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Conserved domains on  [gi|160714832|ref|NP_001104018|]
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uncharacterized protein Dmel_CG17691, isoform C [Drosophila melanogaster]

Protein Classification

alpha-ketoacid dehydrogenase subunit beta( domain architecture ID 11488188)

alpha-ketoacid dehydrogenase subunit beta similar to pyruvate dehydrogenase E1 component subunit beta, 2-oxoisovalerate dehydrogenase subunit beta, and TPP-dependent acetoin dehydrogenase E1 subunit beta

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTZ00182 PTZ00182
3-methyl-2-oxobutanate dehydrogenase; Provisional
 10-362 0e+00

3-methyl-2-oxobutanate dehydrogenase; Provisional


:

Pssm-ID: 185502 [Multi-domain]  Cd Length: 355  Bit Score: 548.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832  10 NSLYNCVRSNLRWPLWTRSHFTYYPTRMGTGKRMNMFNAINNAMDLALDENKSALLFGEDVG-FGGVFRCSVNLRDKYGS 88
Cdd:PTZ00182   2 SSFSSTLLGSRLPNSFSSASRSSSTESKGATVKMNVREAINSALDEELARDPKVFVLGEDVAqYGGVYKCTKGLLDKYGP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832  89 QRVFNTPLCEQGIAGFAIGVANTGATAIAEIQFADYIFPSFDQIVNEAAKYRYRSGGLFDCGsLTFRVPCGAVGHGALYH 168
Cdd:PTZ00182  82 DRVFDTPITEQGFAGFAIGAAMNGLRPIAEFMFADFIFPAFDQIVNEAAKYRYMSGGQFDCP-IVIRGPNGAVGHGGAYH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832 169 SQSPEAYFAHTPGLRVVVPRGPIKAKGLILACIRDPNPCIVFEPKTLYRAAVEEVPAEYYTSQLGKADILRHGKDVTLIG 248
Cdd:PTZ00182 161 SQSFEAYFAHVPGLKVVAPSDPEDAKGLLKAAIRDPNPVVFFEPKLLYRESVEVVPEADYTLPLGKAKVVREGKDVTIVG 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832 249 WGTQVHVLLEVAEIAKsTLNIDCEVIDLVSILPWDAITICTSAKKTGRVIIAHEAPLTQGFGSELASYIQEKCFLHLEAP 328
Cdd:PTZ00182 241 YGSQVHVALKAAEELA-KEGISCEVIDLRSLRPWDRETIVKSVKKTGRCVIVHEAPPTCGIGAEIAAQIMEDCFLYLEAP 319

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 160714832 329 VKRVAGWDTPFPHV--FEPFYMPDKHRCLSAINDIV 362
Cdd:PTZ00182 320 IKRVCGADTPFPYAknLEPAYLPDKEKVVEAAKRVL 355
 
Name Accession Description Interval E-value
PTZ00182 PTZ00182
3-methyl-2-oxobutanate dehydrogenase; Provisional
 10-362 0e+00

3-methyl-2-oxobutanate dehydrogenase; Provisional


Pssm-ID: 185502 [Multi-domain]  Cd Length: 355  Bit Score: 548.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832  10 NSLYNCVRSNLRWPLWTRSHFTYYPTRMGTGKRMNMFNAINNAMDLALDENKSALLFGEDVG-FGGVFRCSVNLRDKYGS 88
Cdd:PTZ00182   2 SSFSSTLLGSRLPNSFSSASRSSSTESKGATVKMNVREAINSALDEELARDPKVFVLGEDVAqYGGVYKCTKGLLDKYGP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832  89 QRVFNTPLCEQGIAGFAIGVANTGATAIAEIQFADYIFPSFDQIVNEAAKYRYRSGGLFDCGsLTFRVPCGAVGHGALYH 168
Cdd:PTZ00182  82 DRVFDTPITEQGFAGFAIGAAMNGLRPIAEFMFADFIFPAFDQIVNEAAKYRYMSGGQFDCP-IVIRGPNGAVGHGGAYH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832 169 SQSPEAYFAHTPGLRVVVPRGPIKAKGLILACIRDPNPCIVFEPKTLYRAAVEEVPAEYYTSQLGKADILRHGKDVTLIG 248
Cdd:PTZ00182 161 SQSFEAYFAHVPGLKVVAPSDPEDAKGLLKAAIRDPNPVVFFEPKLLYRESVEVVPEADYTLPLGKAKVVREGKDVTIVG 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832 249 WGTQVHVLLEVAEIAKsTLNIDCEVIDLVSILPWDAITICTSAKKTGRVIIAHEAPLTQGFGSELASYIQEKCFLHLEAP 328
Cdd:PTZ00182 241 YGSQVHVALKAAEELA-KEGISCEVIDLRSLRPWDRETIVKSVKKTGRCVIVHEAPPTCGIGAEIAAQIMEDCFLYLEAP 319

