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Reviewed, UniProtKB/Swiss-Prot P52899 (ODPA_CAEEL)

Last modified November 4, 2008. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 · Relevant documents

Names and origin

Protein namesRecommended name:
    Probable pyruvate dehydrogenase E1 component subunit alpha, mitochondrial
      Short name=PDHE1-A
    EC=1.2.4.1
Gene names
ORF Names: T05H10.6
OrganismCaenorhabditis elegans [Complete proteome]
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryotaMetazoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length397 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology.

General annotation (Comments)

Function

The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). 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 + CO(2).

Cofactor

Thiamine pyrophosphate By similarity.

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 By similarity.

Subcellular location

Mitochondrion matrixBy similarity.

Ontologies

Keywords

   Biological processGlycolysis
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandPyruvate
Thiamine pyrophosphate
   Molecular functionOxidoreductase
   PTMPhosphoprotein
   Technical termComplete proteome

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

Transit peptide1 – ?Mitochondrion Potential
Chain? – 397Probable pyruvate dehydrogenase E1 component subunit alpha, mitochondrialPRO_0000020439

Sequences

Sequence LengthMass (Da)Tools
P52899-1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 27FB6410B0EA8513

FASTA39743,792
        10         20         30         40         50         60 
MSLFARQLQS LTASGIRTQQ VRLASTEVSF HTKPCKLHKL DNGPNTSVTL NREDALKYYR 

        70         80         90        100        110        120 
DMQVIRRMES AAGNLYKEKK IRGFCHLYSG QEACAVGMKA AMTEGDAVIT AYRCHGWTWL 

       130        140        150        160        170        180 
LGATVTEVLA ELTGRVAGNV HGKGGSMHMY TKNFYGGNGI VGAQQPLGAG VALAMKYREQ 

       190        200        210        220        230        240 
KNVCVTLYGD GAANQGQLFE ATNMAKLWDL PVLFVCENNG FGMGTTAERS SASTEYYTRG 

       250        260        270        280        290        300 
DYVPGIWVDG MDILAVREAT KWAKEYCDSG KGPLMMEMAT YRYHGHSMSD PGTSYRTREE 

       310        320        330        340        350        360 
IQEVRKTRDP ITGFKDRIIT SSLATEEELK AIDKEVRKEV DEALKIATSD GVLPPEALYA 

       370        380        390 
DIYHNTPAQE IRGATIDETI VQPFKTSADV LKSIGRA 

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References

[1]"Genome sequence of the nematode C. elegans: a platform for investigating biology."
The C. elegans sequencing consortium
Science 282:2012-2018(1998) [PubMed: 9851916] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bristol N2.

Cross-references

Sequence databases

Z47812 Genomic DNA. Translation: CAA87793.1.
PIRT24557.
RefSeqNP_495693.1.
UniGeneCel.7502

3D structure databases

HSSPHSSP built from PDB template 1NI4 based on UniProtKB P08559.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:24909N.

Genome annotation databases

EnsemblT05H10.6. Caenorhabditis elegans. [Contig view]
GeneID3565996.
KEGGcel:T05H10.6.

Organism-specific databases

WormBaseWBGene00011510. T05H10.6.
WormPepT05H10.6. CE01643. [WorfDB]

Family and domain databases

InterProIPR001017. DHase_E1.
IPR017597. Pyrv_DH_E1_asu_subgrp-y.
[Graphical view]
PfamPF00676. E1_dh. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio958671.

Entry information

Entry nameODPA_CAEEL
AccessionPrimary (citable) accession number: P52899
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 4, 2008
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectCaenorhabditis annotation project

Relevant documents

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormPep

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents