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Q10489

- ODPA_SCHPO

UniProt

Q10489 - ODPA_SCHPO

Protein

Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial

Gene

pda1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    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

    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

    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. 6 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.
    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: October 1, 2014
    This is version 103 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