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 160714832 329 VKRVAGWDTPFPHV--FEPFYMPDKHRCLSAINDIV 362
Cdd:PTZ00182 320 IKRVCGADTPFPYAknLEPAYLPDKEKVVEAAKRVL 355
AcoB COG0022
Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta ...
 41-364 1.03e-165

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: 465.65  E-value: 1.03e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832  41 KRMNMFNAINNAMDLALDENKSALLFGEDVG-FGGVFRCSVNLRDKYGSQRVFNTPLCEQGIAGFAIGVANTGATAIAEI 119
Cdd:COG0022    2 RELTYREAINEALREEMERDPRVFVMGEDVGkYGGVFGVTKGLQEKFGPDRVFDTPISEAGIVGAAIGAALAGLRPVVEI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832 120 QFADYIFPSFDQIVNEAAKYRYRSGGLFDCgSLTFRVPCGAVGHGALYHSQSPEAYFAHTPGLRVVVPRGPIKAKGLILA 199
Cdd:COG0022   82 QFADFIYPAFDQIVNQAAKLRYMSGGQFKV-PMVIRTPYGGGIGAGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832 200 CIRDPNPCIVFEPKTLYRAAvEEVPAEYYTSQLGKADILRHGKDVTLIGWGTQVHVLLEVAEIAKStLNIDCEVIDLVSI 279
Cdd:COG0022  161 AIRDDDPVIFLEHKRLYRLK-GEVPEEDYTVPLGKARVVREGTDVTIVTYGAMVHRALEAAEELAE-EGISAEVIDLRTL 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832 280 LPWDAITICTSAKKTGRVIIAHEAPLTQGFGSELASYIQEKCFLHLEAPVKRVAGWDTPFP--HVFEPFYMPDKHRCLSA 357
Cdd:COG0022  239 SPLDEETILESVKKTGRLVVVDEAPRTGGFGAEIAARIAEEAFDYLDAPVKRVTGPDTPIPyaPALEKAYLPSADRIVAA 318


                 ....*..
gi 160714832 358 INDIVNF 364
Cdd:COG0022  319 VRELLAY 325
TPP_PYR_E1-PDHc-beta_like cd07036
Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate ...
 48-213 1.68e-87

Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate dehydrogenase complex (E1- PDHc) and related proteins; Thiamine pyrophosphate (TPP) family, pyrimidine (PYR) binding domain of the beta subunits of the E1 components of: human pyruvate dehydrogenase complex (E1- PDHc), the acetoin dehydrogenase complex (ADC), and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC), 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. E1-PDHc is an alpha2beta2 dimer-of-heterodimers having two active sites lying between PYR and PP domains of separate subunits, the PYR domains are arranged on the beta subunit, the PP domains on the alpha subunits. PDHc 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. 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: 132919 [Multi-domain]  Cd Length: 167  Bit Score: 261.26  E-value: 1.68e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832  48 AINNAMDLALDENKSALLFGEDVG-FGGVFRCSVNLRDKYGSQRVFNTPLCEQGIAGFAIGVANTGATAIAEIQFADYIF 126
Cdd:cd07036    2 AINEALDEEMERDPRVVVLGEDVGdYGGVFKVTKGLLDKFGPDRVIDTPIAEAGIVGLAVGAAMNGLRPIVEIMFADFAL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832 127 PSFDQIVNEAAKYRYRSGGLFDCGsLTFRVPCGAVGHGALYHSQSPEAYFAHTPGLRVVVPRGPIKAKGLILACIRDPNP 206
Cdd:cd07036   82 PAFDQIVNEAAKLRYMSGGQFKVP-IVIRGPNGGGIGGGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKAAIRDDDP 160


                 ....*..
gi 160714832 207 CIVFEPK 213
Cdd:cd07036  161 VIFLEHK 167
Transketolase_C pfam02780
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ...
 233-353 1.10e-40

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: 139.27  E-value: 1.10e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832  233 GKADILRHGKDVTLIGWGTQVHVLLEVAEIAKSTlNIDCEVIDLVSILPWDAITICTSAKKTGRVIIAHEAPLTQGFGSE 312
Cdd:pfam02780   1 GKAEILREGDDVTIVAYGSMVEEALEAAELLAKE-GISAEVVDLRTIKPLDKETILESVKKTGRLVTVEEAVPRGGFGSE 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 160714832  313 LASYIQEKCFLHLEAPVKRVAGWDTPFP---HVFEPFYMPDKHR 353
Cdd:pfam02780  80 VAAALAEEAFDGLDAPVLRVGGPDFPEPgsaDELEKLYGLTPEK 123
Transket_pyr smart00861
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ...
 92-217 5.84e-35

