Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P52899 (ODPA_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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 [Reference proteome]
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

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 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 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 matrix By similarity.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandPyruvate
Thiamine pyrophosphate
   Molecular functionOxidoreductase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from direct assay PubMed 20188671. Source: WormBase

   Molecular_functionpyruvate dehydrogenase (acetyl-transferring) activity

Inferred from electronic annotation. Source: UniProtKB-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 [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 

« Hide

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bristol N2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z47812 Genomic DNA. Translation: CAA87793.1.
PIRT24557.
RefSeqNP_495693.1. NM_063292.4.
UniGeneCel.38645.

3D structure databases

ProteinModelPortalP52899.
SMRP52899. Positions 25-374.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-24909N.
STRING6239.T05H10.6b.

Proteomic databases

PaxDbP52899.
PRIDEP52899.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaT05H10.6a.1; T05H10.6a.1; T05H10.6.
T05H10.6a.2; T05H10.6a.2; T05H10.6.
T05H10.6a.3; T05H10.6a.3; T05H10.6.
GeneID3565996.
KEGGcel:CELE_T05H10.6.
UCSCT05H10.6b. c. elegans.

Organism-specific databases

CTD3565996.
WormBaseT05H10.6a; CE01643; WBGene00011510.

Phylogenomic databases

eggNOGCOG1071.
HOGENOMHOG000281336.
KOK00161.

Family and domain databases

InterProIPR001017. DH_E1.
IPR017597. Pyrv_DH_E1_asu_subgrp-y.
[Graphical view]
PfamPF00676. E1_dh. 1 hit.
[Graphical view]
TIGRFAMsTIGR03182. PDH_E1_alph_y. 1 hit.
ProtoNetSearch...

Other

NextBio958671.
PROP52899.

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: April 16, 2014
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Relevant documents

Caenorhabditis elegans

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