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P52900 (ODPA_SMIMA) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 73. 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

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 CO2, and thereby links the glycolytic pathway to the tricarboxylic cycle By similarity.

Catalytic activity

Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2.

Cofactor

Thiamine pyrophosphate By similarity.

Enzyme regulation

Pyruvate dehydrogenase activity is inhibited by phosphorylation of PDHA1; it is reactivated by dephosphorylation By similarity.

Subunit structure

Heterotetramer of two PDHA1 and two PDHB subunits. The heterotetramer interacts with DLAT, and is part of the multimeric pyruvate dehydrogenase complex that contains multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (DLAT, E2) and lipoamide dehydrogenase (DLD, E3). These subunits are bound to an inner core composed of about 48 DLAT and 12 PDHX molecules By similarity.

Subcellular location

Mitochondrion matrix By similarity.

Post-translational modification

Phosphorylation at Ser-205, Ser-266 and Ser-273 by PDK family kinases inactivates the enzyme; for this phosphorylation at a single site is sufficient. Phosphorylation at Ser-266 interferes with access to active site, and thereby inactivates the enzyme. Dephosphorylation at all three sites, i.e. at Ser-205, Ser-266 and Ser-273, is required for reactivation By similarity.

Acetylation alters the phosphorylation pattern. Deacetylated by SIRT3 By similarity.

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 residue361N6-acetyllysine; alternate By similarity
Modified residue361N6-succinyllysine; alternate By similarity
Modified residue2051Phosphoserine; by PDK1 By similarity
Modified residue2171N6-acetyllysine; alternate By similarity
Modified residue2171N6-succinyllysine; alternate By similarity
Modified residue2401N6-acetyllysine By similarity
Modified residue2501N6-succinyllysine By similarity
Modified residue2661Phosphoserine; by PDK1, PDK2, PDK3 and PDK4 By similarity
Modified residue2681Phosphoserine By similarity
Modified residue2731Phosphoserine; by PDK1, PDK2, PDK3 and PDK4 By similarity
Modified residue2741Phosphotyrosine By similarity
Modified residue2861N6-acetyllysine; alternate By similarity
Modified residue2861N6-succinyllysine; alternate By similarity
Modified residue2941N6-acetyllysine By similarity
Modified residue3091N6-acetyllysine By similarity
Modified residue3581N6-succinyllysine By similarity

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
P52900 [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 

« Hide

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Testis.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L20774 mRNA. Translation: AAA31589.1.

3D structure databases

ProteinModelPortalP52900.
SMRP52900. Positions 2-363.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP52900.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG001863.

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_SMIMA
AccessionPrimary (citable) accession number: P52900
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: March 19, 2014
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program