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: 124.91  E-value: 5.84e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832    92 FNTPLCEQGIAGFAIGVANTGATAIAEIQFADYIFpsfdqivneaAKYRYRSGGLFDCGSLTFRVPCGAVGH--GALYHS 169
Cdd:smart00861  18 IDTGIAEQAMVGFAAGLALHGLRPVVEIFFTFFDR----------AKDQIRSAGASGNVPVVFRHDGGGGVGedGPTHHS 87

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 160714832   170 QSPEAYFAHTPGLRVVVPRGPIKAKGLILACIRDPNP-CIVFEPKTLYR 217
Cdd:smart00861  88 IEDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDGPvVIRLERKSLYR 136
 
Name Accession Description Interval E-value
PTZ00182 PTZ00182
3-methyl-2-oxobutanate dehydrogenase; Provisional
 10-362 0e+00

3-methyl-2-oxobutanate dehydrogenase; Provisional


Pssm-ID: 185502 [Multi-domain]  Cd Length: 355  Bit Score: 548.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832  10 NSLYNCVRSNLRWPLWTRSHFTYYPTRMGTGKRMNMFNAINNAMDLALDENKSALLFGEDVG-FGGVFRCSVNLRDKYGS 88
Cdd:PTZ00182   2 SSFSSTLLGSRLPNSFSSASRSSSTESKGATVKMNVREAINSALDEELARDPKVFVLGEDVAqYGGVYKCTKGLLDKYGP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832  89 QRVFNTPLCEQGIAGFAIGVANTGATAIAEIQFADYIFPSFDQIVNEAAKYRYRSGGLFDCGsLTFRVPCGAVGHGALYH 168
Cdd:PTZ00182  82 DRVFDTPITEQGFAGFAIGAAMNGLRPIAEFMFADFIFPAFDQIVNEAAKYRYMSGGQFDCP-IVIRGPNGAVGHGGAYH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832 169 SQSPEAYFAHTPGLRVVVPRGPIKAKGLILACIRDPNPCIVFEPKTLYRAAVEEVPAEYYTSQLGKADILRHGKDVTLIG 248
Cdd:PTZ00182 161 SQSFEAYFAHVPGLKVVAPSDPEDAKGLLKAAIRDPNPVVFFEPKLLYRESVEVVPEADYTLPLGKAKVVREGKDVTIVG 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832 249 WGTQVHVLLEVAEIAKsTLNIDCEVIDLVSILPWDAITICTSAKKTGRVIIAHEAPLTQGFGSELASYIQEKCFLHLEAP 328
Cdd:PTZ00182 241 YGSQVHVALKAAEELA-KEGISCEVIDLRSLRPWDRETIVKSVKKTGRCVIVHEAPPTCGIGAEIAAQIMEDCFLYLEAP 319

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 160714832 329 VKRVAGWDTPFPHV--FEPFYMPDKHRCLSAINDIV 362
Cdd:PTZ00182 320 IKRVCGADTPFPYAknLEPAYLPDKEKVVEAAKRVL 355
AcoB COG0022
Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta ...
 41-364 1.03e-165

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: 465.65  E-value: 1.03e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832  41 KRMNMFNAINNAMDLALDENKSALLFGEDVG-FGGVFRCSVNLRDKYGSQRVFNTPLCEQGIAGFAIGVANTGATAIAEI 119
Cdd:COG0022    2 RELTYREAINEALREEMERDPRVFVMGEDVGkYGGVFGVTKGLQEKFGPDRVFDTPISEAGIVGAAIGAALAGLRPVVEI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832 120 QFADYIFPSFDQIVNEAAKYRYRSGGLFDCgSLTFRVPCGAVGHGALYHSQSPEAYFAHTPGLRVVVPRGPIKAKGLILA 199
Cdd:COG0022   82 QFADFIYPAFDQIVNQAAKLRYMSGGQFKV-PMVIRTPYGGGIGAGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832 200 CIRDPNPCIVFEPKTLYRAAvEEVPAEYYTSQLGKADILRHGKDVTLIGWGTQVHVLLEVAEIAKStLNIDCEVIDLVSI 279
Cdd:COG0022  161 AIRDDDPVIFLEHKRLYRLK-GEVPEEDYTVPLGKARVVREGTDVTIVTYGAMVHRALEAAEELAE-EGISAEVIDLRTL 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832 280 LPWDAITICTSAKKTGRVIIAHEAPLTQGFGSELASYIQEKCFLHLEAPVKRVAGWDTPFP--HVFEPFYMPDKHRCLSA 357
Cdd:COG0022  239 SPLDEETILESVKKTGRLVVVDEAPRTGGFGAEIAARIAEEAFDYLDAPVKRVTGPDTPIPyaPALEKAYLPSADRIVAA 318


