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Reviewed, UniProtKB/Swiss-Prot P52900 (ODPA_SMIMA)

Last modified November 4, 2008. Version 50. 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, mitochondrial
      Short name=PDHE1-A
    EC=1.2.4.1
Gene names
Name: PDHA
OrganismSminthopsis macroura (Stripe-faced dunnart)
Taxonomic identifier9302 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaMetatheriaDasyuromorphiaDasyuridaeSminthopsis

Protein attributes

Sequence length363 AA.
Sequence statusFragment.
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 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.

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
   DomainTransit peptide
   LigandPyruvate
Thiamine pyrophosphate
   Molecular functionOxidoreductase
   PTMPhosphoprotein

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 peptide‹1 – 2›2Mitochondrion By similarity
Chain3 – 363361Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial
PRO_0000020446

Amino acid modifications

Modified residue2051Phosphoserine By similarity
Modified residue2621Phosphotyrosine By similarity
Modified residue2661Phosphoserine By similarity
Modified residue2681Phosphoserine By similarity
Modified residue2731Phosphoserine By similarity
Modified residue2741Phosphotyrosine By similarity

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
P52900-1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 4884E0A17D7A15A8

FASTA36340,735
        10         20         30         40         50         60 
RNFANDATFD IKKCDVHRLE EGPPTTAVLT REEGLKYYKI MQTVRRMELK ADQLYKQKII 

        70         80         90        100        110        120 
RGFCHLYDGQ EACCMGLEAG INPTDHVITA YRAHGFTYTR GLPVREILAE LTGRRGGCAK 

       130        140        150        160        170        180 
GKGGSMHMYA KNFYGGNGIV GAQVPLGVGI ALACKYNEKD EICLTLYGDG AANQGQIFEA 

       190        200        210        220        230        240 
YNMAALWKLP CIFICENNRY GMGTSVERAA ASTDYYKRGD FIPGIMVDGM DVLCVREATK 

       250        260        270        280        290        300 
FAAAYCRSGK GPMLMELQTY RYHGHSMSDP GVSYRTREEI QEVRSKSDPI MLLKDRMVNN 

       310        320        330        340        350        360 
NLASIEELKE IDVEVRKEIE DAAQFATADP EPPLEELGYH IYSRDPPFEV RGANQWIKYK 


SVS 

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References

[1]"A eutherian X-linked gene, PDHA1, is autosomal in marsupials: a model for the evolution of a second, testis-specific variant in eutherian mammals."
Fitzgerald J., Wilcox S.A., Graves J.A., Dahl H.H.M.
Genomics 18:636-642(1993) [PubMed: 8307573] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Testis.

Cross-references

Sequence databases

L20774 mRNA. Translation: AAA31589.1.

3D structure databases

HSSPHSSP built from PDB template 1NI4 based on UniProtKB P08559.
SMRP52900. Positions 2-363.
ModBaseSearch...

Phylogenomic databases

HOVERGENP52900.

Family and domain databases

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

Entry information

Entry nameODPA_SMIMA
AccessionPrimary (citable) accession number: P52900
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 4, 2008
This is version 50 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