TPS1_SCHPO
ID TPS1_SCHPO Reviewed; 513 AA.
AC P40387; Q9P3U3;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Alpha,alpha-trehalose-phosphate synthase [UDP-forming];
DE EC=2.4.1.15 {ECO:0000250|UniProtKB:Q00764};
DE AltName: Full=Trehalose-6-phosphate synthase;
DE AltName: Full=UDP-glucose-glucosephosphate glucosyltransferase;
GN Name=tps1 {ECO:0000303|PubMed:8021171};
GN ORFNames=SPAC328.03 {ECO:0000312|PomBase:SPAC328.03};
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=8021171; DOI=10.1128/jb.176.13.3895-3902.1994;
RA Blazquez M.A., Stucka R., Feldmann H., Gancedo C.;
RT "Trehalose-6-P synthase is dispensable for growth on glucose but not for
RT spore germination in Schizosaccharomyces pombe.";
RL J. Bacteriol. 176:3895-3902(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9729425; DOI=10.1016/s0304-4165(98)00039-7;
RA Cansado J., Vicente-Soler J., Soto T., Fernandez J., Gacto M.;
RT "Trehalose-6P synthase is essential for trehalase activation triggered by
RT glucose, nitrogen source or heat shock, but not by osmostress, in
RT Schizosaccharomyces pombe.";
RL Biochim. Biophys. Acta 1381:271-278(1998).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9495778; DOI=10.1128/jb.180.5.1342-1345.1998;
RA Cansado J., Soto T., Fernandez J., Vicente-Soler J., Gacto M.;
RT "Characterization of mutants devoid of neutral trehalase activity in the
RT fission yeast Schizosaccharomyces pombe: partial protection from heat shock
RT and high-salt stress.";
RL J. Bacteriol. 180:1342-1345(1998).
RN [5]
RP IDENTIFICATION IN THE TREHALOSE SYNTHASE COMPLEX, AND INTERACTION WITH NTP1
RP AND TPP1.
RX PubMed=12153582; DOI=10.1046/j.1432-1033.2002.03082.x;
RA Soto T., Franco A., Padmanabhan S., Vicente-Soler J., Cansado J., Gacto M.;
RT "Molecular interaction of neutral trehalase with other enzymes of trehalose
RT metabolism in the fission yeast Schizosaccharomyces pombe.";
RL Eur. J. Biochem. 269:3847-3855(2002).
RN [6]
RP INTERACTION WITH NTP1.
RX PubMed=12943532; DOI=10.1042/bj20030825;
RA Franco A., Soto T., Vicente-Soler J., Paredes V., Madrid M., Gacto M.,
RA Cansado J.;
RT "A role for calcium in the regulation of neutral trehalase activity in the
RT fission yeast Schizosaccharomyces pombe.";
RL Biochem. J. 376:209-217(2003).
RN [7]
RP INTERACTION WITH NTP1.
RX PubMed=15965643; DOI=10.1007/s00203-005-0005-4;
RA Franco A., Soto T., Madrid M., Vicente-Soler J., Gacto M., Cansado J.;
RT "Functional characterization of Schizosaccharomyces pombe neutral trehalase
RT altered in phosphorylatable serine residues.";
RL Arch. Microbiol. 183:394-400(2005).
RN [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-40 AND SER-503, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Synthase catalytic subunit of the trehalose synthase complex
CC that catalyzes the production of trehalose from glucose-6-phosphate and
CC UDP-alpha-D-glucose in a two step process (PubMed:8021171). The
CC disaccharide trehalose serves as a storage carbohydrate that is
CC mobilized during nutrient stress and spore germination (PubMed:8021171,
CC PubMed:9729425). Together with ntp1, regulates the level of trehalose
CC as a protectant for cell integrity during thermal and osmotic stress
CC (PubMed:9495778, PubMed:8021171). {ECO:0000269|PubMed:8021171,
CC ECO:0000269|PubMed:9495778, ECO:0000269|PubMed:9729425}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose 6-phosphate + UDP-alpha-D-glucose = alpha,alpha-
CC trehalose 6-phosphate + H(+) + UDP; Xref=Rhea:RHEA:18889,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58429,
CC ChEBI:CHEBI:58885, ChEBI:CHEBI:61548; EC=2.4.1.15;
CC Evidence={ECO:0000250|UniProtKB:Q00764};
CC -!- PATHWAY: Carbohydrate biosynthesis. {ECO:0000305}.
CC -!- SUBUNIT: Homomer (PubMed:12153582). Component of the trehalose synthase
CC complex that contains at least tps1, ntp1 and tpp1 (PubMed:12153582).
CC Interacts with tpp1 (PubMed:12153582). Interacts with ntp1; the
CC interaction is independent of stress conditions (PubMed:12153582,
CC PubMed:12943532, PubMed:15965643). {ECO:0000269|PubMed:12153582,
CC ECO:0000269|PubMed:12943532, ECO:0000269|PubMed:15965643}.
