NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|320546221|ref|NP_001104016|]
View 

uncharacterized protein Dmel_CG17691, isoform F [Drosophila melanogaster]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PTZ00182 super family cl33170
3-methyl-2-oxobutanate dehydrogenase; Provisional
 10-106 2.95e-35

3-methyl-2-oxobutanate dehydrogenase; Provisional


The actual alignment was detected with superfamily member PTZ00182:

Pssm-ID: 185502 [Multi-domain]  Cd Length: 355  Bit Score: 123.17  E-value: 2.95e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546221  10 NSLYNCVRSNLRWPLWTRSHFTYYPTRMGTGKRMNMFNAINNAMDLALDENKSALLFGEDVG-FGGVFRCSVNLRDKYGS 88
Cdd:PTZ00182   2 SSFSSTLLGSRLPNSFSSASRSSSTESKGATVKMNVREAINSALDEELARDPKVFVLGEDVAqYGGVYKCTKGLLDKYGP 81

                         90
                 ....*....|....*...
gi 320546221  89 QRVFNTPLCEQGIAGYVI 106
Cdd:PTZ00182  82 DRVFDTPITEQGFAGFAI 99
 
Name Accession Description Interval E-value
PTZ00182 PTZ00182
3-methyl-2-oxobutanate dehydrogenase; Provisional
 10-106 2.95e-35

3-methyl-2-oxobutanate dehydrogenase; Provisional


Pssm-ID: 185502 [Multi-domain]  Cd Length: 355  Bit Score: 123.17  E-value: 2.95e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546221  10 NSLYNCVRSNLRWPLWTRSHFTYYPTRMGTGKRMNMFNAINNAMDLALDENKSALLFGEDVG-FGGVFRCSVNLRDKYGS 88
Cdd:PTZ00182   2 SSFSSTLLGSRLPNSFSSASRSSSTESKGATVKMNVREAINSALDEELARDPKVFVLGEDVAqYGGVYKCTKGLLDKYGP 81

                         90
                 ....*....|....*...
gi 320546221  89 QRVFNTPLCEQGIAGYVI 106
Cdd:PTZ00182  82 DRVFDTPITEQGFAGFAI 99
AcoB COG0022
Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta ...
 41-103 2.09e-24

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: 93.93  E-value: 2.09e-24
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 320546221  41 KRMNMFNAINNAMDLALDENKSALLFGEDVG-FGGVFRCSVNLRDKYGSQRVFNTPLCEQGIAG 103
Cdd:COG0022    2 RELTYREAINEALREEMERDPRVFVMGEDVGkYGGVFGVTKGLQEKFGPDRVFDTPISEAGIVG 65
TPP_PYR_E1-PDHc-beta_like cd07036
Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate ...
 48-106 5.48e-24

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: 89.46  E-value: 5.48e-24
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546221  48 AINNAMDLALDENKSALLFGEDVG-FGGVFRCSVNLRDKYGSQRVFNTPLCEQGIAGYVI 106
Cdd:cd07036    2 AINEALDEEMERDPRVVVLGEDVGdYGGVFKVTKGLLDKFGPDRVIDTPIAEAGIVGLAV 61
Transket_pyr pfam02779
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ...
 43-103 2.50e-10

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: 54.09  E-value: 2.50e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 320546221   43 MNMFNAINNAMDLALDENKSALLFGEDVGfGGVFRCSVNLRDKYGSQRVFNTPLCEQGIAG 103
Cdd:pfam02779   3 IATRKASGEALAELAKRDPRVVGGGADLA-GGTFTVTKGLLHPQGAGRVIDTGIAEQAMVG 62
 
Name Accession Description Interval E-value
PTZ00182 PTZ00182
3-methyl-2-oxobutanate dehydrogenase; Provisional
 10-106 2.95e-35

3-methyl-2-oxobutanate dehydrogenase; Provisional


Pssm-ID: 185502 [Multi-domain]  Cd Length: 355  Bit Score: 123.17  E-value: 2.95e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546221  10 NSLYNCVRSNLRWPLWTRSHFTYYPTRMGTGKRMNMFNAINNAMDLALDENKSALLFGEDVG-FGGVFRCSVNLRDKYGS 88
Cdd:PTZ00182   2 SSFSSTLLGSRLPNSFSSASRSSSTESKGATVKMNVREAINSALDEELARDPKVFVLGEDVAqYGGVYKCTKGLLDKYGP 81

                         90
                 ....*....|....*...
gi 320546221  89 QRVFNTPLCEQGIAGYVI 106
Cdd:PTZ00182  82 DRVFDTPITEQGFAGFAI 99
AcoB COG0022
Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta ...
 41-103 2.09e-24

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: 93.93  E-value: 2.09e-24
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 320546221  41 KRMNMFNAINNAMDLALDENKSALLFGEDVG-FGGVFRCSVNLRDKYGSQRVFNTPLCEQGIAG 103
Cdd:COG0022    2 RELTYREAINEALREEMERDPRVFVMGEDVGkYGGVFGVTKGLQEKFGPDRVFDTPISEAGIVG 65
TPP_PYR_E1-PDHc-beta_like cd07036
Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate ...
 48-106 5.48e-24

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: 89.46  E-value: 5.48e-24
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 320546221  48 AINNAMDLALDENKSALLFGEDVG-FGGVFRCSVNLRDKYGSQRVFNTPLCEQGIAGYVI 106
Cdd:cd07036    2 AINEALDEEMERDPRVVVLGEDVGdYGGVFKVTKGLLDKFGPDRVIDTPIAEAGIVGLAV 61
Transket_pyr pfam02779
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ...
 43-103 2.50e-10

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: 54.09  E-value: 2.50e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 320546221   43 MNMFNAINNAMDLALDENKSALLFGEDVGfGGVFRCSVNLRDKYGSQRVFNTPLCEQGIAG 103
Cdd:pfam02779   3 IATRKASGEALAELAKRDPRVVGGGADLA-GGTFTVTKGLLHPQGAGRVIDTGIAEQAMVG 62
odpB CHL00144
pyruvate dehydrogenase E1 component beta subunit; Validated
 45-106 5.10e-10

pyruvate dehydrogenase E1 component beta subunit; Validated


Pssm-ID: 177066 [Multi-domain]  Cd Length: 327  Bit Score: 54.75  E-value: 5.10e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 320546221  45 MFNAINNAMDLALDENKSALLFGEDVG-FGGVFRCSVNLRDKYGSQRVFNTPLCEQGIAGYVI 106
Cdd:CHL00144   6 LFEALREAIDEEMARDPRVFVIGEDVGhYGGSYKVTKGLHEKYGDLRVLDTPIAENSFTGMAI 68
PLN02683 PLN02683
pyruvate dehydrogenase E1 component subunit beta
 40-103 3.42e-09

pyruvate dehydrogenase E1 component subunit beta


Pssm-ID: 215368 [Multi-domain]  Cd Length: 356  Bit Score: 52.13  E-value: 3.42e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 320546221  40 GKRMNMFNAINNAMDLALDENKSALLFGEDVG-FGGVFRCSVNLRDKYGSQRVFNTPLCEQGIAG 103
Cdd:PLN02683  24 AKEMTVRDALNSALDEEMSADPKVFIMGEEVGeYQGAYKITKGLLQKYGPDRVLDTPITEAGFTG 88
PRK09212 PRK09212
pyruvate dehydrogenase subunit beta; Validated
 48-103 4.74e-08

pyruvate dehydrogenase subunit beta; Validated


Pssm-ID: 169719 [Multi-domain]  Cd Length: 327  Bit Score: 48.95  E-value: 4.74e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 320546221  48 AINNAMDLALDENKSALLFGEDVG-FGGVFRCSVNLRDKYGSQRVFNTPLCEQGIAG 103
Cdd:PRK09212   9 ALRDAMQEEMERDPKVFLMGEEVGeYQGAYKVTQGLLEQFGPKRVIDTPITEHGFAG 65
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH