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Protein

Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial

Gene

pda1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2.

Cofactori

Enzyme regulationi

E1 activity is regulated by phosphorylation (inactivation) and dephosphorylation (activation) of the alpha subunit.By similarity

GO - Molecular functioni

  1. pyruvate dehydrogenase (acetyl-transferring) activity Source: PomBase

GO - Biological processi

  1. acetyl-CoA biosynthetic process from pyruvate Source: PomBase
  2. glycolytic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Pyruvate, Thiamine pyrophosphate

Enzyme and pathway databases

ReactomeiREACT_332635. Regulation of pyruvate dehydrogenase (PDH) complex.
REACT_341792. Pyruvate metabolism.
REACT_352376. Signaling by Retinoic Acid.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial (EC:1.2.4.1)
Short name:
PDHE1-A
Gene namesi
Name:pda1
ORF Names:SPAC26F1.03
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome I

Organism-specific databases

PomBaseiSPAC26F1.03.

Subcellular locationi

Mitochondrion matrix By similarity

GO - Cellular componenti

  1. mitochondrial pyruvate dehydrogenase complex Source: PomBase
  2. mitochondrion Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 409Pyruvate dehydrogenase E1 component subunit alpha, mitochondrialPRO_0000020451
Transit peptidei1 – ?MitochondrionSequence Analysis

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei6 – 61Phosphothreonine1 Publication
Modified residuei306 – 3061Phosphotyrosine1 Publication
Modified residuei310 – 3101Phosphoserine1 Publication
Modified residuei312 – 3121Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ10489.
PaxDbiQ10489.
PRIDEiQ10489.

Interactioni

Subunit structurei

Tetramer of 2 alpha and 2 beta subunits.By similarity

Protein-protein interaction databases

BioGridi278076. 4 interactions.
MINTiMINT-4699682.
STRINGi4896.SPAC26F1.03-1.

Structurei

3D structure databases

ProteinModelPortaliQ10489.
SMRiQ10489. Positions 62-404.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1071.
HOGENOMiHOG000281336.
InParanoidiQ10489.
KOiK00161.
OMAiPESHYAY.
OrthoDBiEOG7QZGMC.
PhylomeDBiQ10489.

Family and domain databases

Gene3Di3.40.50.970. 1 hit.
InterProiIPR001017. DH_E1.
IPR017597. Pyrv_DH_E1_asu_subgrp-y.
IPR029061. THDP-binding.
[Graphical view]
PfamiPF00676. E1_dh. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 1 hit.
TIGRFAMsiTIGR03182. PDH_E1_alph_y. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q10489-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFRTCTKIGT VPKVLVNQKG LIDGLRRVTT DATTSRANPA HVPEEHDKPF
60 70 80 90 100
PVKLDDSVFE GYKIDVPSTE IEVTKGELLG LYEKMVTIRR LELACDALYK
110 120 130 140 150
AKKIRGFCHL SIGQEAVAAG IEGAITLDDS IITSYRCHGF AYTRGLSIRS
160 170 180 190 200
IIGELMGRQC GASKGKGGSM HIFAKNFYGG NGIVGAQIPL GAGIGFAQKY
210 220 230 240 250
LEKPTTTFAL YGDGASNQGQ AFEAFNMAKL WGLPVIFACE NNKYGMGTSA
260 270 280 290 300
ERSSAMTEFY KRGQYIPGLL VNGMDVLAVL QASKFAKKYT VENSQPLLME
310 320 330 340 350
FVTYRYGGHS MSDPGTTYRS REEVQKVRAA RDPIEGLKKH IMEWGVANAN
360 370 380 390 400
ELKNIEKRIR GMVDEEVRIA EESPFPDPIE ESLFSDVYVA GTEPAYARGR

NSLEYHQYK
Length:409
Mass (Da):45,138
Last modified:October 1, 1996 - v1
Checksum:i0FAE33765847C185
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAA97360.1.
PIRiT38417.
RefSeqiNP_594892.1. NM_001020321.2.

Genome annotation databases

EnsemblFungiiSPAC26F1.03.1; SPAC26F1.03.1:pep; SPAC26F1.03.
GeneIDi2541579.
KEGGispo:SPAC26F1.03.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAA97360.1.
PIRiT38417.
RefSeqiNP_594892.1. NM_001020321.2.

3D structure databases

ProteinModelPortaliQ10489.
SMRiQ10489. Positions 62-404.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278076. 4 interactions.
MINTiMINT-4699682.
STRINGi4896.SPAC26F1.03-1.

Proteomic databases

MaxQBiQ10489.
PaxDbiQ10489.
PRIDEiQ10489.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC26F1.03.1; SPAC26F1.03.1:pep; SPAC26F1.03.
GeneIDi2541579.
KEGGispo:SPAC26F1.03.

Organism-specific databases

PomBaseiSPAC26F1.03.

Phylogenomic databases

eggNOGiCOG1071.
HOGENOMiHOG000281336.
InParanoidiQ10489.
KOiK00161.
OMAiPESHYAY.
OrthoDBiEOG7QZGMC.
PhylomeDBiQ10489.

Enzyme and pathway databases

ReactomeiREACT_332635. Regulation of pyruvate dehydrogenase (PDH) complex.
REACT_341792. Pyruvate metabolism.
REACT_352376. Signaling by Retinoic Acid.

Miscellaneous databases

NextBioi20802673.
PROiQ10489.

Family and domain databases

Gene3Di3.40.50.970. 1 hit.
InterProiIPR001017. DH_E1.
IPR017597. Pyrv_DH_E1_asu_subgrp-y.
IPR029061. THDP-binding.
[Graphical view]
PfamiPF00676. E1_dh. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 1 hit.
TIGRFAMsiTIGR03182. PDH_E1_alph_y. 1 hit.
ProtoNetiSearch...

Publicationsi

  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(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-6; TYR-306; SER-310 AND SER-312, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiODPA_SCHPO
AccessioniPrimary (citable) accession number: Q10489
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 1, 2015
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.