CC -!- INTERACTION:
CC P40387; O42893: ntp1; NbExp=3; IntAct=EBI-26616873, EBI-26616855;
CC P40387; P78875: tpp1; NbExp=2; IntAct=EBI-26616873, EBI-26616958;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- INDUCTION: By thermal stress. {ECO:0000269|PubMed:8021171}.
CC -!- DISRUPTION PHENOTYPE: Abolishes cytoplasmic neutral trehalase
CC activation during thermal stress; activation during osmotic stress is
CC normal (PubMed:9729425). Decreases cellular trehalose 6-phosphate level
CC in stationary phase and during thermal stress (PubMed:8021171).
CC Sensitive to heat shock and osmotic stress (PubMed:9495778).
CC {ECO:0000269|PubMed:8021171, ECO:0000269|PubMed:9495778,
CC ECO:0000269|PubMed:9729425}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 20 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA82861.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Z29971; CAA82861.1; ALT_FRAME; Genomic_DNA.
DR EMBL; CU329670; CAB95998.1; -; Genomic_DNA.
DR PIR; T46564; T46564.
DR RefSeq; NP_594205.1; NM_001019628.2.
DR AlphaFoldDB; P40387; -.
DR SMR; P40387; -.
DR BioGRID; 279113; 97.
DR ComplexPortal; CPX-6423; Trehalose-6-phosphate synthase/phosphatase complex.
DR IntAct; P40387; 2.
DR STRING; 4896.SPAC328.03.1; -.
DR CAZy; GT20; Glycosyltransferase Family 20.
DR iPTMnet; P40387; -.
DR MaxQB; P40387; -.
DR PaxDb; P40387; -.
DR PRIDE; P40387; -.
DR EnsemblFungi; SPAC328.03.1; SPAC328.03.1:pep; SPAC328.03.
DR GeneID; 2542660; -.
DR KEGG; spo:SPAC328.03; -.
DR PomBase; SPAC328.03; tps1.
DR VEuPathDB; FungiDB:SPAC328.03; -.
DR eggNOG; KOG1050; Eukaryota.
DR HOGENOM; CLU_002351_7_2_1; -.
DR InParanoid; P40387; -.
DR OMA; YYGFSNR; -.
DR PhylomeDB; P40387; -.
DR PRO; PR:P40387; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005946; C:alpha,alpha-trehalose-phosphate synthase complex (UDP-forming); IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003825; F:alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity; IMP:PomBase.
DR GO; GO:0030437; P:ascospore formation; IMP:PomBase.
DR GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
DR GO; GO:0005992; P:trehalose biosynthetic process; IMP:PomBase.
DR GO; GO:0005993; P:trehalose catabolic process; IDA:ComplexPortal.
DR GO; GO:0070413; P:trehalose metabolism in response to stress; IMP:PomBase.
DR CDD; cd03788; GT20_TPS; 1.
DR InterPro; IPR001830; Glyco_trans_20.
DR InterPro; IPR012766; Trehalose_OtsA.
DR PANTHER; PTHR10788; PTHR10788; 1.
DR Pfam; PF00982; Glyco_transf_20; 1.
DR TIGRFAMs; TIGR02400; trehalose_OtsA; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Glycosyltransferase; Nucleus; Phosphoprotein;
KW Reference proteome; Stress response; Transferase.
FT CHAIN 1..513
FT /note="Alpha,alpha-trehalose-phosphate synthase [UDP-
FT forming]"
FT /id="PRO_0000122500"
FT BINDING 104
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 158
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 294
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 294
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 299
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 299
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 332
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 393..401
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 397..401
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT MOD_RES 40
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 503
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 277
FT /note="A -> R (in Ref. 1; CAA82861)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 513 AA; 58493 MW; 9FC247B626CE2B00 CRC64;
MSDAHDTIKS LTGDASNSRR LIVVSNRLPI TIKRKDNGTY DFSMSSGGLV SALSGLKKLM
TFQWLGWCGQ EIPEDEKPMI IQRLQDECSA IPVFLDDETA DRHYNGFSNS ILWPLFHYHP
GEINFDEENW EAYRAANYAF AEAIVKNLQD GDLIWVQDYH LMVLPQMLRE LIGDKFKDIK
IGFFLHTPFP SSEIYRVLPV RNEILEGVLN CDLVGFHTYD YARHFLSACS RILNLSTLPN
GVEYNGQMVS VGTFPIGIDP EKFSDALKSD VVKDRIASIE RRLQGVKVIV GVDRLDYIKG
VPQKFHAFEV FLEQYPEWVG KVVLVQVAVP SRQDVEEYQN LRAVVNELVG RINGRFGTVE
YTPIHFLHKS VRFEELVALY NVSDVCLITS TRDGMNLVSY EYICTQQERH GALILSEFAG
AAQSLNGSIV INPWNTEELA NSIHDALTMP EKQREANENK LFRYVNKYTS QFWGQSFVGE
LQRIQHYSHP HPRRTNPILR TKSAQVLSMN SSS
