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Conserved domains on  [gi|2668426475|ref|WP_330425272|]
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MULTISPECIES: transketolase C-terminal domain-containing protein [unclassified Butyricicoccus]

Protein Classification

transketolase family protein( domain architecture ID 11467696)

transketolase family protein similar to Sinorhizobium fredii Y4mN

EC:  2.2.1.-
Gene Ontology:  GO:0016740

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TktA2 COG3958
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
2-215 1.24e-102

Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];


:

Pssm-ID: 443158 [Multi-domain]  Cd Length: 308  Bit Score: 299.31  E-value: 1.24e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668426475   2 FDQAFLAAGYSELPVHVIGSDPGVCAAFNGATHMPFEDCALYMNIPNAVVIDSCDFAQTKALTRKLAACGSPSYMRLIRK 81
Cdd:COG3958    86 YEQIRNDIAYPNLNVKIVGSHAGLSYGEDGATHQALEDIALMRALPNMTVIVPADAVETEAAVRAAAEHDGPVYLRLGRG 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668426475  82 GFTTVYADGSDFEIGKGVTLRDGKDVTIIASGILVDEALKAEEQLAAQGISARVIDMHTWKPLDEELVLRAAAETGCIVT 161
Cdd:COG3958   166 AVPVVYDEDYEFEIGKARVLREGKDVTIIATGIMVAEALEAAELLAKEGISARVINMHTIKPLDEEAILKAARKTGAVVT 245

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2668426475 162 AENHQVGTGLGSAITNLTSAKNPVPVERIGIQNRFGQVGPQDFLMQQYNLTAED 215
Cdd:COG3958   246 AEEHSIIGGLGSAVAEVLAENYPVPLRRIGVPDRFGESGSPEELLEKYGLDAEG 299
 
Name Accession Description Interval E-value
TktA2 COG3958
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
2-215 1.24e-102

Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];


Pssm-ID: 443158 [Multi-domain]  Cd Length: 308  Bit Score: 299.31  E-value: 1.24e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668426475   2 FDQAFLAAGYSELPVHVIGSDPGVCAAFNGATHMPFEDCALYMNIPNAVVIDSCDFAQTKALTRKLAACGSPSYMRLIRK 81
Cdd:COG3958    86 YEQIRNDIAYPNLNVKIVGSHAGLSYGEDGATHQALEDIALMRALPNMTVIVPADAVETEAAVRAAAEHDGPVYLRLGRG 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668426475  82 GFTTVYADGSDFEIGKGVTLRDGKDVTIIASGILVDEALKAEEQLAAQGISARVIDMHTWKPLDEELVLRAAAETGCIVT 161
Cdd:COG3958   166 AVPVVYDEDYEFEIGKARVLREGKDVTIIATGIMVAEALEAAELLAKEGISARVINMHTIKPLDEEAILKAARKTGAVVT 245

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2668426475 162 AENHQVGTGLGSAITNLTSAKNPVPVERIGIQNRFGQVGPQDFLMQQYNLTAED 215
Cdd:COG3958   246 AEEHSIIGGLGSAVAEVLAENYPVPLRRIGVPDRFGESGSPEELLEKYGLDAEG 299
Transketolase_C pfam02780
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ...
 96-215 2.07e-31

Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as a regulatory molecule binding site.


Pssm-ID: 460693 [Multi-domain]  Cd Length: 124  Bit Score: 111.53  E-value: 2.07e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668426475  96 GKGVTLRDGKDVTIIASGILVDEALKAEEQLAAQGISARVIDMHTWKPLDEELVLRAAAETGCIVTAENHQVGTGLGSAI 175
Cdd:pfam02780   1 GKAEILREGDDVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLDKETILESVKKTGRLVTVEEAVPRGGFGSEV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2668426475 176 TNLTSAKN----PVPVERIGIQnRFGQVGPQDFLMQQYNLTAED 215
Cdd:pfam02780  81 AAALAEEAfdglDAPVLRVGGP-DFPEPGSADELEKLYGLTPEK 123
PRK05444 PRK05444
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
 31-215 1.08e-27

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


Pssm-ID: 235470 [Multi-domain]  Cd Length: 580  Bit Score: 110.17  E-value: 1.08e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668426475  31 GATHMPFEDCALYMNIPNAVVIDSCDFAQTKALTRK-LAACGSPSYMRLIR-KGFTTVYADGSDFEIGKGVTLRDGKDVT 108
Cdd:PRK05444  388 GPTHQGAFDLSYLRCIPNMVIMAPSDENELRQMLYTaLAYDDGPIAIRYPRgNGVGVELPELEPLPIGKGEVLREGEDVA 467

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668426475 109 IIASGILVDEALKAEEQLAaqgiSARVIDMHTWKPLDEELVLRAAAETGCIVTAENHQVGTGLGSAITNLTSAKN-PVPV 187
Cdd:PRK05444  468 ILAFGTMLAEALKAAERLA----SATVVDARFVKPLDEELLLELAAKHDLVVTVEEGAIMGGFGSAVLEFLADHGlDVPV 543

                         170       180
                  ....*....|....*....|....*...
gi 2668426475 188 ERIGIQNRFGQVGPQDFLMQQYNLTAED 215
Cdd:PRK05444  544 LNLGLPDEFIDHGSREELLAELGLDAEG 571
TPP_PYR_DXS_TK_like cd07033
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ...
 1-80 1.92e-18

Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), transketolase (TK), and related proteins; Thiamine pyrophosphate (TPP) family, pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), transketolase (TK), and the beta subunits of the E1 component of the human pyruvate dehydrogenase complex (E1- PDHc), subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Like many TPP-dependent enzymes DXS and TK are homodimers having a PYR and a PP domain on the same subunit. TK has two active sites per dimer which lie between PYR and PP domains of different subunits. For DXS each active site is located at the interface of a PYR and a PP domain from the same subunit. E1-PDHc is an alpha2beta2 dimer-of-heterodimers having two active sites but having the PYR and PP domains arranged on separate subunits, the PYR domains on the beta subunits, the PP domains on the alpha subunits. DXS is a regulatory enzyme of the mevalonate-independent pathway involved in terpenoid biosynthesis, it catalyzes a transketolase-type condensation of pyruvate with D-glyceraldehyde-3-phosphate to form 1-deoxy-D-xylulose-5-phosphate (DXP) and carbon dioxide. 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. TK also plays a central role in the Calvin cycle in plants. PDHc catalyzes the irreversible oxidative decarboxylation of pyruvate to produce acetyl-CoA in the bridging step between glycolysis and the citric acid cycle. This subfamily includes the beta subunits of the E1 component of the acetoin dehydrogenase complex (ADC) and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC). ADC participates in the breakdown of acetoin. BCADC catalyzes the oxidative decarboxylation of 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate during the breakdown of branched chain amino acids.


Pssm-ID: 132916 [Multi-domain]  Cd Length: 156  Bit Score: 78.64  E-value: 1.92e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668426475   1 MFDQAFLAAGYSELPVHVIGSDPGVCAAFNGATHMPFEDCALYMNIPNAVVIDSCDFAQTKALTRKLAACGSPSYMRLIR 80
Cdd:cd07033    77 AYDQIRHDVALQNLPVKFVGTHAGISVGEDGPTHQGIEDIALLRAIPNMTVLRPADANETAAALEAALEYDGPVYIRLPR 156
Transket_pyr smart00861
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ...
 1-82 8.25e-11

Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer of a two-carbon ketol unit from xylulose 5-phosphate to an aldose receptor, such as ribose 5-phosphate, to form sedoheptulose 7-phosphate and glyceraldehyde 3- phosphate. This enzyme, together with transaldolase, provides a link between the glycolytic and pentose-phosphate pathways. TK requires thiamine pyrophosphate as a cofactor. In most sources where TK has been purified, it is a homodimer of approximately 70 Kd subunits. TK sequences from a variety of eukaryotic and prokaryotic sources show that the enzyme has been evolutionarily conserved. In the peroxisomes of methylotrophic yeast Hansenula polymorpha, there is a highly related enzyme, dihydroxy-acetone synthase (DHAS) (also known as formaldehyde transketolase), which exhibits a very unusual specificity by including formaldehyde amongst its substrates.


