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P40387

- TPS1_SCHPO

UniProt

P40387 - TPS1_SCHPO

Protein

Alpha,alpha-trehalose-phosphate synthase [UDP-forming]

Gene

tps1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 2 (14 Aug 2001)
      Previous versions | rss
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    Functioni

    Appears to have a role in spore germination. In S.pombe it appears to have no role in the control of the initial steps of glycolysis.

    Catalytic activityi

    UDP-glucose + D-glucose 6-phosphate = UDP + alpha,alpha-trehalose 6-phosphate.

    GO - Molecular functioni

    1. alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity Source: PomBase
    2. protein binding Source: PomBase

    GO - Biological processi

    1. ascospore formation Source: PomBase
    2. cellular response to desiccation Source: PomBase
    3. cellular response to ethanol Source: PomBase
    4. cellular response to freezing Source: PomBase
    5. cellular response to heat Source: PomBase
    6. positive regulation of trehalose catabolic process Source: PomBase
    7. trehalose biosynthesis in response to heat stress Source: PomBase

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Stress response

    Protein family/group databases

    CAZyiGT20. Glycosyltransferase Family 20.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha,alpha-trehalose-phosphate synthase [UDP-forming] (EC:2.4.1.15)
    Alternative name(s):
    Trehalose-6-phosphate synthase
    UDP-glucose-glucosephosphate glucosyltransferase
    Gene namesi
    Name:tps1
    ORF Names:SPAC328.03
    OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
    Taxonomic identifieri284812 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
    ProteomesiUP000002485: Chromosome I

    Organism-specific databases

    PomBaseiSPAC328.03.

    Subcellular locationi

    GO - Cellular componenti

    1. alpha,alpha-trehalose-phosphate synthase complex (UDP-forming) Source: PomBase
    2. cytosol Source: PomBase

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 513513Alpha,alpha-trehalose-phosphate synthase [UDP-forming]PRO_0000122500Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei40 – 401Phosphotyrosine1 Publication
    Modified residuei503 – 5031Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP40387.
    PaxDbiP40387.

    Expressioni

    Inductioni

    By heat shock.

    Interactioni

    Protein-protein interaction databases

    BioGridi279113. 93 interactions.
    MINTiMINT-4689743.
    STRINGi4896.SPAC328.03-1.

    Structurei

    3D structure databases

    ProteinModelPortaliP40387.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyltransferase 20 family.Curated

    Phylogenomic databases

    eggNOGiCOG0380.
    HOGENOMiHOG000191477.
    KOiK00697.
    OMAiWGESFVK.
    OrthoDBiEOG76QFS6.
    PhylomeDBiP40387.

    Family and domain databases

    InterProiIPR001830. Glyco_trans_20.
    IPR012766. Trehalose_OtsA.
    [Graphical view]
    PfamiPF00982. Glyco_transf_20. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR02400. trehalose_OtsA. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P40387-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSDAHDTIKS LTGDASNSRR LIVVSNRLPI TIKRKDNGTY DFSMSSGGLV    50
    SALSGLKKLM TFQWLGWCGQ EIPEDEKPMI IQRLQDECSA IPVFLDDETA 100
    DRHYNGFSNS ILWPLFHYHP GEINFDEENW EAYRAANYAF AEAIVKNLQD 150
    GDLIWVQDYH LMVLPQMLRE LIGDKFKDIK IGFFLHTPFP SSEIYRVLPV 200
    RNEILEGVLN CDLVGFHTYD YARHFLSACS RILNLSTLPN GVEYNGQMVS 250
    VGTFPIGIDP EKFSDALKSD VVKDRIASIE RRLQGVKVIV GVDRLDYIKG 300
    VPQKFHAFEV FLEQYPEWVG KVVLVQVAVP SRQDVEEYQN LRAVVNELVG 350
    RINGRFGTVE YTPIHFLHKS VRFEELVALY NVSDVCLITS TRDGMNLVSY 400
    EYICTQQERH GALILSEFAG AAQSLNGSIV INPWNTEELA NSIHDALTMP 450
    EKQREANENK LFRYVNKYTS QFWGQSFVGE LQRIQHYSHP HPRRTNPILR 500
    TKSAQVLSMN SSS 513
    Length:513
    Mass (Da):58,493
    Last modified:August 14, 2001 - v2
    Checksum:i9FC247B626CE2B00
    GO

    Sequence cautioni

    The sequence CAA82861.1 differs from that shown. Reason: Frameshift at position 475.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti277 – 2771A → R in CAA82861. (PubMed:8021171)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z29971 Genomic DNA. Translation: CAA82861.1. Frameshift.
    CU329670 Genomic DNA. Translation: CAB95998.1.
    PIRiT46564.
    RefSeqiNP_594205.1. NM_001019628.2.

    Genome annotation databases

    EnsemblFungiiSPAC328.03.1; SPAC328.03.1:pep; SPAC328.03.
    GeneIDi2542660.
    KEGGispo:SPAC328.03.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z29971 Genomic DNA. Translation: CAA82861.1 . Frameshift.
    CU329670 Genomic DNA. Translation: CAB95998.1 .
    PIRi T46564.
    RefSeqi NP_594205.1. NM_001019628.2.

    3D structure databases

    ProteinModelPortali P40387.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 279113. 93 interactions.
    MINTi MINT-4689743.
    STRINGi 4896.SPAC328.03-1.

    Protein family/group databases

    CAZyi GT20. Glycosyltransferase Family 20.

    Proteomic databases

    MaxQBi P40387.
    PaxDbi P40387.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii SPAC328.03.1 ; SPAC328.03.1:pep ; SPAC328.03 .
    GeneIDi 2542660.
    KEGGi spo:SPAC328.03.

    Organism-specific databases

    PomBasei SPAC328.03.

    Phylogenomic databases

    eggNOGi COG0380.
    HOGENOMi HOG000191477.
    KOi K00697.
    OMAi WGESFVK.
    OrthoDBi EOG76QFS6.
    PhylomeDBi P40387.

    Miscellaneous databases

    NextBioi 20803708.
    PROi P40387.

    Family and domain databases

    InterProi IPR001830. Glyco_trans_20.
    IPR012766. Trehalose_OtsA.
    [Graphical view ]
    Pfami PF00982. Glyco_transf_20. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR02400. trehalose_OtsA. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Trehalose-6-P synthase is dispensable for growth on glucose but not for spore germination in Schizosaccharomyces pombe."
      Blazquez M.A., Stucka R., Feldmann H., Gancedo C.
      J. Bacteriol. 176:3895-3902(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "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.
    3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-40 AND SER-503, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiTPS1_SCHPO
    AccessioniPrimary (citable) accession number: P40387
    Secondary accession number(s): Q9P3U3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: August 14, 2001
    Last modified: October 1, 2014
    This is version 109 of the entry and version 2 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
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3