYAGQEAAQVGIAAALEPGDYIIPGYRDHGNLLARGLSLEEIFAELYGRVAkg 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286560  131 ------GNYYAEDLNALPPQIIIGAQYIQAAGVALGLKKRGKENVVFTYTGDGGSSQGDFYEAINFAGAYQANGVFIIQN 204
Cdd:pfam00676  81 kggsmhGYYGAKGNRFYGGNGILGAQVPLGAGIALAAKYRGKKEVAITLYGDGAANQGDFFEGLNFAALWKLPVIFVCEN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286560  205 NGFAISTPREKQTAAKTLAQKAVAAGIPGIQVDGMDPLAVYAIAKEARDWSAAGNGPVLIETLTYRYGPHTLSgDDPTRY 284
Cdd:pfam00676 161 NQYGISTPAERASASTTYADRARGYGIPGLHVDGMDPLAVYQASKFAAERARTGKGPFLIELVTYRYGGHSMS-DDPSTY 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488286560  285 RS-KEMDDEWVQKDPLTRFRKYLTDKGLWSEAKEEEIIEKTKEEIKVAIAEADKAPKQKVS 344
Cdd:pfam00676 240 RTrDEYEEVRKKKDPIQRFKEHLVSKGVWSEEELKAIEKEVRKEVEEAFKKAESAPEPHPE 300
odpA CHL00149
pyruvate dehydrogenase E1 component alpha subunit; Reviewed
 43-351 1.20e-39

pyruvate dehydrogenase E1 component alpha subunit; Reviewed


Pssm-ID: 177069 [Multi-domain]  Cd Length: 341  Bit Score: 143.47  E-value: 1.20e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286560  43 DLSDEELVELMTRMVWSRVLDQRSTALNRQGRL-GFFAPTAGQEASQLASQFAMEKEDYLLPGYRDVPQLVQHGLPLR-- 119
Cdd:CHL00149  16 NINSMWLLVLYEDMLLGRNFEDMCAQMYYRGKMfGFVHLYNGQEAVSTGVIKLLAETDYVCSTYRDHVHALSKGVPPKnv 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286560 120 --EAFLWSRGHVAGNYYAEDLNALPPQIIIGAQYI-QAAGVALG-----------LKKRGKENVVFTYTGDGGSSQGDFY 185
Cdd:CHL00149  96 maELFGKETGCSRGRGGSMHIFSAPHNFLGGFAFIgEGIPIALGaafqsiyrqqvLKEVQPLRVTACFFGDGTTNNGQFF 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286560 186 EAINFAGAYQANGVFIIQNNGFAISTPREKQTAAKTLAQKAVAAGIPGIQVDGMDPLAVYAIAKEARDWSAAGNGPVLIE 265
Cdd:CHL00149 176 ECLNMAVLWKLPIIFVVENNQWAIGMAHHRSTSIPEIHKKAEAFGLPGIEVDGMDVLAVREVAKEAVERARQGDGPTLIE 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286560 266 TLTYRYGPHTLSgdDPTRYRSKEMDDEWVQKDPLTRFRKYLTDKGLWSEAKEEEIIEKTKEEIKVAIAEADKAPKQKVSD 345
Cdd:CHL00149 256 ALTYRFRGHSLA--DPDELRSKQEKEAWVARDPIKKLKSYIIDNELASQKELNKIQREVKIEIEQAVQFAISSPEPNISD 333


                 ....*.
gi 488286560 346 FLKNMF 351
Cdd:CHL00149 334 LKKYLF 339
 
Name Accession Description Interval E-value
PDH_E1_alph_x TIGR03181
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the ...
 24-365 0e+00