Pssm-ID: 214865 [Multi-domain]  Cd Length: 136  Bit Score: 57.88  E-value: 8.25e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668426475    1 MFDQAFLAAGYSELPVhVIGSDPGVCAAFNGATHMPFEDCALYMNIPNAVVIDSCDFAQTKALTRKLAACGSPSYMRLIR 80
Cdd:smart00861  53 AKDQIRSAGASGNVPV-VFRHDGGGGVGEDGPTHHSIEDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDGPVVIRLER 131


                   ..
gi 2668426475   81 KG 82
Cdd:smart00861 132 KS 133
 
Name Accession Description Interval E-value
TktA2 COG3958
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
2-215 1.24e-102

Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];


Pssm-ID: 443158 [Multi-domain]  Cd Length: 308  Bit Score: 299.31  E-value: 1.24e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668426475   2 FDQAFLAAGYSELPVHVIGSDPGVCAAFNGATHMPFEDCALYMNIPNAVVIDSCDFAQTKALTRKLAACGSPSYMRLIRK 81
Cdd:COG3958    86 YEQIRNDIAYPNLNVKIVGSHAGLSYGEDGATHQALEDIALMRALPNMTVIVPADAVETEAAVRAAAEHDGPVYLRLGRG 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668426475  82 GFTTVYADGSDFEIGKGVTLRDGKDVTIIASGILVDEALKAEEQLAAQGISARVIDMHTWKPLDEELVLRAAAETGCIVT 161
Cdd:COG3958   166 AVPVVYDEDYEFEIGKARVLREGKDVTIIATGIMVAEALEAAELLAKEGISARVINMHTIKPLDEEAILKAARKTGAVVT 245

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2668426475 162 AENHQVGTGLGSAITNLTSAKNPVPVERIGIQNRFGQVGPQDFLMQQYNLTAED 215
Cdd:COG3958   246 AEEHSIIGGLGSAVAEVLAENYPVPLRRIGVPDRFGESGSPEELLEKYGLDAEG 299
Dxs COG1154
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ...
 31-215 1.63e-34

Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and metabolism]; Deoxyxylulose-5-phosphate synthase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis


Pssm-ID: 440768 [Multi-domain]  Cd Length: 623  Bit Score: 129.36  E-value: 1.63e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668426475  31 GATHMPFEDCALYMNIPNAVVIDSCDFAQTKALTRKLAACGSPSymrLIR--KG---FTTVYADGSDFEIGKGVTLRDGK 105
Cdd:COG1154   426 GPTHHGVFDLSYLRCIPNMVIMAPKDENELRHMLYTALAYDGPT---AIRypRGngpGVELPAELEPLPIGKGEVLREGK 502

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668426475 106 DVTIIASGILVDEALKAEEQLAAQGISARVIDMHTWKPLDEELVLRAAAETGCIVTAENHQVGTGLGSAITNLTSAKN-P 184
Cdd:COG1154   503 DVAILAFGTMVAEALEAAERLAAEGISATVVDARFVKPLDEELILELAREHDLVVTVEEGVLAGGFGSAVLEFLADAGlD 582

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2668426475 185 VPVERIGIQNRFGQVGPQDFLMQQYNLTAED 215
Cdd:COG1154   583 VPVLRLGLPDRFIEHGSRAELLAELGLDAEG 613
Transketolase_C pfam02780
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ...
 96-215 2.07e-31

Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as a regulatory molecule binding site.


Pssm-ID: 460693 [Multi-domain]  Cd Length: 124  Bit Score: 111.53  E-value: 2.07e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668426475  96 GKGVTLRDGKDVTIIASGILVDEALKAEEQLAAQGISARVIDMHTWKPLDEELVLRAAAETGCIVTAENHQVGTGLGSAI 175
Cdd:pfam02780   1 GKAEILREGDDVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLDKETILESVKKTGRLVTVEEAVPRGGFGSEV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2668426475 176 TNLTSAKN----PVPVERIGIQnRFGQVGPQDFLMQQYNLTAED 215
Cdd:pfam02780  81 AAALAEEAfdglDAPVLRVGGP-DFPEPGSADELEKLYGLTPEK 123
PRK05444 PRK05444
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
 31-215 1.08e-27

