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Reviewed, UniProtKB/Swiss-Prot P49432 (ODPB_RAT)

Last modified January 19, 2010. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information

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Names and origin

Protein namesRecommended name:
    Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
      Short name=PDHE1-B
    EC=1.2.4.1
Gene names
Name: Pdhb
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

Sequence length359 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).

Catalytic activity

Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2.

Cofactor

Thiamine pyrophosphate.

Subunit structure

Tetramer of 2 alpha and 2 beta subunits.

Subcellular location

Mitochondrion matrix.

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Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandPyruvate
Thiamine pyrophosphate
   Molecular functionOxidoreductase
   PTMPhosphoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processacetyl-CoA biosynthetic process from pyruvate

Inferred from direct assay. Source: RGD

glycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

pyruvate dehydrogenase complex

Inferred from direct assay. Source: RGD

   Molecular functionpyruvate dehydrogenase (acetyl-transferring) activity

Inferred from direct assay. Source: RGD

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3030Mitochondrion Ref.3
Chain31 – 359329Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
PRO_0000020459

Sites

Binding site891Thiamine pyrophosphate By similarity

Amino acid modifications

Modified residue671Phosphotyrosine By similarity

Experimental info

Sequence conflict31A → G Ref.1
Sequence conflict11 – 155PLRQA → LCGRL Ref.1
Sequence conflict221R → L Ref.1
Sequence conflict251R → C Ref.1
Sequence conflict2381T → N Ref.1
Sequence conflict241 – 2422AH → CY Ref.1
Sequence conflict2591E → G Ref.1

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Sequences

Sequence LengthMass (Da)Tools
P49432-1 [UniParc].

Last modified January 9, 2007. Version 2.
Checksum: 1B942D0A68C86D51

FASTA35938,982
        10         20         30         40         50         60 
MAAVAGLVRG PLRQASGLLK RRFHRSAPAA VQLTVREAIN QGMDEELERD EKVFLLGEEV 

        70         80         90        100        110        120 
AQYDGAYKVS RGLWKKYGDK RIIDTPISEM GFAGIAVGAA MAGLRPICEF MTFNFSMQAI 

       130        140        150        160        170        180 
DQVINSAAKT YYMSAGLQPV PIVFRGPNGA SAGVAAQHSQ CFAAWYGHCP GLKVVSPWNS 

       190        200        210        220        230        240 
EDAKGLIKSA IRDDNPVVML ENELMYGVAF ELPTEAQSKD FLIPIGKAKI ERQGTHITVV 

       250        260        270        280        290        300 
AHSRPVGHCL EAAAVLSKEG IECEVINLRT IRPMDIEAIE ASVMKTNHLV TVEGGWPQFG 

       310        320        330        340        350 
VGAEICARIM EGPAFNFLDA PAVRVTGADV PMPYAKILED NSIPQVKDII FAIKKTLNI

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References

« Hide 'large scale' references
[1]"The alpha-ketoacid dehydrogenase complexes. Sequence similarity of rat pyruvate dehydrogenase with Escherichia coli and Azotobacter vinelandii alpha-ketoglutarate dehydrogenase."
Matuda S., Nakano K., Ohta S., Saheki T., Kawanishi Y., Miyata T.
Biochim. Biophys. Acta 1089:1-7(1991) [PubMed: 2025639] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
[3]Dunn M.J.
Submitted (MAR-1996) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 31-38.
Tissue: Heart.
[4]Lubec G., Afjehi-Sadat L., Diao W.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 286-324, MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Hippocampus and Spinal cord.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BC079137 mRNA. Translation: AAH79137.1.
IPIIPI00194324.
PIRS15892.
RefSeqNP_001007621.1.
UniGeneRn.102424

3D structure databases

SMRP49432. Positions 30-359.
ModBaseSearch...

Protein-protein interaction databases

STRINGP49432.

PTM databases

PhosphoSiteP49432.

2-D gel databases

HSC-2DPAGEP49432.

Proteomic databases

PRIDEP49432.

Genome annotation databases

EnsemblENSRNOT00000010545; ENSRNOP00000010545; ENSRNOG00000007895; Rattus norvegicus. [Genome view]
GeneID289950.
KEGGrno:289950.
NMPDRfig|10116.3.peg.11094.
UCSCNM_001007620. rat.

Organism-specific databases

CTD289950.
RGD1359146. Pdhb.

Phylogenomic databases

eggNOGroNOG10273.
HOVERGENP49432.
InParanoidP49432.
OMAAIEASVM.
OrthoDBEOG99GP20.
PhylomeDBP49432.

Enzyme and pathway databases

BRENDA1.2.4.1. 248.

Gene expression databases

ArrayExpressP49432.
GenevestigatorP49432.
GermOnlineENSRNOG00000007895. Rattus norvegicus.

Family and domain databases

InterProIPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR015941. Transketolase-like_C.
IPR005475. Transketolase-like_Pyr-bd.
IPR005476. Transketolase_C.
[Graphical view]
Gene3DG3DSA:3.40.50.920. Transketo_C_like. 1 hit.
PfamPF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view]
SMARTSM00861. Transket_pyr. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio630523.

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Entry information

Entry nameODPB_RAT
AccessionPrimary (citable) accession number: P49432
Secondary accession number(s): Q6AY95
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 9, 2007
Last modified: January 19, 2010
This is version 82 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information