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A5A6L0 (ODPA_PANTR) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 50. 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, somatic form, mitochondrial

EC=1.2.4.1
Alternative name(s):
PDHE1-A type I
Gene names
Name:PDHA1
OrganismPan troglodytes (Chimpanzee) [Reference proteome]
Taxonomic identifier9598 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePan

Protein attributes

Sequence length390 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, 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-232, Ser-293 and Ser-300 by PDK family kinases inactivates the enzyme; for this phosphorylation at a single site is sufficient. Phosphorylation at Ser-293 interferes with access to active site, and thereby inactivates the enzyme. Dephosphorylation at all three sites, i.e. at Ser-232, Ser-293 and Ser-300, 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 peptide1 – 2929Mitochondrion By similarity
Chain30 – 390361Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial
PRO_0000297491

Amino acid modifications

Modified residue631N6-acetyllysine; alternate By similarity
Modified residue631N6-succinyllysine; alternate By similarity
Modified residue2321Phosphoserine; by PDK1 By similarity
Modified residue2441N6-acetyllysine; alternate By similarity
Modified residue2441N6-succinyllysine; alternate By similarity
Modified residue2771N6-succinyllysine By similarity
Modified residue2931Phosphoserine; by PDK1, PDK2, PDK3 and PDK4 By similarity
Modified residue2951Phosphoserine By similarity
Modified residue3001Phosphoserine; by PDK1, PDK2, PDK3 and PDK4 By similarity
Modified residue3011Phosphotyrosine By similarity
Modified residue3131N6-acetyllysine; alternate By similarity
Modified residue3131N6-succinyllysine; alternate By similarity
Modified residue3211N6-acetyllysine By similarity
Modified residue3361N6-acetyllysine By similarity
Modified residue3851N6-succinyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A5A6L0 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: 4F95746CBB792E78

FASTA39043,238
        10         20         30         40         50         60 
MRKMLAAVSR VLSGASQKPA SRVLVASRNF ANDATFEIKK CDLHRLEEGP PVTTVLTRED 

        70         80         90        100        110        120 
GLKYYRMMQT VRRMELKADQ LYKQKIIRGF CHLCDGQEAC CVGLEAGINP TDHLITAYRA 

       130        140        150        160        170        180 
HGFTFTRGLS VREILAELTG RKGGCAKGKG GSMHMYAKNF YGGNGIVGAQ VPLGAGIALA 

       190        200        210        220        230        240 
CKYNGKDEVC LTLYGDGAAN QGQIFEAYNM AALWKLPCIF ICENNRYGMG TSVERAAAST 

       250        260        270        280        290        300 
DYYKRGDFIP GLRVDGMDIL CVREATRFAA AYCRSGKGPI LMELQTYRYH GHSMSGPGVS 

       310        320        330        340        350        360 
YRTREEIQEV RSKSDPIMLL KDRMVNSNLA SVEELKEIDV EVRKEIEDAA QFATADPEPP 

       370        380        390 
LEELGYHIYS SDPPFEVRGA NQWIKFKSVS 

« Hide

References

[1]"Mapping of chimpanzee full-length cDNAs onto the human genome unveils large potential divergence of the transcriptome."
Sakate R., Suto Y., Imanishi T., Tanoue T., Hida M., Hayasaka I., Kusuda J., Gojobori T., Hashimoto K., Hirai M.
Gene 399:1-10(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB222138 mRNA. Translation: BAF62383.1.
RefSeqNP_001104283.1. NM_001110813.1.
UniGenePtr.3278.

3D structure databases

ProteinModelPortalA5A6L0.
SMRA5A6L0. Positions 29-390.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEA5A6L0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID465525.
KEGGptr:465525.

Organism-specific databases

CTD5160.

Phylogenomic databases

eggNOGCOG1071.
HOGENOMHOG000281336.
HOVERGENHBG001863.
InParanoidA5A6L0.
KOK00161.

Family and domain databases

Gene3D3.40.50.970. 1 hit.
InterProIPR001017. DH_E1.
IPR017597. Pyrv_DH_E1_asu_subgrp-y.
IPR029061. THDP-binding.
[Graphical view]
PfamPF00676. E1_dh. 1 hit.
[Graphical view]
SUPFAMSSF52518. SSF52518. 1 hit.
TIGRFAMsTIGR03182. PDH_E1_alph_y. 1 hit.
ProtoNetSearch...

Other

NextBio20843882.

Entry information

Entry nameODPA_PANTR
AccessionPrimary (citable) accession number: A5A6L0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 24, 2007
Last sequence update: June 12, 2007
Last modified: June 11, 2014
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program