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


Pssm-ID: 235470 [Multi-domain]  Cd Length: 580  Bit Score: 110.17  E-value: 1.08e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668426475  31 GATHMPFEDCALYMNIPNAVVIDSCDFAQTKALTRK-LAACGSPSYMRLIR-KGFTTVYADGSDFEIGKGVTLRDGKDVT 108
Cdd:PRK05444  388 GPTHQGAFDLSYLRCIPNMVIMAPSDENELRQMLYTaLAYDDGPIAIRYPRgNGVGVELPELEPLPIGKGEVLREGEDVA 467

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668426475 109 IIASGILVDEALKAEEQLAaqgiSARVIDMHTWKPLDEELVLRAAAETGCIVTAENHQVGTGLGSAITNLTSAKN-PVPV 187
Cdd:PRK05444  468 ILAFGTMLAEALKAAERLA----SATVVDARFVKPLDEELLLELAAKHDLVVTVEEGAIMGGFGSAVLEFLADHGlDVPV 543

                         170       180
                  ....*....|....*....|....*...
gi 2668426475 188 ERIGIQNRFGQVGPQDFLMQQYNLTAED 215
Cdd:PRK05444  544 LNLGLPDEFIDHGSREELLAELGLDAEG 571
PRK05899 PRK05899
transketolase; Reviewed
 1-216 1.73e-26

transketolase; Reviewed


Pssm-ID: 235639 [Multi-domain]  Cd Length: 586  Bit Score: 106.76  E-value: 1.73e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668426475   1 MFDQAFLAAgYSELPVHVIGSDPGVCAAFNGATHMPFEDCALYMNIPNAVVIDSCDFAQTKALTRK-LAACGSPSYMRLI 79
Cdd:PRK05899  368 ARNAIRLAA-LMKLPVIYVFTHDSIGVGEDGPTHQPVEQLASLRAIPNLTVIRPADANETAAAWKYaLERKDGPSALVLT 446

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668426475  80 RKGFTTVYADGSDFEIGKG-VTLRDGKDVTIIASGILVDEALKAEEQLAAQGISARVIDMHTWKPLDEELvlrAAAETGC 158
Cdd:PRK05899  447 RQNLPVLERTAQEEGVAKGgYVLRDDPDVILIATGSEVHLALEAADELEAEGIKVRVVSMPSTELFDEQD---AAYKESV 523

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2668426475 159 IVTAENHQVGtgLGSAITNLTSAKNPVPVERIGIqNRFGQVGPQDFLMQQYNLTAEDI 216
Cdd:PRK05899  524 LPAAVTARVA--VEAGVADGWYKYVGLDGKVLGI-DTFGASAPADELFKEFGFTVENI 578
PRK12571 PRK12571
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
 2-215 2.97e-21

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


Pssm-ID: 183601 [Multi-domain]  Cd Length: 641  Bit Score: 91.71  E-value: 2.97e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668426475   2 FDQAFLAAGYSELPVHVIGSDPGVCAAfNGATHMPFEDCALYMNIPNAVVIDSCDFAQTKALTRKLAACGS-PSYMRLIR 80
Cdd:PRK12571  400 YDQLLHDVALQNLPVRFVLDRAGLVGA-DGATHAGAFDLAFLTNLPNMTVMAPRDEAELRHMLRTAAAHDDgPIAVRFPR 478

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668426475  81 KGFTTVY--ADGSDFEIGKGVTLRDGKDVTIIASGILVDEALKAEEQLAAQGISARVIDMHTWKPLDEELVLRAAAETGC 158
Cdd:PRK12571  479 GEGVGVEipAEGTILGIGKGRVPREGPDVAILSVGAHLHECLDAADLLEAEGISVTVADPRFVKPLDEALTDLLVRHHIV 558

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2668426475 159 IVTAENHQVGtGLGSAITNLTSAKNP----VPVERIGIQNRFGQVGPQDFLMQQYNLTAED 215
Cdd:PRK12571  559 VIVEEQGAMG-GFGAHVLHHLADTGLldggLKLRTLGLPDRFIDHASREEMYAEAGLTAPD 618
AcoB COG0022
Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta ...
 94-175 1.15e-20

Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta subunit [Energy production and conversion]; Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta subunit is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 439793 [Multi-domain]  Cd Length: 325  Bit Score: 88.15  E-value: 1.15e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668426475  94 EIGKGVTLRDGKDVTIIASGILVDEALKAEEQLAAQGISARVIDMHTWKPLDEELVLRAAAETG-CIVTAENHQVGtGLG 172
Cdd:COG0022   191 PLGKARVVREGTDVTIVTYGAMVHRALEAAEELAEEGISAEVIDLRTLSPLDEETILESVKKTGrLVVVDEAPRTG-GFG 269


                  ...
gi 2668426475 173 SAI 175
Cdd:COG0022   270 AEI 272
TPP_PYR_DXS_TK_like cd07033
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ...
 1-80 1.92e-18

Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), transketolase (TK), and related proteins; Thiamine pyrophosphate (TPP) family, pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), transketolase (TK), and the beta subunits of the E1 component of the human pyruvate dehydrogenase complex (E1- PDHc), subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Like many TPP-dependent enzymes DXS and TK are homodimers having a PYR and a PP domain on the same subunit. TK has two active sites per dimer which lie between PYR and PP domains of different subunits. For DXS each active site is located at the interface of a PYR and a PP domain from the same subunit. E1-PDHc is an alpha2beta2 dimer-of-heterodimers having two active sites but having the PYR and PP domains arranged on separate subunits, the PYR domains on the beta subunits, the PP domains on the alpha subunits. DXS is a regulatory enzyme of the mevalonate-independent pathway involved in terpenoid biosynthesis, it catalyzes a transketolase-type condensation of pyruvate with D-glyceraldehyde-3-phosphate to form 1-deoxy-D-xylulose-5-phosphate (DXP) and carbon dioxide. 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. TK also plays a central role in the Calvin cycle in plants. PDHc catalyzes the irreversible oxidative decarboxylation of pyruvate to produce acetyl-CoA in the bridging step between glycolysis and the citric acid cycle. This subfamily includes the beta subunits of the E1 component of the acetoin dehydrogenase complex (ADC) and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC). ADC participates in the breakdown of acetoin. BCADC catalyzes the oxidative decarboxylation of 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate during the breakdown of branched chain amino acids.


Pssm-ID: 132916 [Multi-domain]  Cd Length: 156  Bit Score: 78.64  E-value: 1.92e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668426475   1 MFDQAFLAAGYSELPVHVIGSDPGVCAAFNGATHMPFEDCALYMNIPNAVVIDSCDFAQTKALTRKLAACGSPSYMRLIR 80
Cdd:cd07033    77 AYDQIRHDVALQNLPVKFVGTHAGISVGEDGPTHQGIEDIALLRAIPNMTVLRPADANETAAALEAALEYDGPVYIRLPR 156
PRK11892 PRK11892
pyruvate dehydrogenase subunit beta; Provisional
 95-163 2.41e-17

pyruvate dehydrogenase subunit beta; Provisional


Pssm-ID: 237011 [Multi-domain]  Cd Length: 464  Bit Score: 79.96  E-value: 2.41e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2668426475  95 IGKGVTLRDGKDVTIIASGILVDEALKAEEQLAAQGISARVIDMHTWKPLDEELVLRAAAETGCIVTAE 163
Cdd:PRK11892  331 IGKARIHREGKDVTIVSFSIGMTYALKAAEELAKEGIDAEVIDLRTIRPMDTETIVESVKKTNRLVTVE 399
PRK09212 PRK09212
pyruvate dehydrogenase subunit beta; Validated
 94-190 2.64e-17

pyruvate dehydrogenase subunit beta; Validated


Pssm-ID: 169719 [Multi-domain]  Cd Length: 327  Bit Score: 79.00  E-value: 2.64e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668426475  94 EIGKGVTLRDGKDVTIIASGILVDEALKAEEQLAAQGISARVIDMHTWKPLDEELVLRAAAETGCIVTAENHQVGTGLGS 173
Cdd:PRK09212  191 PIGKAAILREGSDVTIVTFSIQVKLALEAAELLEKEGISVEVIDLRTLRPLDTETIIESVKKTNRLVVVEEGWPFAGVGA 270

                          90       100
                  ....*....|....*....|.
gi 2668426475 174 AITNLTSAKN----PVPVERI 190
Cdd:PRK09212  271 EIAALIMKEAfdylDAPVERV 291
PTZ00182 PTZ00182
3-methyl-2-oxobutanate dehydrogenase; Provisional
 94-176 4.01e-17

