Skip Header

 
Contribute Send feedback
Read comments (1) or add your own

Reviewed, UniProtKB/Swiss-Prot P29804 (ODPA_PIG)

Last modified June 16, 2009. Version 59. 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

Hide | Top

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)
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Hide | Top

Protein attributes

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

Hide | Top

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.

Hide | Top

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...

Hide | Top

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 residue2311Phosphoserine Ref.2
Modified residue2881Phosphotyrosine By similarity
Modified residue2921Phosphoserine Ref.2
Modified residue2941Phosphoserine By similarity
Modified residue2991Phosphoserine Ref.2
Modified residue3001Phosphotyrosine By similarity

Experimental info

Non-terminal residue11

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
P29804-1 [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

Hide | Top

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.

Hide | Top

Cross-references

Sequence databases

X52990 mRNA. Translation: CAA37180.1.
PIRDEPGPA. S20813.

3D structure databases

HSSPHSSP built from PDB template 1NI4 based on UniProtKB P08559.
SMRP29804. Positions 28-389.
ModBaseSearch...

Phylogenomic databases

HOVERGENP29804.

Enzyme and pathway databases

BRENDA1.2.4.1. 249.

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...

Hide | Top

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 16, 2009
This is version 59 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