                 ....*..
gi 160714832 358 INDIVNF 364
Cdd:COG0022  319 VRELLAY 325
PRK09212 PRK09212
pyruvate dehydrogenase subunit beta; Validated
 48-358 4.54e-88

pyruvate dehydrogenase subunit beta; Validated


Pssm-ID: 169719 [Multi-domain]  Cd Length: 327  Bit Score: 268.51  E-value: 4.54e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832  48 AINNAMDLALDENKSALLFGEDVG-FGGVFRCSVNLRDKYGSQRVFNTPLCEQGIAGFAIGVANTGATAIAEIQFADYIF 126
Cdd:PRK09212   9 ALRDAMQEEMERDPKVFLMGEEVGeYQGAYKVTQGLLEQFGPKRVIDTPITEHGFAGLAVGAAFAGLRPIVEFMTFNFSM 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832 127 PSFDQIVNEAAKYRYRSGGLFDCgSLTFRVPCGAVGHGALYHSQSPEAYFAHTPGLRVVVPRGPIKAKGLILACIRDPNP 206
Cdd:PRK09212  89 QAIDQIVNSAAKTNYMSGGQLKC-PIVFRGPNGAAARVAAQHSQCYAAWYSHIPGLKVVAPYFAADCKGLLKTAIRDPNP 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832 207 CIVFEPKTLYrAAVEEVPAEYYTSQLGKADILRHGKDVTLIGWGTQVHVLLEVAEIAKSTlNIDCEVIDLVSILPWDAIT 286
Cdd:PRK09212 168 VIFLENEILY-GHSHEVPEEEESIPIGKAAILREGSDVTIVTFSIQVKLALEAAELLEKE-GISVEVIDLRTLRPLDTET 245

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 160714832 287 ICTSAKKTGRVIIAHEAPLTQGFGSELASYIQEKCFLHLEAPVKRVAGWDTPFPHV--FEPFYMPDKHRCLSAI 358
Cdd:PRK09212 246 IIESVKKTNRLVVVEEGWPFAGVGAEIAALIMKEAFDYLDAPVERVTGKDVPLPYAanLEKLALPSEEDIIEAV 319
TPP_PYR_E1-PDHc-beta_like cd07036
Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate ...
 48-213 1.68e-87

Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate dehydrogenase complex (E1- PDHc) and related proteins; Thiamine pyrophosphate (TPP) family, pyrimidine (PYR) binding domain of the beta subunits of the E1 components of: human pyruvate dehydrogenase complex (E1- PDHc), the acetoin dehydrogenase complex (ADC), and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC), 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. E1-PDHc is an alpha2beta2 dimer-of-heterodimers having two active sites lying between PYR and PP domains of separate subunits, the PYR domains are arranged on the beta subunit, the PP domains on the alpha subunits. PDHc 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. 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: 132919 [Multi-domain]  Cd Length: 167  Bit Score: 261.26  E-value: 1.68e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832  48 AINNAMDLALDENKSALLFGEDVG-FGGVFRCSVNLRDKYGSQRVFNTPLCEQGIAGFAIGVANTGATAIAEIQFADYIF 126
Cdd:cd07036    2 AINEALDEEMERDPRVVVLGEDVGdYGGVFKVTKGLLDKFGPDRVIDTPIAEAGIVGLAVGAAMNGLRPIVEIMFADFAL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832 127 PSFDQIVNEAAKYRYRSGGLFDCGsLTFRVPCGAVGHGALYHSQSPEAYFAHTPGLRVVVPRGPIKAKGLILACIRDPNP 206
Cdd:cd07036   82 PAFDQIVNEAAKLRYMSGGQFKVP-IVIRGPNGGGIGGGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKAAIRDDDP 160


                 ....*..
gi 160714832 207 CIVFEPK 213
Cdd:cd07036  161 VIFLEHK 167
PLN02683 PLN02683
pyruvate dehydrogenase E1 component subunit beta
 40-341 1.92e-71

pyruvate dehydrogenase E1 component subunit beta


Pssm-ID: 215368 [Multi-domain]  Cd Length: 356  Bit Score: 226.62  E-value: 1.92e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832  40 GKRMNMFNAINNAMDLALDENKSALLFGEDVG-FGGVFRCSVNLRDKYGSQRVFNTPLCEQGIAGFAIGVANTGATAIAE 118
Cdd:PLN02683  24 AKEMTVRDALNSALDEEMSADPKVFIMGEEVGeYQGAYKITKGLLQKYGPDRVLDTPITEAGFTGIGVGAAYAGLKPVVE 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832 119 IQFADYIFPSFDQIVNEAAKYRYRSGGLFDCgSLTFRVPCGAVGHGALYHSQSPEAYFAHTPGLRVVVPRGPIKAKGLIL 198
Cdd:PLN02683 104 FMTFNFSMQAIDHIINSAAKTNYMSAGQISV-PIVFRGPNGAAAGVGAQHSQCFAAWYSSVPGLKVLAPYSSEDARGLLK 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832 199 ACIRDPNPCIVFEPKTLYRAAV---EEVPAEYYTSQLGKADILRHGKDVTLIGWGTQVHVLLEVAEIAKSTlNIDCEVID 275
Cdd:PLN02683 183 AAIRDPDPVVFLENELLYGESFpvsAEVLDSSFVLPIGKAKIEREGKDVTIVAFSKMVGYALKAAEILAKE-GISAEVIN 261