3-methyl-2-oxobutanate dehydrogenase; Provisional


Pssm-ID: 185502 [Multi-domain]  Cd Length: 355  Bit Score: 78.87  E-value: 4.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668426475  94 EIGKGVTLRDGKDVTIIASGILVDEALKAEEQLAAQGISARVIDMHTWKPLDEELVLRAAAETGCIVTAENHQVGTGLGS 173
Cdd:PTZ00182  223 PLGKAKVVREGKDVTIVGYGSQVHVALKAAEELAKEGISCEVIDLRSLRPWDRETIVKSVKKTGRCVIVHEAPPTCGIGA 302


                  ...
gi 2668426475 174 AIT 176
Cdd:PTZ00182  303 EIA 305
PLN02683 PLN02683
pyruvate dehydrogenase E1 component subunit beta
 95-190 3.66e-15

pyruvate dehydrogenase E1 component subunit beta


Pssm-ID: 215368 [Multi-domain]  Cd Length: 356  Bit Score: 73.32  E-value: 3.66e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668426475  95 IGKGVTLRDGKDVTIIASGILVDEALKAEEQLAAQGISARVIDMHTWKPLDEELVLRAAAETGCIVTAE----NHQVGTG 170
Cdd:PLN02683  219 IGKAKIEREGKDVTIVAFSKMVGYALKAAEILAKEGISAEVINLRSIRPLDRDTINASVRKTNRLVTVEegwpQHGVGAE 298

                          90       100
                  ....*....|....*....|
gi 2668426475 171 LGSAITNLTSAKNPVPVERI 190
Cdd:PLN02683  299 ICASVVEESFDYLDAPVERI 318
PLN02582 PLN02582
1-deoxy-D-xylulose-5-phosphate synthase
 2-175 4.69e-11

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


Pssm-ID: 178194 [Multi-domain]  Cd Length: 677  Bit Score: 61.84  E-value: 4.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668426475   2 FDQAFLAAGYSELPVHVIGSDPGVCAAfNGATHMPFEDCALYMNIPNAVVIDSCDFAQTKALTRKLAAC-GSPSYMRLIR 80
Cdd:PLN02582  437 YDQVVHDVDLQKLPVRFAMDRAGLVGA-DGPTHCGAFDVTYMACLPNMVVMAPSDEAELFHMVATAAAIdDRPSCFRYPR 515

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668426475  81 KGFTTVYA----DGSDFEIGKGVTLRDGKDVTIIASGILVDEALKAEEQLAAQGISARVIDMHTWKPLDEELVLRAAAET 156
Cdd:PLN02582  516 GNGIGVQLppnnKGIPIEVGKGRILLEGERVALLGYGTAVQSCLAAASLLERHGLSATVADARFCKPLDRALIRSLAKSH 595

                         170
                  ....*....|....*....
gi 2668426475 157 GCIVTAENHQVGtGLGSAI 175
Cdd:PLN02582  596 EVLITVEEGSIG-GFGSHV 613
Transket_pyr smart00861
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ...
 1-82 8.25e-11

Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer of a two-carbon ketol unit from xylulose 5-phosphate to an aldose receptor, such as ribose 5-phosphate, to form sedoheptulose 7-phosphate and glyceraldehyde 3- phosphate. This enzyme, together with transaldolase, provides a link between the glycolytic and pentose-phosphate pathways. TK requires thiamine pyrophosphate as a cofactor. In most sources where TK has been purified, it is a homodimer of approximately 70 Kd subunits. TK sequences from a variety of eukaryotic and prokaryotic sources show that the enzyme has been evolutionarily conserved. In the peroxisomes of methylotrophic yeast Hansenula polymorpha, there is a highly related enzyme, dihydroxy-acetone synthase (DHAS) (also known as formaldehyde transketolase), which exhibits a very unusual specificity by including formaldehyde amongst its substrates.