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: 534.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286560   24 PTFQILDQDGKIVNEDLVPDLSDEELVELMTRMVWSRVLDQRSTALNRQGRLGFFAPTAGQEASQLASQFAMEKEDYLLP 103
Cdd:TIGR03181   1 ELVQVLDEDGNVVDPEPAPDLSDEELVELYRDMVLTRRFDTKALALQRQGRLGTYAPNLGQEAAQVGSALALRKDDWVFP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286560  104 GYRDVPQLVQHGLPLREAFLWSRGHVAGNYYAEDLNALPPQIIIGAQYIQAAGVALGLKKRGKENVVFTYTGDGGSSQGD 183
Cdd:TIGR03181  81 SYRDHAAMLARGVPLVEILLYWRGDERGSWDPEGVNILPPNIPIGTQYLHAAGVAYALKLRGEDNVAVTYFGDGGTSEGD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286560  184 FYEAINFAGAYQANGVFIIQNNGFAISTPREKQTAAKTLAQKAVAAGIPGIQVDGMDPLAVYAIAKEARDWSAAGNGPVL 263
Cdd:TIGR03181 161 FYEALNFAGVFKAPVVFFVQNNQWAISVPRSKQTAAPTLAQKAIAYGIPGVQVDGNDVLAVYAVTKEAVERARSGGGPTL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286560  264 IETLTYRYGPHTLSgDDPTRYRSKEMDDEWVQKDPLTRFRKYLTDKGLWSEAKEEEIIEKTKEEIKVAIAEADKAPKQKV 343
Cdd:TIGR03181 241 IEAVTYRLGPHTTA-DDPTRYRTKEEEEEWRKKDPILRLRKYLERKGLWDEEQEEALEEEAEAEVAEAVAEALALPPPPV 319

                         330       340
                  ....*....|....*....|..
gi 488286560  344 SDFLKNMFEVQPQTIKEQIAFY 365
Cdd:TIGR03181 320 DDIFDHVYAELPPELEEQRAEL 341
AcoA COG1071
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ...
 25-367 7.83e-147

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: 418.78  E-value: 7.83e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286560  25 TFQILDQDGKivnEDLVPDLSDEELVELMTRMVWSRVLDQRSTALNRQGRLGFFAPTAGQEASQLASQFAMEKEDYLLPG 104
Cdd:COG1071    1 LVQVLDPDGT---EAALPDLSKEELLELYRDMLLIRRFEERALALQRQGKIGFYHLSIGQEAAQVGAAAALRPGDWIFPT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286560 105 YRDVPQLVQHGLPLREAFLWSRGHVAGN---------YYAEDLNALPPQIIIGAQYIQAAGVALGLKKRGKENVVFTYTG 175
Cdd:COG1071   78 YRDHGHALARGVDPKELMAELFGKATGPskgrggsmhFFDKELNFLGGSGIVGGQLPHAVGAALAAKLRGEDEVAVAFFG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286560 176 DGGSSQGDFYEAINFAGAYQANGVFIIQNNGFAISTPREKQTAAKTLAQKAVAAGIPGIQVDGMDPLAVYAIAKEARDWS 255
Cdd:COG1071  158 DGATSEGDFHEALNFAAVWKLPVVFVCENNGYAISTPVERQTAVETIADRAAGYGIPGVRVDGNDVLAVYAAVKEAVERA 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286560 256 AAGNGPVLIETLTYRYGPHTLSgDDPTRYRSKEMDDEWVQKDPLTRFRKYLTDKGLWSEAKEEEIIEKTKEEIKVAIAEA 335
Cdd:COG1071  238 RAGEGPTLIEAKTYRLGGHSTS-DDPTRYRTKEEVEEWRERDPIERLRAYLLEEGLLTEEELEAIEAEAKAEVEEAVEFA 316

                        330       340       350
                 ....*....|....*....|....*....|..
gi 488286560 336 DKAPKQKVSDFLKNMFEVQPQTIKEQIAFYEA 367
Cdd:COG1071  317 EASPEPDPEELFDDVYAEPPPHLAEQRAELAA 348
TPP_E1_PDC_ADC_BCADC cd02000
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ...
 52-313 3.26e-112

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: 329.07  E-value: 3.26e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286560  52 LMTRMVWSRVLDQRSTALNRQGRLGFF-APTAGQEASQLASQFAMEKEDYLLPGYRDVPQLVQHGLPLREAFLWSRGHVA 130
Cdd:cd02000    1 LYRTMVLIRRFDERLLELYRQGKIGGFyHLSIGQEAVAVGVAAALRPGDWVFPTYRDHGHALARGVDLKEMLAELFGKET 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286560 131 GN---------YYAEDLNALPPQIIIGAQYIQAAGVALGLKKRGKENVVFTYTGDGGSSQGDFYEAINFAGAYQANGVFI 201
Cdd:cd02000   81 GPckgrggsmhIGDKEKNFFGGNGIVGGQVPLAAGAALALKYRGEDRVAVCFFGDGATNEGDFHEALNFAALWKLPVIFV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286560 202 IQNNGFAISTPREKQTAAKTLAQKAVAAGIPGIQVDGMDPLAVYAIAKEARDWSAAGNGPVLIETLTYRYGPHTLSgDDP 281
Cdd:cd02000  161 CENNGYAISTPTSRQTAGTSIADRAAAYGIPGIRVDGNDVLAVYEAAKEAVERARAGGGPTLIEAVTYRLGGHSTS-DDP 239

