Reviewed, UniProtKB/Swiss-Prot A5A6L0 (ODPA_PANTR)

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

Pan troglodytes (Chimpanzee)

Taxonomic identifier

9598 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pan

Protein attributes

Sequence length	390 AA.
Sequence status	Complete.
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 CO2. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) By similarity.
Catalytic activity	Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2.
Cofactor	Thiamine pyrophosphate By similarity.
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 By similarity.
Subcellular location	Mitochondrion matrix By similarity.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Pyruvate Thiamine pyrophosphate
Molecular function	Oxidoreductase
PTM	Acetylation 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 – 29	29	Mitochondrion By similarity
	Chain	30 – 390	361	Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial		PRO_0000297491
Amino acid modifications
	Modified residue	77	1	N6-acetyllysine By similarity
	Modified residue	83	1	N6-acetyllysine By similarity
	Modified residue	232	1	Phosphoserine By similarity
	Modified residue	289	1	Phosphotyrosine By similarity
	Modified residue	293	1	Phosphoserine By similarity
	Modified residue	295	1	Phosphoserine By similarity
	Modified residue	300	1	Phosphoserine By similarity
	Modified residue	301	1	Phosphotyrosine By similarity
	Modified residue	321	1	N6-acetyllysine By similarity
	Modified residue	336	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A5A6L0-1 [UniParc]. Last modified June 12, 2007. Version 1. Checksum: 4F95746CBB792E78	FASTA	390	43,238
	10 20 30 40 50 60 MRKMLAAVSR VLSGASQKPA SRVLVASRNF ANDATFEIKK CDLHRLEEGP PVTTVLTRED 70 80 90 100 110 120 GLKYYRMMQT VRRMELKADQ LYKQKIIRGF CHLCDGQEAC CVGLEAGINP TDHLITAYRA 130 140 150 160 170 180 HGFTFTRGLS VREILAELTG RKGGCAKGKG GSMHMYAKNF YGGNGIVGAQ VPLGAGIALA 190 200 210 220 230 240 CKYNGKDEVC LTLYGDGAAN QGQIFEAYNM AALWKLPCIF ICENNRYGMG TSVERAAAST 250 260 270 280 290 300 DYYKRGDFIP GLRVDGMDIL CVREATRFAA AYCRSGKGPI LMELQTYRYH GHSMSGPGVS 310 320 330 340 350 360 YRTREEIQEV RSKSDPIMLL KDRMVNSNLA SVEELKEIDV EVRKEIEDAA QFATADPEPP 370 380 390 LEELGYHIYS SDPPFEVRGA NQWIKFKSVS

References

[1]

"Mapping of chimpanzee full-length cDNAs onto the human genome unveils large potential divergence of the transcriptome." Sakate R., Suto Y., Imanishi T., Tanoue T., Hida M., Hayasaka I., Kusuda J., Gojobori T., Hashimoto K., Hirai M. Gene 399:1-10(2007) [PubMed: 17574350] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB222138 mRNA. Translation: BAF62383.1.
RefSeq	NP_001104283.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	A5A6L0.
Genome annotation databases
Ensembl	ENSPTRT00000040292; ENSPTRP00000037227; ENSPTRG00000021717; Pan troglodytes. [Genome view]
GeneID	465525.
KEGG	ptr:465525.
Organism-specific databases
CTD	465525.
Enzyme and pathway databases
BRENDA	1.2.4.1. 264977.
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_PANTR

Accession

Primary (citable) accession number: A5A6L0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 24, 2007
Last sequence update:	June 12, 2007
Last modified:	October 13, 2009
This is version 21 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)