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Reviewed, UniProtKB/Swiss-Prot P49823 (ODPA_CANFA)

Last modified January 20, 2009. Version 44. 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

Names and origin

Protein namesRecommended name:
    Pyruvate dehydrogenase E1 component subunit alpha, somatic form
    EC=1.2.4.1
Alternative name(s):
    PDHE1-A type I
Gene names
Name: PDHA1
OrganismCanis familiaris (Dog)
Taxonomic identifier9615 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis

Protein attributes

Sequence length13 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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.

Enzyme regulation

E1 activity is regulated by phosphorylation (inactivation) and dephosphorylation (activation) of the alpha subunit By similarity.

Subunit structure

Tetramer of 2 alpha and 2 beta subunits.

Subcellular location

Mitochondrion matrix.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentMitochondrion
   LigandPyruvate
Thiamine pyrophosphate
   Molecular functionOxidoreductase
   PTMPhosphoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processglycolysis

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

   Molecular functionpyruvate dehydrogenase (acetyl-transferring) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›13›13Pyruvate dehydrogenase E1 component subunit alpha, somatic form
PRO_0000162214

Experimental info

Non-terminal residue131

Sequences

Sequence LengthMass (Da)Tools
P49823-1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: C97EEBF844085B19

FASTA131,513
        10 
XXDATFEIKK XDL 

« Hide

References

[1]"HSC-2DPAGE and the two-dimensional gel electrophoresis database of dog heart proteins."
Dunn M.J., Corbett J.M., Wheeler C.H.
Electrophoresis 18:2795-2802(1997) [PubMed: 9504812] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Heart.

Cross-references

3D structure databases

ModBaseSearch...

2-D gel databases

HSC-2DPAGEP49823.

Phylogenomic databases

HOVERGENP49823.

Enzyme and pathway databases

BRENDA1.2.4.1. 463.

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameODPA_CANFA
AccessionPrimary (citable) accession number: P49823
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: January 20, 2009
This is version 44 of the entry and version 1 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