Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial precursor

Contribute

Send feedback

Read comments (?) or add your own

P29804 (ODPA_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 75. History...

Clusters with 100%, 90%, 50% identity |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info Customize order

Names and origin

Protein names

Recommended 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

Organism

Sus scrofa (Pig) [Reference proteome]

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length	389 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Glucose metabolism Tricarboxylic acid cycle
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Pyruvate Thiamine pyrophosphate
Molecular function	Oxidoreductase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	acetyl-CoA biosynthetic process from pyruvate Inferred from sequence or structural similarity. Source: UniProtKB glycolysis Inferred from electronic annotation. Source: InterPro tricarboxylic acid cycle Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell pyruvate dehydrogenase complex Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	pyruvate dehydrogenase (acetyl-transferring) activity Inferred from electronic annotation. Source: EC pyruvate dehydrogenase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

‹1 – 28

›28

Mitochondrion By similarity

Chain

29 – 389

361

Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial

PRO_0000020443

Amino acid modifications

Modified residue

231

Phosphoserine; by PDK1 By similarity

Modified residue

288

Phosphotyrosine By similarity

Modified residue

292

Phosphoserine; by PDK1, PDK2, PDK3 and PDK4 By similarity

Modified residue

294

Phosphoserine By similarity

Modified residue

299

Phosphoserine; by PDK1, PDK2, PDK3 and PDK4 By similarity

Modified residue

300

Phosphotyrosine By similarity

Modified residue

320

N6-acetyllysine By similarity

Experimental info

Non-terminal residue

Sequences

Sequence

Length

Mass (Da)

Tools

P29804 [UniParc].

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

FASTA

389

43,121

        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.
PIR	DEPGPA. S20813.
UniGene	Ssc.50287.
3D structure databases
ProteinModelPortal	P29804.
SMR	P29804. Positions 28-389.
ModBase	Search...
Proteomic databases
PRIDE	P29804.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
HOVERGEN	HBG001863.
Family and domain databases
InterPro	IPR001017. DH_E1. IPR017597. Pyrv_DH_E1_asu_subgrp-y. [Graphical view]
Pfam	PF00676. E1_dh. 1 hit. [Graphical view]
TIGRFAMs	TIGR03182. PDH_E1_alph_y. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ODPA_PIG

Accession

Primary (citable) accession number: P29804

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	April 3, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Proteomic databases

Protocols and materials databases

Phylogenomic databases

Family and domain databases

Entry information