Skip Header

Contribute Send feedback
Read comments (?) or add your own

P52902 (ODPA_PEA) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 65. Feed History...

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

Names and origin

Protein namesRecommended name:
Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial
Short name=PDHE1-A
EC=1.2.4.1
OrganismPisum sativum (Garden pea)
Taxonomic identifier3888 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Fabales › Fabaceae › Papilionoideae › Fabeae › Pisum

Protein attributes

Sequence length397 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 By similarity.

Subcellular location

Mitochondrion matrix.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandPyruvate
Thiamine pyrophosphate
   Molecular functionOxidoreductase
   PTMPhosphoprotein
Gene Ontology (GO)
   Biological processglycolysis

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? – 397Pyruvate dehydrogenase E1 component subunit alpha, mitochondrialPRO_0000020454

Sequences

Sequence LengthMass (Da)Tools
P52902 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 3C0257CB0032E50B

FASTA39743,530
        10         20         30         40         50         60 
MALSRLSSSS SSSNGSNLFN PFSAAFTLNR PISSDTTATL TIETSLPFTA HNCDPPSRSV 

        70         80         90        100        110        120 
TTSPSELLSF FRTMALMRRM EIAADSLYKA NLIRGFCHLY DGQEAVAVGM EAGTTKKDCI 

       130        140        150        160        170        180 
ITAYRDHCTF LGRGGTLLRV YAELMGRRDG CSKGKGGSMH FYKKDSGFYG GHGIVGAQVP 

       190        200        210        220        230        240 
LGCGLAFGQK YLKDESVTFA LYGDGAANQG QLFEALNISA LWDLPAILVC ENNHYGMGTA 

       250        260        270        280        290        300 
TWRSAKSPAY FKRGDYVPGL KVDGMDALAV KQACKFAKEH ALKNGPIILE MDTYRYHGHS 

       310        320        330        340        350        360 
MSDPGSTYRT RDEISGVRQE RDPIERVRKL LLSHDIATEK ELKDTEKEVR KEVDEAIAKA 

       370        380        390 
KDSPMPDPSD LFSNVYVKGY GVEAFGVDRK EVRVTLP

« Hide

References

[1]Luethy M.H., Miernyk J.A., Randall D.D.
Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U51918 mRNA. Translation: AAA97411.1.
PIRT06531.

3D structure databases

ProteinModelPortalP52902.
ModBaseSearch...

Protein-protein interaction databases

IntActP52902. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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...

Entry information

Entry nameODPA_PEA
AccessionPrimary (citable) accession number: P52902
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: September 21, 2011
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info