Skip Header

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

P29804 (ODPA_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified June 28, 2011. Version 69. 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, somatic form, mitochondrial
EC=1.2.4.1
Alternative name(s):
PDHE1-A type I
Gene names
Name:PDHA1
OrganismSus scrofa (Pig) [Complete proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

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. 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.

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
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
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 peptide‹1 – 28›28Mitochondrion By similarity
Chain29 – 389361Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial
PRO_0000020443

Amino acid modifications

Modified residue761N6-acetyllysine By similarity
Modified residue821N6-acetyllysine By similarity
Modified residue2301Phosphothreonine By similarity
Modified residue2311Phosphoserine Ref.2
Modified residue2881Phosphotyrosine By similarity
Modified residue2921Phosphoserine Ref.2
Modified residue2941Phosphoserine By similarity
Modified residue2991Phosphoserine Ref.2
Modified residue3001Phosphotyrosine By similarity
Modified residue3201N6-acetyllysine By similarity
Modified residue3351N6-acetyllysine 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: 2395657] [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: 227365] [Abstract]
Cited for: 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.

3D structure databases

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

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_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 28, 2011
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info