                        250       260       270
                 ....*....|....*....|....*....|..
gi 488286560 282 TRYRSKEMDDEWVQKDPLTRFRKYLTDKGLWS 313
Cdd:cd02000  240 SRYRTKEEVEEWKKRDPILRLRKYLIEAGILT 271
E1_dh pfam00676
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ...
 53-344 5.36e-108

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: 318.50  E-value: 5.36e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286560   53 MTRMVWSRVLDQRSTALNRQGRLGFFAPTAGQEASQLASQFAMEKEDYLLPGYRDVPQLVQHGLPLREAFLWSRGHVA-- 130
Cdd:pfam00676   1 RRMMTLRRMEDARDALYKRQGIRGFYHLYAGQEAAQVGIAAALEPGDYIIPGYRDHGNLLARGLSLEEIFAELYGRVAkg 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286560  131 ------GNYYAEDLNALPPQIIIGAQYIQAAGVALGLKKRGKENVVFTYTGDGGSSQGDFYEAINFAGAYQANGVFIIQN 204
Cdd:pfam00676  81 kggsmhGYYGAKGNRFYGGNGILGAQVPLGAGIALAAKYRGKKEVAITLYGDGAANQGDFFEGLNFAALWKLPVIFVCEN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286560  205 NGFAISTPREKQTAAKTLAQKAVAAGIPGIQVDGMDPLAVYAIAKEARDWSAAGNGPVLIETLTYRYGPHTLSgDDPTRY 284
Cdd:pfam00676 161 NQYGISTPAERASASTTYADRARGYGIPGLHVDGMDPLAVYQASKFAAERARTGKGPFLIELVTYRYGGHSMS-DDPSTY 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488286560  285 RS-KEMDDEWVQKDPLTRFRKYLTDKGLWSEAKEEEIIEKTKEEIKVAIAEADKAPKQKVS 344
Cdd:pfam00676 240 RTrDEYEEVRKKKDPIQRFKEHLVSKGVWSEEELKAIEKEVRKEVEEAFKKAESAPEPHPE 300
PDH_E1_alph_y TIGR03182
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the ...
 47-351 1.77e-60

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: 197.41  E-value: 1.77e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286560   47 EELVELMTRMVWSRVLDQRSTALNRQGRL-GFFAPTAGQEASQLASQFAMEKEDYLLPGYRDVPQLVQHGLPLREAFLWS 125
Cdd:TIGR03182   2 EELLELYRDMLLIRRFEEKAGQLYGMGKIgGFCHLYIGQEAVAVGLIAALKPDDYVITSYRDHGHALARGVPPKEVMAEL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286560  126 RGHVAGN---------YYAEDLNALPPQIIIGAQYIQAAGVALGLKKRGKENVVFTYTGDGGSSQGDFYEAINFAGAYQA 196
Cdd:TIGR03182  82 TGRETGCskgkggsmhMFDREKNFYGGHGIVGAQVPLATGLAFANKYRGNDNVTACFFGDGAANQGQFYESFNMAALWKL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286560  197 NGVFIIQNNGFAISTPREKQTAAKTLAQKAVAAGIPGIQVDGMDPLAVYAIAKEARDWSAAGNGPVLIETLTYRYGPHTL 276
Cdd:TIGR03182 162 PVIFVIENNLYAMGTAVERSSSVTDLYKRGESFGIPGERVDGMDVLAVREAAKEAVERARSGKGPILLEMKTYRFRGHSM 241

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488286560  277 SgdDPTRYRSKEMDDEWVQKDPLTRFRKYLTDKGLWSEAKEEEIIEKTKEEIKVAIAEADKAPKQKVSDFLKNMF 351
Cdd:TIGR03182 242 S--DPAKYRSKEEVEEWRKRDPIEKLKARLIEQGIASEEELKEIDKEVRAEVEEAVEFAENSPEPPVEELYTDVY 314
odpA CHL00149
pyruvate dehydrogenase E1 component alpha subunit; Reviewed
 43-351 1.20e-39

