Reviewed, UniProtKB/Swiss-Prot P26267 (ODPA_ASCSU)

Names and origin

Protein names	Recommended name:     Pyruvate dehydrogenase E1 component subunit alpha type I, mitochondrial       Short name=PDHE1-A     EC=1.2.4.1
Organism	Ascaris suum (Pig roundworm) (Ascaris lumbricoides)
Taxonomic identifier	6253 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › 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. 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 + CO2.
Cofactor	Thiamine pyrophosphate.
Enzyme regulation	E1 activity is regulated by phosphorylation (inactivation) and dephosphorylation (activation) of the alpha subunit.
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
Technical term	Direct protein sequencing
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 – 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)
	P26267-1 [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: 1565136] [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: 3198613] [Abstract] Cited for: PROTEIN SEQUENCE OF 285-298, PHOSPHORYLATION AT SER-289 AND SER-296.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M76555 mRNA. Translation: AAA29376.1.
PIR	A31963. A45608.
3D structure databases
HSSP	HSSP built from PDB template 1NI4 based on UniProtKB P08559.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.2.4.1. 649.
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:	June 16, 2009
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)