Pssm-ID: 214865 [Multi-domain]  Cd Length: 136  Bit Score: 57.88  E-value: 8.25e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668426475    1 MFDQAFLAAGYSELPVhVIGSDPGVCAAFNGATHMPFEDCALYMNIPNAVVIDSCDFAQTKALTRKLAACGSPSYMRLIR 80
Cdd:smart00861  53 AKDQIRSAGASGNVPV-VFRHDGGGGVGEDGPTHHSIEDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDGPVVIRLER 131


                   ..
gi 2668426475   81 KG 82
Cdd:smart00861 132 KS 133
PLN02234 PLN02234
1-deoxy-D-xylulose-5-phosphate synthase
 2-178 4.25e-10

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


Pssm-ID: 177878 [Multi-domain]  Cd Length: 641  Bit Score: 58.96  E-value: 4.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668426475   2 FDQAFLAAGYSELPVHVIGSDPGVCAAfNGATHMPFEDCALYMNIPNAVVIDSCDFAQTKALTRKLAACGS-PSYMRLIR 80
Cdd:PLN02234  438 YDQVVHDVDLQKLPVRFAIDRAGLMGA-DGPTHCGAFDVTFMACLPNMIVMAPSDEAELFNMVATAAAIDDrPSCFRYHR 516

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668426475  81 KGFTTVYA----DGSDFEIGKGVTLRDGKDVTIIASGILVDEALKAEEQLAAQGISARVIDMHTWKPLDEELVLRAAAET 156
Cdd:PLN02234  517 GNGIGVSLppgnKGVPLQIGRGRILRDGERVALLGYGSAVQRCLEAASMLSERGLKITVADARFCKPLDVALIRSLAKSH 596

                         170       180
                  ....*....|....*....|..
gi 2668426475 157 GCIVTAENHQVGtGLGSAITNL 178
Cdd:PLN02234  597 EVLITVEEGSIG-GFGSHVVQF 617
PLN02225 PLN02225
1-deoxy-D-xylulose-5-phosphate synthase
 18-180 5.99e-08

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


Pssm-ID: 177870 [Multi-domain]  Cd Length: 701  Bit Score: 52.79  E-value: 5.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668426475  18 VIGSD-PGVCAAFngathmpfeDCALYMNIPNAVVIDSCDFAQTKALTRKLA-ACGSPSYMRLIRKGFTT---VYADGSD 92
Cdd:PLN02225  485 LVGSDgPVQCGAF---------DIAFMSSLPNMIAMAPADEDELVNMVATAAyVTDRPVCFRFPRGSIVNmnyLVPTGLP 555

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668426475  93 FEIGKGVTLRDGKDVTIIASGILVDEALKAEEQLAAQGISARVIDMHTWKPLDEELVLRAAAETGCIVTAENHQVGtGLG 172
Cdd:PLN02225  556 IEIGRGRVLVEGQDVALLGYGAMVQNCLHAHSLLSKLGLNVTVADARFCKPLDIKLVRDLCQNHKFLITVEEGCVG-GFG 634


                  ....*...
gi 2668426475 173 SAITNLTS 180
Cdd:PLN02225  635 SHVAQFIA 642
PRK12315 PRK12315
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
 6-214 4.73e-07

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


Pssm-ID: 237053 [Multi-domain]  Cd Length: 581  Bit Score: 49.62  E-value: 4.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668426475   6 FLAAGYSELPVHV-IGSDPGVCAAFNG------ATHMPFEDCALYMNIPNAVVIDSCDFAQTKALTR-KLAACGSPSYMR 77
Cdd:PRK12315  354 FLQRAYDQLSHDLaINNNPAVMIVFGGsisgndVTHLGIFDIPMISNIPNLVYLAPTTKEELIAMLEwALTQHEHPVAIR 433

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668426475  78 LIRKGFTTVYADGSDFEIGKGVTLRDGKDVTIIASGILVDEALKAEEQLAAQ-GISARVIDMHTWKPLDEELVLRAAAET 156
Cdd:PRK12315  434 VPEHGVESGPTVDTDYSTLKYEVTKAGEKVAILALGDFYELGEKVAKKLKEElGIDATLINPKFITGLDEELLEKLKEDH 513