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160714832 276 LVSILPWDAITICTSAKKTGRVIIAHEAPLTQGFGSELASYIQEKCFLHLEAPVKRVAGWDTPFPH 341
Cdd:PLN02683 262 LRSIRPLDRDTINASVRKTNRLVTVEEGWPQHGVGAEICASVVEESFDYLDAPVERIAGADVPMPY 327
PRK11892 PRK11892
pyruvate dehydrogenase subunit beta; Provisional
 48-340 6.61e-70

pyruvate dehydrogenase subunit beta; Provisional


Pssm-ID: 237011 [Multi-domain]  Cd Length: 464  Bit Score: 225.95  E-value: 6.61e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832  48 AINNAMDLALDENKSALLFGEDVG-FGGVFRCSVNLRDKYGSQRVFNTPLCEQGIAGFAIGVANTGATAIAEIQFADYIF 126
Cdd:PRK11892 147 ALRDAMAEEMRRDEDVFVMGEEVAeYQGAYKVTQGLLQEFGARRVIDTPITEHGFAGIGVGAAFAGLKPIVEFMTFNFAM 226

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832 127 PSFDQIVNEAAKYRYRSGGLFDCgSLTFRVPCGAVGHGALYHSQSPEAYFAHTPGLRVVVPRGPIKAKGLILACIRDPNP 206
Cdd:PRK11892 227 QAIDQIINSAAKTLYMSGGQMGC-PIVFRGPNGAAARVAAQHSQDYAAWYSHIPGLKVVAPYSAADAKGLLKAAIRDPNP 305

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832 207 CIVFEPKTLYRAAVEeVP-AEYYTSQLGKADILRHGKDVTLIGWGTQVHVLLEVA-EIAKstLNIDCEVIDLVSILPWDA 284
Cdd:PRK11892 306 VIFLENEILYGQSFD-VPkLDDFVLPIGKARIHREGKDVTIVSFSIGMTYALKAAeELAK--EGIDAEVIDLRTIRPMDT 382

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 160714832 285 ITICTSAKKTGRVIIAHEAPLTQGFGSELASYIQEKCFLHLEAPVKRVAGWDTPFP 340
Cdd:PRK11892 383 ETIVESVKKTNRLVTVEEGWPQSGVGAEIAARVMEQAFDYLDAPVLRVTGKDVPMP 438
odpB CHL00144
pyruvate dehydrogenase E1 component beta subunit; Validated
 45-341 2.17e-65

pyruvate dehydrogenase E1 component beta subunit; Validated


Pssm-ID: 177066 [Multi-domain]  Cd Length: 327  Bit Score: 210.37  E-value: 2.17e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832  45 MFNAINNAMDLALDENKSALLFGEDVG-FGGVFRCSVNLRDKYGSQRVFNTPLCEQGIAGFAIGVANTGATAIAEIQFAD 123
Cdd:CHL00144   6 LFEALREAIDEEMARDPRVFVIGEDVGhYGGSYKVTKGLHEKYGDLRVLDTPIAENSFTGMAIGAAMTGLRPIVEGMNMG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832 124 YIFPSFDQIVNEAAKYRYRSGGLFDCgSLTFRVPcGAVGH--GAlYHSQSPEAYFAHTPGLRVVVPRGPIKAKGLILACI 201
Cdd:CHL00144  86 FLLLAFNQISNNAGMLHYTSGGNFTI-PIVIRGP-GGVGRqlGA-EHSQRLESYFQSVPGLQIVACSTPYNAKGLLKSAI 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832 202 RDPNPCIVFEPKTLYRAAvEEVPAEYYTSQLGKADILRHGKDVTLIGWGTQVHvllEVAEIAKSTLN--IDCEVIDLVSI 279
Cdd:CHL00144 163 RSNNPVIFFEHVLLYNLK-EEIPDNEYLLPLEKAEVVRPGNDITILTYSRMRH---HVLQAVKVLVEkgYDPEIIDLISL 238

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 160714832 280 LPWDAITICTSAKKTGRVIIAHEAPLTQGFGSELASYIQEKCFLHLEAPVKRVAGWDTPFPH 341
Cdd:CHL00144 239 KPLDLGTISKSVKKTHKVLIVEECMKTGGIGAELIAQINEHLFDELDAPIVRLSSQDVPTPY 300
Transketolase_C pfam02780
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ...
 233-353 1.10e-40

