Reviewed, UniProtKB/Swiss-Prot P52900 (ODPA_SMIMA)

Names and origin

Protein names

Recommended name:
    Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial
      Short name=PDHE1-A
    EC=1.2.4.1

Gene names

Name:

PDHA

Organism

Sminthopsis macroura (Stripe-faced dunnart)

Taxonomic identifier

9302 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Metatheria › Dasyuromorphia › Dasyuridae › Sminthopsis

Protein attributes

Sequence length	363 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). 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 + CO(2).
Cofactor	Thiamine pyrophosphate.
Enzyme regulation	E1 activity is regulated by phosphorylation (inactivation) and dephosphorylation (activation) of the alpha subunit By similarity.
Subunit structure	Tetramer of 2 alpha and 2 beta subunits.
Subcellular location	Mitochondrion matrix.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Pyruvate Thiamine pyrophosphate
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	pyruvate dehydrogenase (acetyl-transferring) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	‹1 – 2	›2	Mitochondrion By similarity
	Chain	3 – 363	361	Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial		PRO_0000020446
Amino acid modifications
	Modified residue	205	1	Phosphoserine By similarity
	Modified residue	262	1	Phosphotyrosine By similarity
	Modified residue	266	1	Phosphoserine By similarity
	Modified residue	268	1	Phosphoserine By similarity
	Modified residue	273	1	Phosphoserine By similarity
	Modified residue	274	1	Phosphotyrosine By similarity
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	P52900-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 4884E0A17D7A15A8	FASTA	363	40,735
	10 20 30 40 50 60 RNFANDATFD IKKCDVHRLE EGPPTTAVLT REEGLKYYKI MQTVRRMELK ADQLYKQKII 70 80 90 100 110 120 RGFCHLYDGQ EACCMGLEAG INPTDHVITA YRAHGFTYTR GLPVREILAE LTGRRGGCAK 130 140 150 160 170 180 GKGGSMHMYA KNFYGGNGIV GAQVPLGVGI ALACKYNEKD EICLTLYGDG AANQGQIFEA 190 200 210 220 230 240 YNMAALWKLP CIFICENNRY GMGTSVERAA ASTDYYKRGD FIPGIMVDGM DVLCVREATK 250 260 270 280 290 300 FAAAYCRSGK GPMLMELQTY RYHGHSMSDP GVSYRTREEI QEVRSKSDPI MLLKDRMVNN 310 320 330 340 350 360 NLASIEELKE IDVEVRKEIE DAAQFATADP EPPLEELGYH IYSRDPPFEV RGANQWIKYK SVS

References

[1]

"A eutherian X-linked gene, PDHA1, is autosomal in marsupials: a model for the evolution of a second, testis-specific variant in eutherian mammals." Fitzgerald J., Wilcox S.A., Graves J.A., Dahl H.H.M. Genomics 18:636-642(1993) [PubMed: 8307573] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Testis.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L20774 mRNA. Translation: AAA31589.1.
3D structure databases
HSSP	HSSP built from PDB template 1NI4 based on UniProtKB P08559.
SMR	P52900. Positions 2-363.
ModBase	Search...
Phylogenomic databases
HOVERGEN	P52900.
Family and domain databases
InterPro	IPR001017. DHase_E1. IPR017597. Pyrv_DH_E1_asu_subgrp-y. [Graphical view]
Pfam	PF00676. E1_dh. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ODPA_SMIMA

Accession

Primary (citable) accession number: P52900

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	November 4, 2008
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)