pyruvate dehydrogenase E1 component alpha subunit; Reviewed


Pssm-ID: 177069 [Multi-domain]  Cd Length: 341  Bit Score: 143.47  E-value: 1.20e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286560  43 DLSDEELVELMTRMVWSRVLDQRSTALNRQGRL-GFFAPTAGQEASQLASQFAMEKEDYLLPGYRDVPQLVQHGLPLR-- 119
Cdd:CHL00149  16 NINSMWLLVLYEDMLLGRNFEDMCAQMYYRGKMfGFVHLYNGQEAVSTGVIKLLAETDYVCSTYRDHVHALSKGVPPKnv 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286560 120 --EAFLWSRGHVAGNYYAEDLNALPPQIIIGAQYI-QAAGVALG-----------LKKRGKENVVFTYTGDGGSSQGDFY 185
Cdd:CHL00149  96 maELFGKETGCSRGRGGSMHIFSAPHNFLGGFAFIgEGIPIALGaafqsiyrqqvLKEVQPLRVTACFFGDGTTNNGQFF 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286560 186 EAINFAGAYQANGVFIIQNNGFAISTPREKQTAAKTLAQKAVAAGIPGIQVDGMDPLAVYAIAKEARDWSAAGNGPVLIE 265
Cdd:CHL00149 176 ECLNMAVLWKLPIIFVVENNQWAIGMAHHRSTSIPEIHKKAEAFGLPGIEVDGMDVLAVREVAKEAVERARQGDGPTLIE 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286560 266 TLTYRYGPHTLSgdDPTRYRSKEMDDEWVQKDPLTRFRKYLTDKGLWSEAKEEEIIEKTKEEIKVAIAEADKAPKQKVSD 345
Cdd:CHL00149 256 ALTYRFRGHSLA--DPDELRSKQEKEAWVARDPIKKLKSYIIDNELASQKELNKIQREVKIEIEQAVQFAISSPEPNISD 333


                 ....*.
gi 488286560 346 FLKNMF 351
Cdd:CHL00149 334 LKKYLF 339
PLN02374 PLN02374
pyruvate dehydrogenase (acetyl-transferring)
 44-351 3.78e-38

pyruvate dehydrogenase (acetyl-transferring)


Pssm-ID: 215213 [Multi-domain]  Cd Length: 433  Bit Score: 141.62  E-value: 3.78e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286560  44 LSDEELVELMTRMVWSRVLDQRSTALNRQGRL-GFFAPTAGQEASQLASQFAMEKEDYLLPGYRDVPQLVQHGLPLREAF 122
Cdd:PLN02374  83 VTREEGLELYEDMVLGRSFEDMCAQMYYRGKMfGFVHLYNGQEAVSTGFIKLLKKDDSVVSTYRDHVHALSKGVPARAVM 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286560 123 LWSRGHVAG---------NYYAEDLNALPPQIIIGAQYIQAAGVALG-------LKKRGKENVVFTYTGDGGSSQGDFYE 186
Cdd:PLN02374 163 SELFGKATGccrgqggsmHMFSKEHNLLGGFAFIGEGIPVATGAAFSskyrrevLKEESCDDVTLAFFGDGTCNNGQFFE 242

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286560 187 AINFAGAYQANGVFIIQNNGFAISTPREKQTAAKTLAQKAVAAGIPGIQVDGMDPLAVYAIAKEARDWSAAGNGPVLIET 266
Cdd:PLN02374 243 CLNMAALWKLPIVFVVENNLWAIGMSHLRATSDPEIWKKGPAFGMPGVHVDGMDVLKVREVAKEAIERARRGEGPTLVEC 322

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286560 267 LTYRYGPHTLSgdDPTRYRSKEMDDEWVQKDPLTRFRKYLTDKGLWSEAKEEEIIEKTKEEIKVAIAEADKAPKQKVSDF 346
Cdd:PLN02374 323 ETYRFRGHSLA--DPDELRDPAEKAHYAARDPIAALKKYLIENGLATEAELKAIEKKIDEVVEDAVEFADASPLPPRSQL 400


                 ....*
gi 488286560 347 LKNMF 351
Cdd:PLN02374 401 LENVF 405
PLN02269 PLN02269
Pyruvate dehydrogenase E1 component subunit alpha
 45-351 3.11e-35