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: 139.27  E-value: 1.10e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832  233 GKADILRHGKDVTLIGWGTQVHVLLEVAEIAKSTlNIDCEVIDLVSILPWDAITICTSAKKTGRVIIAHEAPLTQGFGSE 312
Cdd:pfam02780   1 GKAEILREGDDVTIVAYGSMVEEALEAAELLAKE-GISAEVVDLRTIKPLDKETILESVKKTGRLVTVEEAVPRGGFGSE 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 160714832  313 LASYIQEKCFLHLEAPVKRVAGWDTPFP---HVFEPFYMPDKHR 353
Cdd:pfam02780  80 VAAALAEEAFDGLDAPVLRVGGPDFPEPgsaDELEKLYGLTPEK 123
Transket_pyr pfam02779
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ...
 43-217 2.81e-38

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: 134.99  E-value: 2.81e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832   43 MNMFNAINNAMDLALDENKSALLFGEDVGfGGVFRCSVNLRDKYGSQRVFNTPLCEQGIAGFAIGVANTG-ATAIAEIQF 121
Cdd:pfam02779   3 IATRKASGEALAELAKRDPRVVGGGADLA-GGTFTVTKGLLHPQGAGRVIDTGIAEQAMVGFANGMALHGpLLPPVEATF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832  122 ADYIFPSFDQIVneaakyRYRSGGLFDCGSLTFRVPCGAVGHGALYHSQSPEAYFAHTPGLRVVVPRGPIKAKGLILACI 201
Cdd:pfam02779  82 SDFLNRADDAIR------HGAALGKLPVPFVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRAAI 155

                         170
                  ....*....|....*...
gi 160714832  202 R--DPNPCIVFEPKTLYR 217
Cdd:pfam02779 156 RrdGRKPVVLRLPRQLLR 173
Transket_pyr smart00861
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ...
 92-217 5.84e-35

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: 124.91  E-value: 5.84e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832    92 FNTPLCEQGIAGFAIGVANTGATAIAEIQFADYIFpsfdqivneaAKYRYRSGGLFDCGSLTFRVPCGAVGH--GALYHS 169
Cdd:smart00861  18 IDTGIAEQAMVGFAAGLALHGLRPVVEIFFTFFDR----------AKDQIRSAGASGNVPVVFRHDGGGGVGedGPTHHS 87

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 160714832   170 QSPEAYFAHTPGLRVVVPRGPIKAKGLILACIRDPNP-CIVFEPKTLYR 217
Cdd:smart00861  88 IEDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDGPvVIRLERKSLYR 136
TktA2 COG3958
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
83-363 8.38e-23

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


Pssm-ID: 443158 [Multi-domain]  Cd Length: 308  Bit Score: 97.08  E-value: 8.38e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832  83 RDKYGsQRVFNTPLCEQGIAGFAIGVANTG----ATAIAeiqfadyIFPS---FDQIVNEAAkyrY---------RSGGL 146
Cdd:COG3958   41 AKAFP-DRFFNVGIAEQNMVGVAAGLALAGkipfVSTFA-------PFLTgraYEQIRNDIA---YpnlnvkivgSHAGL 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832 147 fdcgsltfrvpcgAVGHGALYHsQSPE--AYFAHTPGLRVVVPRGPIKAKGLILACIRDPNPCIVFepktLYRAAVEEVP 224
Cdd:COG3958  110 -------------SYGEDGATH-QALEdiALMRALPNMTVIVPADAVETEAAVRAAAEHDGPVYLR----LGRGAVPVVY 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832 225 AEYYTSQLGKADILRHGKDVTLIGWGTQVHVLLEVAEIAKStLNIDCEVIDLVSILPWDAITICTSAKKTGRVIIAHEAP 304
Cdd:COG3958  172 DEDYEFEIGKARVLREGKDVTIIATGIMVAEALEAAELLAK-EGISARVINMHTIKPLDEEAILKAARKTGAVVTAEEHS 250

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 160714832 305 LTQGFGSELASYIQEKCFlhleAPVKRVAGWDTpFPHVFEPFYMPDKHRcLSAiNDIVN 363
Cdd:COG3958  251 IIGGLGSAVAEVLAENYP----VPLRRIGVPDR-FGESGSPEELLEKYG-LDA-EGIVA 302
Dxs COG1154
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ...
 174-333 2.17e-15

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: 77.36  E-value: 2.17e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832 174 AYFAHTPGLRVVVPR----------------GPIkakglilaCIRDPnpcivfepktlyRAAVEEV--PAEYYTSQLGKA 235
Cdd:COG1154  436 SYLRCIPNMVIMAPKdenelrhmlytalaydGPT--------AIRYP------------RGNGPGVelPAELEPLPIGKG 495

