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P29804 (ODPA_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 80. 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
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length389 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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. Ref.2

Catalytic activity

Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2. Ref.2

Cofactor

Thiamine pyrophosphate. Ref.2

Enzyme regulation

Pyruvate dehydrogenase activity is inhibited by phosphorylation of PDHA1; it is reactivated by dephosphorylation. Ref.2

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 Ref.2.

Post-translational modification

Phosphorylation at Ser-231, Ser-292 and Ser-299 by PDK family kinases inactivates the enzyme; for this phosphorylation at a single site is sufficient. Phosphorylation at Ser-292 interferes with access to active site, and thereby inactivates the enzyme. Dephosphorylation at all three sites, i.e. at Ser-231, Ser-292 and Ser-299, is required for reactivation.

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide‹1 – 28›28Mitochondrion By similarity
Chain29 – 389361Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial
PRO_0000020443

Amino acid modifications

Modified residue621N6-acetyllysine; alternate By similarity
Modified residue621N6-succinyllysine; alternate By similarity
Modified residue2311Phosphoserine; by PDK1 By similarity
Modified residue2431N6-acetyllysine; alternate By similarity
Modified residue2431N6-succinyllysine; alternate By similarity
Modified residue2761N6-succinyllysine By similarity
Modified residue2921Phosphoserine; by PDK1, PDK2, PDK3 and PDK4 By similarity
Modified residue2941Phosphoserine By similarity
Modified residue2991Phosphoserine; by PDK1, PDK2, PDK3 and PDK4 By similarity
Modified residue3001Phosphotyrosine By similarity
Modified residue3121N6-acetyllysine; alternate By similarity
Modified residue3121N6-succinyllysine; alternate By similarity
Modified residue3201N6-acetyllysine By similarity
Modified residue3351N6-acetyllysine By similarity
Modified residue3841N6-succinyllysine By similarity

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
P29804 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: E9C7DF85389A9A47

FASTA38943,121
        10         20         30         40         50         60 
GKMLAAVSRV LSGVAQKPAS RVLVASRTFA NDATFEIKKC DLHRLEEGPP VTTVLTREDG 

        70         80         90        100        110        120 
LKYYRMMQTV RRMELKADQL YKQKIIRGFC HLCDGQEACC VGLEAGINPT DHLITAYRAH 

       130        140        150        160        170        180 
GFTFTRGLSV REILAELTGR RGGCGKGKGG SMHMYAKNFY GGNGIVGAQV PLGAGIALAC 

       190        200        210        220        230        240 
KYNGKDEVCL TLYGDGAANQ GQIFEAYNMA ALWKLPCVFI CENNRYGMGT SVERAAASTD 

       250        260        270        280        290        300 
YYKRGDFIPG LRVDGMDILC VREATRFAAA YCRSGKGPIL MELQTYRYHG HSMSDPGVSY 

       310        320        330        340        350        360 
RTREEIQEVR SKSDPIMLLK DRMVNSNLAS VEELKEIDVE VRKEIEDAAQ FATADPEPPL 

       370        380 
EELGYHIYCN DPPFEVRGAN QWIKFKSIS 

« Hide

References

[1]"Characterisation of a cDNA for porcine PDH-E1 alpha and comparison with the human cDNA."
Sermon K., Demeirleir L., Elpers I., Lissens W., Liebaers I.
Nucleic Acids Res. 18:4925-4925(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Muscle.
[2]"Regulation of kinase reactions in pig heart pyruvate dehydrogenase complex."
Kerbey A.L., Radcliffe P.M., Randle P.J., Sugden P.H.
Biochem. J. 181:427-433(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, COFACTOR, PHOSPHORYLATION AT SER-231; SER-292 AND SER-299.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X52990 mRNA. Translation: CAA37180.1.
PIRDEPGPA. S20813.
UniGeneSsc.50287.
Ssc.98154.

3D structure databases

ProteinModelPortalP29804.
SMRP29804. Positions 28-389.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP29804.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG001863.

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...

Entry information

Entry nameODPA_PIG
AccessionPrimary (citable) accession number: P29804
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: June 11, 2014
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program