Reviewed, UniProtKB/Swiss-Prot Q10489 (ODPA_SCHPO)

Names and origin

Protein names

Recommended name:
    Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial
      Short name=PDHE1-A
    EC=1.2.4.1

Gene names

Name:	pda1
ORF Names:	SPAC26F1.03

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	409 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 CO(2). 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 + CO(2).
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 matrixBy similarity.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Pyruvate Thiamine pyrophosphate
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome
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 – ?		Mitochondrion Potential
	Chain	? – 409		Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial		PRO_0000020451
Amino acid modifications
	Modified residue	6	1	Phosphothreonine
	Modified residue	306	1	Phosphotyrosine
	Modified residue	310	1	Phosphoserine
	Modified residue	312	1	Phosphoserine

Sequences

	Sequence		Length	Mass (Da)
	Q10489-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 0FAE33765847C185	FASTA	409	45,138
	10 20 30 40 50 60 MFRTCTKIGT VPKVLVNQKG LIDGLRRVTT DATTSRANPA HVPEEHDKPF PVKLDDSVFE 70 80 90 100 110 120 GYKIDVPSTE IEVTKGELLG LYEKMVTIRR LELACDALYK AKKIRGFCHL SIGQEAVAAG 130 140 150 160 170 180 IEGAITLDDS IITSYRCHGF AYTRGLSIRS IIGELMGRQC GASKGKGGSM HIFAKNFYGG 190 200 210 220 230 240 NGIVGAQIPL GAGIGFAQKY LEKPTTTFAL YGDGASNQGQ AFEAFNMAKL WGLPVIFACE 250 260 270 280 290 300 NNKYGMGTSA ERSSAMTEFY KRGQYIPGLL VNGMDVLAVL QASKFAKKYT VENSQPLLME 310 320 330 340 350 360 FVTYRYGGHS MSDPGTTYRS REEVQKVRAA RDPIEGLKKH IMEWGVANAN ELKNIEKRIR 370 380 390 400 GMVDEEVRIA EESPFPDPIE ESLFSDVYVA GTEPAYARGR NSLEYHQYK

References

[1]

"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.

[2]

"Phosphoproteome analysis of fission yeast." Wilson-Grady J.T., Villen J., Gygi S.P. J. Proteome Res. 7:1088-1097(2008) [PubMed: 18257517] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-6; TYR-306; SER-310 AND SER-312, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CU329670 Genomic DNA. Translation: CAA97360.1.
PIR	T38417.
RefSeq	NP_594892.1.
3D structure databases
HSSP	HSSP built from PDB template 1NI4 based on UniProtKB P08559.
ModBase	Search...
Genome annotation databases
GeneID	2541579.
KEGG	spo:SPAC26F1.03.
NMPDR	fig|4896.1.peg.4862.
Organism-specific databases
GeneDB_Spombe	SPAC26F1.03.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-002960-MON.
Gene expression databases
ArrayExpress	Q10489.
Family and domain databases
InterPro	IPR001017. DHase_E1. IPR017597. Pyrv_DH_E1_asu_subgrp-y. [Graphical view]
Pfam	PF00676. E1_dh. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ODPA_SCHPO

Accession

Primary (citable) accession number: Q10489

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	November 25, 2008
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)