Pyruvate dehydrogenase E1 component subunit alpha


Pssm-ID: 215152 [Multi-domain]  Cd Length: 362  Bit Score: 132.14  E-value: 3.11e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286560  45 SDEELVELMTRMVWSRVLDQRSTALNRqGRL--GFFAPTAGQEASQLASQFAMEKEDYLLPGYRDVPQLVQHGLPLREAF 122
Cdd:PLN02269  28 SKQELVDFFRDMYLMRRMEIAADSLYK-AKLirGFCHLYDGQEAVAVGMEAAITKEDAIITAYRDHCTHLGRGGTVLEVF 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286560 123 LWSRGHVAG---------NYYAEDLNALPPQIIIGAQYIQAAGVALGLKKRGKENVVFTYTGDGGSSQGDFYEAINFAGA 193
Cdd:PLN02269 107 AELMGRKDGcsrgkggsmHFYKKDANFYGGHGIVGAQVPLGAGLAFAQKYNKEENVAFALYGDGAANQGQLFEALNIAAL 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286560 194 YQANGVFIIQNNGFAISTPREKqtAAKTLAQKAVAAGIPGIQVDGMDPLAVYAIAKEARDWsAAGNGPVLIETLTYRYGP 273
Cdd:PLN02269 187 WDLPVIFVCENNHYGMGTAEWR--AAKSPAYYKRGDYVPGLKVDGMDVLAVKQACKFAKEH-ALSNGPIVLEMDTYRYHG 263

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286560 274 HTLSgdDP-TRYRSK-EMDDEWVQKDPLTRFRKYLTDKGLWSEAKEEEIIEKTKEEIKVAIAEADKAPKQKVSDFLKNMF 351
Cdd:PLN02269 264 HSMS--DPgSTYRTRdEISGVRQERDPIERVRKLLLAHELATEAELKDIEKEIRKEVDDAVAKAKESPMPDPSELFTNVY 341
TPP_TK cd02012
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ...
 154-264 2.15e-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: 60.60  E-value: 2.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286560 154 AAGVALGLKKRGKENVVFTYTGDGGSSQGDFYEAINFAGAYQ-ANGVFIIQNNGFAISTPREKQTAAKTLAQKAVAAGIP 232
Cdd:cd02012  114 AVGMALAEKLLGFDYRVYVLLGDGELQEGSVWEAASFAGHYKlDNLIAIVDSNRIQIDGPTDDILFTEDLAKKFEAFGWN 193

                         90       100       110
                 ....*....|....*....|....*....|..
gi 488286560 233 GIQVDGMDPLAVYAIAKEARdwsAAGNGPVLI 264
Cdd:cd02012  194 VIEVDGHDVEEILAALEEAK---KSKGKPTLI 222
TPP_DXS cd02007
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ...
 154-268 3.57e-05

Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; 1-Deoxy-D-xylulose-5-phosphate synthase (DXS) is a regulatory enzyme of the mevalonate-independent pathway involved in terpenoid biosynthesis. Terpeniods are plant natural products with important pharmaceutical activity. DXS catalyzes a transketolase-type condensation of pyruvate with D-glyceraldehyde-3-phosphate to form 1-deoxy-D-xylulose-5-phosphate (DXP) and carbon dioxide. The formation of DXP leads to the formation of the terpene precursor IPP (isopentyl diphosphate) and to the formation of thiamine (vitamin B1) and pyridoxal (vitamin B6).


Pssm-ID: 238965 [Multi-domain]  Cd Length: 195  Bit Score: 44.07  E-value: 3.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286560 154 AAGVALGLKKRGKENVVFTYTGDGGSSQGDFYEAINFAGAYQANGVFIIQNNGFAISTPREKQTAA-KTLAQKAVaaGIp 232
Cdd:cd02007   84 ALGMAVARDLKGKKRKVIAVIGDGALTGGMAFEALNNAGYLKSNMIVILNDNEMSISPNVGTPGNLfEELGFRYI--GP- 160

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 488286560 233 giqVDGMDPLAVYAIAKEARDwsaaGNGPVLIETLT 268
Cdd:cd02007  161 ---VDGHNIEALIKVLKEVKD----LKGPVLLHVVT 189
TPP_enzymes cd00568
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ...
 153-265 4.02e-05

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: 43.40  E-value: 4.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286560 153 QAAGVALGLKKRGKENVVFTYTGDGGssqgdFYEAIN---FAGAYQANGVFIIQNNG-----------FAISTPREKQTA 218
Cdd:cd00568   50 YGLPAAIGAALAAPDRPVVCIAGDGG-----FMMTGQelaTAVRYGLPVIVVVFNNGgygtirmhqeaFYGGRVSGTDLS 124

