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Q10489

- ODPA_SCHPO

UniProt

Q10489 - ODPA_SCHPO

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Protein

Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial

Gene
pda1, SPAC26F1.03
Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - 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

Thiamine pyrophosphate By similarity.

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_215777. Pyruvate metabolism.

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: 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 – ?Mitochondrion Reviewed prediction

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. 6 interactions.
MINTiMINT-4699682.
STRINGi4896.SPAC26F1.03-1.

Structurei

3D structure databases

ProteinModelPortaliQ10489.
SMRiQ10489. Positions 62-404.

Family & Domainsi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1071.
HOGENOMiHOG000281336.
KOiK00161.
OMAiRERTCHA.
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

MFRTCTKIGT VPKVLVNQKG LIDGLRRVTT DATTSRANPA HVPEEHDKPF    50
PVKLDDSVFE GYKIDVPSTE IEVTKGELLG LYEKMVTIRR LELACDALYK 100
AKKIRGFCHL SIGQEAVAAG IEGAITLDDS IITSYRCHGF AYTRGLSIRS 150
IIGELMGRQC GASKGKGGSM HIFAKNFYGG NGIVGAQIPL GAGIGFAQKY 200
LEKPTTTFAL YGDGASNQGQ AFEAFNMAKL WGLPVIFACE NNKYGMGTSA 250
ERSSAMTEFY KRGQYIPGLL VNGMDVLAVL QASKFAKKYT VENSQPLLME 300
FVTYRYGGHS MSDPGTTYRS REEVQKVRAA RDPIEGLKKH IMEWGVANAN 350
ELKNIEKRIR GMVDEEVRIA EESPFPDPIE ESLFSDVYVA GTEPAYARGR 400
NSLEYHQYK 409
Length:409
Mass (Da):45,138
Last modified:October 1, 1996 - v1
Checksum:i0FAE33765847C185
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
CU329670 Genomic DNA. Translation: CAA97360.1 .
PIRi T38417.
RefSeqi NP_594892.1. NM_001020321.2.

3D structure databases

ProteinModelPortali Q10489.
SMRi Q10489. Positions 62-404.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 278076. 6 interactions.
MINTi MINT-4699682.
STRINGi 4896.SPAC26F1.03-1.

Proteomic databases

MaxQBi Q10489.
PaxDbi Q10489.
PRIDEi Q10489.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii SPAC26F1.03.1 ; SPAC26F1.03.1:pep ; SPAC26F1.03 .
GeneIDi 2541579.
KEGGi spo:SPAC26F1.03.

Organism-specific databases

PomBasei SPAC26F1.03.

Phylogenomic databases

eggNOGi COG1071.
HOGENOMi HOG000281336.
KOi K00161.
OMAi RERTCHA.
OrthoDBi EOG7QZGMC.
PhylomeDBi Q10489.

Enzyme and pathway databases

Reactomei REACT_215777. Pyruvate metabolism.

Miscellaneous databases

NextBioi 20802673.
PROi Q10489.

Family and domain databases

Gene3Di 3.40.50.970. 1 hit.
InterProi IPR001017. DH_E1.
IPR017597. Pyrv_DH_E1_asu_subgrp-y.
IPR029061. THDP-binding.
[Graphical view ]
Pfami PF00676. E1_dh. 1 hit.
[Graphical view ]
SUPFAMi SSF52518. SSF52518. 1 hit.
TIGRFAMsi TIGR03182. PDH_E1_alph_y. 1 hit.
ProtoNeti Search...

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(2002) [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: September 3, 2014
This is version 102 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

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