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832 236 DILRHGKDVTLIGWGTQVHVLLEVAEIAKStLNIDCEVIDLVSILPWDAITICTSAKKTGRVIIAHEAPLTQGFGSELAS 315
Cdd:COG1154  496 EVLREGKDVAILAFGTMVAEALEAAERLAA-EGISATVVDARFVKPLDEELILELAREHDLVVTVEEGVLAGGFGSAVLE 574

                        170
                 ....*....|....*...
gi 160714832 316 YIQEKcflHLEAPVKRVA 333
Cdd:COG1154  575 FLADA---GLDVPVLRLG 589
PRK05444 PRK05444
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
 174-341 1.07e-12

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


Pssm-ID: 235470 [Multi-domain]  Cd Length: 580  Bit Score: 68.96  E-value: 1.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832 174 AYFAHTPGLRVVVPRGPIKAKG-LILACIRDPNPCIVFEPKTlyrAAVEEVPAEYYTSQLGKADILRHGKDVTLIGWGTQ 252
Cdd:PRK05444 398 SYLRCIPNMVIMAPSDENELRQmLYTALAYDDGPIAIRYPRG---NGVGVELPELEPLPIGKGEVLREGEDVAILAFGTM 474

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832 253 VHVLLEVAEIAKStlnidCEVIDLVSILPWDAITICTSAKKTGRVIIAHEAPLTQGFGSELASYIQEKcflHLEAPVKRV 332
Cdd:PRK05444 475 LAEALKAAERLAS-----ATVVDARFVKPLDEELLLELAAKHDLVVTVEEGAIMGGFGSAVLEFLADH---GLDVPVLNL 546


                 ....*....
gi 160714832 333 AGWDTPFPH 341
Cdd:PRK05444 547 GLPDEFIDH 555
PRK12571 PRK12571
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
 85-317 8.59e-09

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


Pssm-ID: 183601 [Multi-domain]  Cd Length: 641  Bit Score: 57.04  E-value: 8.59e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832  85 KYGSQRVFNTPLCEQGIAGFAIGVANTGATAIAEIqFADYIFPSFDQIVNEAAkyryrsggLFDCGsLTFRVP-CGAVG- 162
Cdd:PRK12571 357 KRFPNRVFDVGIAEQHAVTFAAGLAAAGLKPFCAV-YSTFLQRGYDQLLHDVA--------LQNLP-VRFVLDrAGLVGa 426

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832 163 HGALYHSQSPEAYFAHTPGLRVVVPRGPIK-AKGLILACIRDPNPCIVFEPKTlyRAAVEEVPAEYYTSQLGKADILRHG 241
Cdd:PRK12571 427 DGATHAGAFDLAFLTNLPNMTVMAPRDEAElRHMLRTAAAHDDGPIAVRFPRG--EGVGVEIPAEGTILGIGKGRVPREG 504

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160714832 242 KDVTLIGWGTQVHVLLEVAEIAKSTlNIDCEVIDLVSILPWDAiTICTSAKKTGRVIIAHEAPLTQGFGSELASYI 317
Cdd:PRK12571 505 PDVAILSVGAHLHECLDAADLLEAE-GISVTVADPRFVKPLDE-ALTDLLVRHHIVVIVEEQGAMGGFGAHVLHHL 578
PLN02234 PLN02234
1-deoxy-D-xylulose-5-phosphate synthase
 80-317 2.23e-05

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


Pssm-ID: 177878 [Multi-domain]  Cd Length: 641  Bit Score: 46.24  E-value: 2.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832  80 VNLRDKYGSQRVFNTPLCEQGIAGFAIGVANTGATAIAEIqFADYIFPSFDQIVNEAakyryrsgglfDCGSLTFRVpcg 159
Cdd:PLN02234 390 LNLFESRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCTI-YSSFMQRAYDQVVHDV-----------DLQKLPVRF--- 454

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832 160 AVGHGALYHSQSPE-------AYFAHTPGLRVVVPRGPIKAKGLIL--ACIRDPNPCIVFEPKTLYRAAV----EEVPAe 226
Cdd:PLN02234 455 AIDRAGLMGADGPThcgafdvTFMACLPNMIVMAPSDEAELFNMVAtaAAIDDRPSCFRYHRGNGIGVSLppgnKGVPL- 533

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832 227 yytsQLGKADILRHGKDVTLIGWGTQVHVLLEVAEIAkSTLNIDCEVIDLVSILPWDaITICTSAKKTGRVIIAHEAPLT 306
Cdd:PLN02234 534 ----QIGRGRILRDGERVALLGYGSAVQRCLEAASML-SERGLKITVADARFCKPLD-VALIRSLAKSHEVLITVEEGSI 607

                        250
                 ....*....|.
gi 160714832 307 QGFGSELASYI 317
Cdd:PLN02234 608 GGFGSHVVQFL 618
TPP_PYR_DXS_TK_like cd07033
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ...
 47-209 5.25e-05