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 488286560 219 AKTLAQKAVAAGIPGIQVDgmDPLAVYAIAKEARdwsaAGNGPVLIE 265
Cdd:cd00568  125 NPDFAALAEAYGAKGVRVE--DPEDLEAALAEAL----AAGGPALIE 165
TPP_E1_OGDC_like cd02016
Thiamine pyrophosphate (TPP) family, E1 of OGDC-like subfamily, TPP-binding module; composed ...
 175-282 7.53e-04

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: 40.59  E-value: 7.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286560 175 GDGG-SSQGDFYEAINFAG--AYQANG-VFIIQNN--GFAISTPREKQTAAKTLAQKAVaaGIPGIQVDGMDPLAVYAIA 248
Cdd:cd02016  148 GDAAfAGQGVVYETLNLSNlpGYTTGGtIHIVVNNqiGFTTDPRDSRSSPYCTDVAKMI--GAPIFHVNGDDPEAVVRAT 225

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 488286560 249 KEARDWSAAGNGPVLIETLTYR-YGpHTlSGDDPT 282
Cdd:cd02016  226 RLALEYRQKFKKDVVIDLVCYRrHG-HN-ELDEPS 258
TPP_enzyme_C pfam02775
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
154-265 1.05e-03

Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;


Pssm-ID: 460689 [Multi-domain]  Cd Length: 151  Bit Score: 39.11  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286560  154 AAGVALGLKKRGKENVVFTYTGDGGssqgdFYEAIN-FAGA--YQANGVFIIQNN--------------GFAISTPREKQ 216
Cdd:pfam02775  33 GLPAAIGAKLARPDRPVVAIAGDGG-----FQMNLQeLATAvrYNLPITVVVLNNggygmtrgqqtpfgGGRYSGPSGKI 107

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 488286560  217 TAAKTLAQKAVAAGIPGIQVDgmDPLAVYAIAKEARdwsaAGNGPVLIE 265
Cdd:pfam02775 108 LPPVDFAKLAEAYGAKGARVE--SPEELEEALKEAL----EHDGPALID 150
PLN02582 PLN02582
1-deoxy-D-xylulose-5-phosphate synthase
 156-205 1.41e-03

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


Pssm-ID: 178194 [Multi-domain]  Cd Length: 677  Bit Score: 40.65  E-value: 1.41e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 488286560 156 GVALGLKKRGKENVVFTYTGDGGSSQGDFYEAINFAGAYQANGVFIIQNN 205
Cdd:PLN02582 155 GMAVGRDLKGKKNNVVAVIGDGAMTAGQAYEAMNNAGYLDSDMIVILNDN 204
PRK05899 PRK05899
transketolase; Reviewed
 154-265 1.55e-03

transketolase; Reviewed


Pssm-ID: 235639 [Multi-domain]  Cd Length: 586  Bit Score: 40.50  E-value: 1.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488286560 154 AAGVALGLKKRGKE------NVV--FTYT--GDGGSSQGDFYEAINFAGAYQ-ANGVFIIQNNGFAISTPREKQTAAKTl 222
Cdd:PRK05899 127 AVGMALAEKYLAALfnrpglDIVdhYTYVlcGDGDLMEGISHEACSLAGHLKlGNLIVIYDDNRISIDGPTEGWFTEDV- 205

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 488286560 223 AQKAVAAGIPGIQVDGMDPLAVYAIAKEARdwsaAGNGPVLIE 265
Cdd:PRK05899 206 KKRFEAYGWHVIEVDGHDVEAIDAAIEEAK----ASTKPTLII 244
PLN02234 PLN02234
1-deoxy-D-xylulose-5-phosphate synthase
 156-205 3.72e-03

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


Pssm-ID: 177878 [Multi-domain]  Cd Length: 641  Bit Score: 39.31  E-value: 3.72e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 488286560 156 GVALGLKKRGKENVVFTYTGDGGSSQGDFYEAINFAGAYQANGVFIIQNN 205
Cdd:PLN02234 188 GMAVGRDLKGMNNSVVSVIGDGAMTAGQAYEAMNNAGYLHSNMIVILNDN 237
PB1 pfam00564
PB1 domain;
8-54 7.69e-03

PB1 domain;


Pssm-ID: 395447  Cd Length: 84  Bit Score: 35.35  E-value: 7.69e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 488286560    8 KPIDFKELMAKVDADFP----TFQI--LDQDGkivneDLVPDLSDEELVELMT 54
Cdd:pfam00564  20 RGISFEELRALVEQRFGlddvDFKLkyPDEDG-----DLVSLTSDEDLEEALE 67
 
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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