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2668426475 157 GCIVTAENHQVGTGLGSAITNLTSAKNpVPVERIGIQNRFGQVGPQDFLMQQYNLTAE 214
Cdd:PRK12315  514 ELVVTLEDGILDGGFGEKIARYYGNSD-MKVLNYGAKKEFNDRVPVEELYKRNHLTPE 570
PLN02790 PLN02790
transketolase
 30-214 3.34e-06

transketolase


Pssm-ID: 215424 [Multi-domain]  Cd Length: 654  Bit Score: 47.32  E-value: 3.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668426475  30 NGATHMPFEDCALYMNIPNAVVIDSCDFAQTK-----ALTRKlaacGSPSYMRLIRKgfTTVYADGSDFE-IGKG-VTLR 102
Cdd:PLN02790  460 DGPTHQPIEHLASLRAMPNILMLRPADGNETAgaykvAVTNR----KRPTVLALSRQ--KVPNLPGTSIEgVEKGgYVIS 533

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668426475 103 DGK-----DVTIIASGILVDEALKAEEQLAAQGISARVIDMHTWKPLDE------ELVLRAAAETGCIVTAenhqvGTGL 171
Cdd:PLN02790  534 DNSsgnkpDLILIGTGSELEIAAKAAKELRKEGKKVRVVSMVCWELFEEqsdeykESVLPSSVTARVSVEA-----GSTF 608

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2668426475 172 GSAitNLTSAKNPVpverIGIqNRFGQVGPQDFLMQQYNLTAE 214
Cdd:PLN02790  609 GWE--KYVGSKGKV----IGV-DRFGASAPAGILYKEFGFTVE 644
PTZ00089 PTZ00089
transketolase; Provisional
 2-215 2.71e-05

transketolase; Provisional


Pssm-ID: 173383 [Multi-domain]  Cd Length: 661  Bit Score: 44.67  E-value: 2.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668426475   2 FDQAFLA---AGYSELPVHVIGSDPGVCAAFNGATHMPFEDCALYMNIPNAVVIDSCDFAQTK-ALTRKLAACGSPSYMR 77
Cdd:PTZ00089  439 YGYALGAvrlAALSHHPVIYVATHDSIGLGEDGPTHQPVETLALLRATPNLLVIRPADGTETSgAYALALANAKTPTILC 518

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668426475  78 LIRKGftTVYADGSDFE-IGKG----VTLRDGKDVTIIASGILVDEALKAEEQLAAQgISARVIDMHTWKPLDEELVlra 152
Cdd:PTZ00089  519 LSRQN--TPPLPGSSIEgVLKGayivVDFTNSPQLILVASGSEVSLCVEAAKALSKE-LNVRVVSMPCWELFDQQSE--- 592

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2668426475 153 aaetgcivtAENHQVgtglgsaitnLTSAKNPV-PVE-------------RIGIqNRFGQVGPQDFLMQQYNLTAED 215
Cdd:PTZ00089  593 ---------EYQQSV----------LPSGGVPVlSVEayvsfgwekyshvHVGI-SGFGASAPANALYKHFGFTVEN 649
Transket_pyr pfam02779
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ...
 1-80 3.06e-05

Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate dehydrogenases, and branched chain alpha-keto acid decarboxylases.


Pssm-ID: 460692 [Multi-domain]  Cd Length: 174  Bit Score: 42.92  E-value: 3.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668426475   1 MFDQAFLAAGYSELPVHVIGSDPGVCAAFNGATHMPFEDCALYMNIPNAVVIDSCDFAQTKALTRKLAACGS--PSYMRL 78
Cdd:pfam02779  88 ADDAIRHGAALGKLPVPFVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRAAIRRDGrkPVVLRL 167


                  ..
gi 2668426475  79 IR 80
Cdd:pfam02779 168 PR 169
odpB CHL00144
pyruvate dehydrogenase E1 component beta subunit; Validated
 97-175 6.76e-03

pyruvate dehydrogenase E1 component beta subunit; Validated


Pssm-ID: 177066 [Multi-domain]  Cd Length: 327  Bit Score: 37.03  E-value: 6.76e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2668426475  97 KGVTLRDGKDVTIIASGILVDEALKAEEQLAAQGISARVIDMHTWKPLDEELVLRAAAETGCIVTAENHQVGTGLGSAI 175
Cdd:CHL00144  194 KAEVVRPGNDITILTYSRMRHHVLQAVKVLVEKGYDPEIIDLISLKPLDLGTISKSVKKTHKVLIVEECMKTGGIGAEL 272
 
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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