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: 42.81  E-value: 5.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832  47 NAINNAMDLALDENKSALLFGEDVGFGGVFRcsvNLRDKYGsQRVFNTPLCEQGIAGFAIGVANTGATAIAEIQ--FADY 124
Cdd:cd07033    1 KAFGEALLELAKKDPRIVALSADLGGSTGLD---KFAKKFP-DRFIDVGIAEQNMVGIAAGLALHGLKPFVSTFsfFLQR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832 125 ifpSFDQIVNEAA------KYRYRSGGLfdcgsltfrvpcgAVGHGALYHsQSPE--AYFAHTPGLRVVVPRGPIKAKGL 196
Cdd:cd07033   77 ---AYDQIRHDVAlqnlpvKFVGTHAGI-------------SVGEDGPTH-QGIEdiALLRAIPNMTVLRPADANETAAA 139

                        170
                 ....*....|...
gi 160714832 197 ILACIRDPNPCIV 209
Cdd:cd07033  140 LEAALEYDGPVYI 152
PLN02225 PLN02225
1-deoxy-D-xylulose-5-phosphate synthase
 90-317 9.70e-05

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


Pssm-ID: 177870 [Multi-domain]  Cd Length: 701  Bit Score: 44.32  E-value: 9.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832  90 RVFNTPLCEQGIAGFAIGVANTGATAIAEIQFAdYIFPSFDQIVNE------AAKYRYRSGGLFDCGSltfRVPCGAVGh 163
Cdd:PLN02225 424 RFFNVGMAEQHAVTFSAGLSSGGLKPFCIIPSA-FLQRAYDQVVHDvdrqrkAVRFVITSAGLVGSDG---PVQCGAFD- 498

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832 164 galyhsqspEAYFAHTPGLRVVVPRGPIKAKGLIL--ACIRDPNPCIVFePKTLYRAAVEEVPAEYyTSQLGKADILRHG 241
Cdd:PLN02225 499 ---------IAFMSSLPNMIAMAPADEDELVNMVAtaAYVTDRPVCFRF-PRGSIVNMNYLVPTGL-PIEIGRGRVLVEG 567

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160714832 242 KDVTLIGWGTQVHVLLEVAEIAkSTLNIDCEVIDLVSILPWDaITICTSAKKTGRVIIAHEAPLTQGFGSELASYI 317
Cdd:PLN02225 568 QDVALLGYGAMVQNCLHAHSLL-SKLGLNVTVADARFCKPLD-IKLVRDLCQNHKFLITVEEGCVGGFGSHVAQFI 641
PLN02582 PLN02582
1-deoxy-D-xylulose-5-phosphate synthase
 80-317 1.83e-04

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


Pssm-ID: 178194 [Multi-domain]  Cd Length: 677  Bit Score: 43.35  E-value: 1.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832  80 VNLRDKYGSQRVFNTPLCEQGIAGFAIGVANTGATAIAEIqFADYIFPSFDQIVNEAakyryrsgglfDCGSLTFRVP-- 157
Cdd:PLN02582 389 LNLFARRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCAI-YSSFLQRGYDQVVHDV-----------DLQKLPVRFAmd 456

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832 158 -CGAVGHGALYHSQSPE-AYFAHTPGLRVVVPRGPIKAKGLIL--ACIRDPNPCIVFePKTlyRAAVEEVPAEYYTS--Q 231
Cdd:PLN02582 457 rAGLVGADGPTHCGAFDvTYMACLPNMVVMAPSDEAELFHMVAtaAAIDDRPSCFRY-PRG--NGIGVQLPPNNKGIpiE 533

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832 232 LGKADILRHGKDVTLIGWGTQVHVLLEVAEIAkSTLNIDCEVIDLVSILPWDAITIcTSAKKTGRVIIAHEAPLTQGFGS 311
Cdd:PLN02582 534 VGKGRILLEGERVALLGYGTAVQSCLAAASLL-ERHGLSATVADARFCKPLDRALI-RSLAKSHEVLITVEEGSIGGFGS 611


                 ....*.
gi 160714832 312 ELASYI 317
Cdd:PLN02582 612 HVAQFM 617
PRK12315 PRK12315
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
 221-316 1.73e-03

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


Pssm-ID: 237053 [Multi-domain]  Cd Length: 581  Bit Score: 40.37  E-value: 1.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160714832 221 EEVPAEYYTSqlgKADILRHGKDVTLIGWGTQVHVLLEVAEIAKSTLNIDCEVIDLVSILPWDAITICTSAKKTGRVIIA 300
Cdd:PRK12315 443 PTVDTDYSTL---KYEVTKAGEKVAILALGDFYELGEKVAKKLKEELGIDATLINPKFITGLDEELLEKLKEDHELVVTL 519

                         90
                 ....*....|....*.
gi 160714832 301 HEAPLTQGFGSELASY 316
Cdd:PRK12315 520 EDGILDGGFGEKIARY 535
 
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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