Reviewed, UniProtKB/Swiss-Prot P52903 (ODPA_SOLTU)

Names and origin

Protein names	Recommended name:     Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial       Short name=PDHE1-A     EC=1.2.4.1
Organism	Solanum tuberosum (Potato)
Taxonomic identifier	4113 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Solanaceae › Solanoideae › Solaneae › Solanum

Protein attributes

Sequence length	391 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 By similarity.
Subunit structure	Tetramer of 2 alpha and 2 beta subunits By similarity.
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 – 26	26	Mitochondrion Ref.2
	Chain	27 – 391	365	Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial		PRO_0000020455

Sequences

	Sequence		Length	Mass (Da)
	P52903-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: F9110B374B022F0D	FASTA	391	43,228
	10 20 30 40 50 60 MALSTSRAIN HIMKPLSAAV CATRRLSSDS TATITVETSL PFTSHNIDPP SRSVETSPKE 70 80 90 100 110 120 LMTFFKDMTE MRRMEIAADS LYKAKLIRGF CHLYDGQEAV AVGMEAAITK KDCIITAYRD 130 140 150 160 170 180 HCIFLGRGGT LVEAFAELMG RRDGCSRGKG GSMHFYKKES GFYGGHGIVG AQVPLGIGLA 190 200 210 220 230 240 FAQKYKKEDY VTFAMYGDGA ANQGQLFEAL NMAALWDLPA ILVCENNHYG MGTAEWRAAK 250 260 270 280 290 300 SPAYYKRGDY VPGLRVDGMD VFAVKQACTF AKQHALKNGP IILEMDTYRY HGHSMSDPGS 310 320 330 340 350 360 TYRTRDEISG VRQERDPVER IRSLILAHNI ATEAELKDIE KENRKVVDEA IAKAKESPMP 370 380 390 DPSELFTNVY VKGFGVEAYG ADRKELRATL P

References

[1]	"Mitochondrial pyruvate dehydrogenase. Molecular cloning of the E1 alpha subunit and expression analysis." Grof C.P., Winning B.M., Scaysbrook T.P., Hill S.A., Leaver C.J. Plant Physiol. 108:1623-1629(1995) [PubMed: 7659754] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Desiree. Tissue: Leaf.
[2]	"Plant mitochondrial pyruvate dehydrogenase complex: purification and identification of catalytic components in potato." Millar A.H., Knorpp C., Leaver C.J., Hill S.A. Biochem. J. 334:571-576(1998) [PubMed: 9729464] [Abstract] Cited for: PROTEIN SEQUENCE OF 27-42. Strain: cv. Romano. Tissue: Tuber.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z26949 mRNA. Translation: CAA81558.1.
PIR	T07372.
3D structure databases
HSSP	HSSP built from PDB template 1NI4 based on UniProtKB P08559.
ModBase	Search...
Protein-protein interaction databases
IntAct	P52903. 1 interaction.
Enzyme and pathway databases
BRENDA	1.2.4.1. 296.
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_SOLTU

Accession

Primary (citable) accession number: P52903

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
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)

Annotation project

PPAP (Plant Proteome Annotation Project)