P26267 (ODPA_ASCSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Pyruvate dehydrogenase E1 component subunit alpha type I, mitochondrial Short name=PDHA1 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	396 AA.
Sequence status	Complete.
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.
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 PDHA1; it is reactivated by dephosphorylation.
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) 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
Technical term	Direct protein sequencing
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 – 25	25	Mitochondrion
	Chain	26 – 396	371	Pyruvate dehydrogenase E1 component subunit alpha type I, mitochondrial		PRO_0000020437
Amino acid modifications
	Modified residue	289	1	Phosphoserine Ref.2
	Modified residue	296	1	Phosphoserine Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P26267 [UniParc]. Last modified May 1, 1992. Version 1. Checksum: 60A810BB5B48B836	FASTA	396	43,771
	10 20 30 40 50 60 MIFVFANIFK VPTVSPSVMA ISVRLASTEA TFQTKPFKLH KLDSGPDINV HVTKEDAVHY 70 80 90 100 110 120 YTQMLTIRRM ESAAGNLYKE KKVRGFCHLY SGQEACAVGT KAAMDAGDAA VTAYRCHGWT 130 140 150 160 170 180 YLSGSSVAKV LCELTGRITG NVYGKGGSMH MYGENFYGGN GIVGAQQPLG TGIAFAMKYR 190 200 210 220 230 240 KEKNVCITMF GDGATNQGQL FESMNMAKLW DLPVLYVCEN NGYGMGTAAA RSSASTDYYT 250 260 270 280 290 300 RGDYVPGIWV DGMDVLAVRQ AVRWAKEWCN AGKGPLMIEM ATYRYSGHSM SDPGTSYRTR 310 320 330 340 350 360 EEVQEVRKTR DPITGFKDKI VTAGLVTEDE IKEIDKQVRK EIDAAVKQAH TDKESPVELM 370 380 390 LTDIYYNTPA QYVRCTTDEV LQKYLTSEEA VKALAK

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].
[2]	"Phosphorylation and inactivation of the pyruvate dehydrogenase from the anaerobic parasitic nematode, Ascaris suum. Stoichiometry and amino acid sequence around the phosphorylation sites." Thissen J., Komuniecki R. J. Biol. Chem. 263:19092-19097(1988) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 285-298, PHOSPHORYLATION AT SER-289 AND SER-296.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M76555 mRNA. Translation: AAA29376.1.
PIR	A31963. A45608.
3D structure databases
ProteinModelPortal	P26267.
SMR	P26267. Positions 27-374.
ModBase	Search...
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

ODPA_ASCSU

Accession

Primary (citable) accession number: P26267

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	May 1, 1992
Last modified:	April 3, 2013
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)