P26268 (ODPT_ASCSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Pyruvate dehydrogenase E1 component subunit alpha type II, mitochondrial Short name=PDHA2 Short name=PDHE1-A EC=1.2.4.1
Organism	Ascaris suum (Pig roundworm) (Ascaris lumbricoides)
Taxonomic identifier	6253 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Nematoda › Chromadorea › Ascaridida › Ascaridoidea › Ascarididae › Ascaris

Protein attributes

Sequence length	391 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 CO2, and thereby links the glycolytic pathway to the tricarboxylic cycle.
Catalytic activity	Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2.
Cofactor	Thiamine pyrophosphate.
Enzyme regulation	Pyruvate dehydrogenase activity is inhibited by phosphorylation of PDHA2; it is reactivated by dephosphorylation.
Subunit structure	Heterotetramer of two PDHA2 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) By similarity.
Subcellular location	Mitochondrion matrix.

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	Phosphoprotein
Gene Ontology (GO)
Biological_process	glycolysis Inferred from electronic annotation. Source: InterPro tricarboxylic acid cycle 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 – 17	›17	Mitochondrion
	Chain	18 – 391	374	Pyruvate dehydrogenase E1 component subunit alpha type II, mitochondrial		PRO_0000020438
Amino acid modifications
	Modified residue	284	1	Phosphoserine Probable
	Modified residue	291	1	Phosphoserine Probable
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	P26268 [UniParc]. Last modified May 1, 1992. Version 1. Checksum: BA66E56C300FB8E7	FASTA	391	43,207
	10 20 30 40 50 60 SNIFKGPTVG SSVVAMSARL ASTEATFQAK PFKLHKLDSG PDVNMHVTKE DALRYYTQMQ 70 80 90 100 110 120 TIRRMETAAG NLYKEKKVRG FCHLYSGQEA CAVGMKAAME PGDAAITAYR CHGWTYLSGS 130 140 150 160 170 180 PVAKVLCELT GRITGNVYGK GGSMHMYGEN FYGGNGIVGA QQPLGTGIAF AMKYKKQKNV 190 200 210 220 230 240 CITLFGDGAT NQGQLYESMN MAKLWELPVL YVCENNGYGM GTSAARSSAS TDYYTRGDYV 250 260 270 280 290 300 PGFWVDGMDV LAVRQAIRWG KEWCNAGKGP LMIEMATYRY GGHSMSDPGT SYRTREEIQE 310 320 330 340 350 360 VRKTRDPITG FKDKIVTAGL VTEDELKEVD KEIRKEVDAA VKQAHTDKEA PVEMLLTDIY 370 380 390 YNTPAQYVRC TTEDVLQQYV TSEEAFKALS K

References

[1]	"Characterization of cDNA clones for the alpha subunit of pyruvate dehydrogenase from Ascaris suum." Johnson K.R., Komuniecki R., Sun Y., Wheelock M.J. Mol. Biochem. Parasitol. 51:37-48(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	M76554 mRNA. Translation: AAA29377.1.
3D structure databases
ProteinModelPortal	P26268.
SMR	P26268. Positions 22-369.
ModBase	Search...
Proteomic databases
PRIDE	P26268.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
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

ODPT_ASCSU

Accession

Primary (citable) accession number: P26268

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	May 1, 1992
Last modified:	April 3, 2013
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)