TPS2_YEAST
ID TPS2_YEAST Reviewed; 896 AA.
AC P31688; D6VS60;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 3.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Trehalose-phosphatase;
DE EC=3.1.3.12 {ECO:0000269|PubMed:2546763};
DE AltName: Full=Trehalose synthase complex catalytic subunit TPS2;
DE AltName: Full=Trehalose-6-phosphate phosphatase;
DE Short=TPP;
GN Name=TPS2 {ECO:0000303|PubMed:8444170}; Synonyms=PFK3;
GN OrderedLocusNames=YDR074W; ORFNames=YD8554.07;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=C13-ABYS86;
RX PubMed=8444170; DOI=10.1111/j.1432-1033.1993.tb17664.x;
RA de Virgilio C., Buerckert N., Bell W., Jenoe P., Boller T., Wiemken A.;
RT "Disruption of TPS2, the gene encoding the 100-kDa subunit of the
RT trehalose-6-phosphate synthase/phosphatase complex in Saccharomyces
RT cerevisiae, causes accumulation of trehalose-6-phosphate and loss of
RT trehalose-6-phosphate phosphatase activity.";
RL Eur. J. Biochem. 212:315-323(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 608-896.
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=1656215; DOI=10.1128/mcb.11.10.4876-4884.1991;
RA Ronne H., Carlberg M., Hu G.-Z., Nehlin J.O.;
RT "Protein phosphatase 2A in Saccharomyces cerevisiae: effects on cell growth
RT and bud morphogenesis.";
RL Mol. Cell. Biol. 11:4876-4884(1991).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=2546763; DOI=10.1111/j.1432-1033.1989.tb14870.x;
RA Vandercammen A., Francois J., Hers H.-G.;
RT "Characterization of trehalose-6-phosphate synthase and trehalose-6-
RT phosphate phosphatase of Saccharomyces cerevisiae.";
RL Eur. J. Biochem. 182:613-620(1989).
RN [6]
RP FUNCTION, AND INTERACTION WITH TPS1; TPS3 AND TSL1.
RX PubMed=9194697; DOI=10.1046/j.1365-2958.1997.3861749.x;
RA Reinders A., Buerckert N., Hohmann S., Thevelein J.M., Boller T.,
RA Wiemken A., De Virgilio C.;
RT "Structural analysis of the subunits of the trehalose-6-phosphate
RT synthase/phosphatase complex in Saccharomyces cerevisiae and their function
RT during heat shock.";
RL Mol. Microbiol. 24:687-695(1997).
RN [7]
RP SUBUNIT.
RX PubMed=9837904; DOI=10.1074/jbc.273.50.33311;
RA Bell W., Sun W., Hohmann S., Wera S., Reinders A., De Virgilio C.,
RA Wiemken A., Thevelein J.M.;
RT "Composition and functional analysis of the Saccharomyces cerevisiae
RT trehalose synthase complex.";
RL J. Biol. Chem. 273:33311-33319(1998).
RN [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [9]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Phosphatase catalytic subunit of the trehalose synthase
CC complex that catalyzes the production of trehalose from glucose-6-
CC phosphate and UDP-alpha-D-glucose in a two step process.
CC {ECO:0000269|PubMed:2546763, ECO:0000269|PubMed:9194697}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha,alpha-trehalose 6-phosphate + H2O = alpha,alpha-
CC trehalose + phosphate; Xref=Rhea:RHEA:23420, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16551, ChEBI:CHEBI:43474, ChEBI:CHEBI:58429; EC=3.1.3.12;
CC Evidence={ECO:0000269|PubMed:2546763};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000305|PubMed:2546763};
CC -!- ACTIVITY REGULATION: Inhibited by EDTA. {ECO:0000305|PubMed:2546763}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.2 mM for trehalose 6-phosphate (at pH 6.0)
CC {ECO:0000269|PubMed:2546763};
CC KM=0.5 mM for trehalose 6-phosphate (at pH 7.5)
CC {ECO:0000269|PubMed:2546763};
CC Vmax=20 nmol/min/mg enzyme (at pH 6.0) {ECO:0000269|PubMed:2546763};
CC Vmax=10 nmol/min/mg enzyme (at pH 7.5) {ECO:0000269|PubMed:2546763};
CC pH dependence:
CC Optimum pH is 6.0. {ECO:0000269|PubMed:2546763};
CC -!- PATHWAY: Carbohydrate biosynthesis. {ECO:0000305}.
CC -!- SUBUNIT: The trehalose synthase complex is composed of the two
CC catalytic subunits TPS1 and TPS2, and at least one of the two
CC regulatory subunits TPS3 or TSL1. {ECO:0000269|PubMed:9837904}.
CC -!- INTERACTION:
CC P31688; Q00764: TPS1; NbExp=7; IntAct=EBI-19440, EBI-19430;
CC P31688; P38426: TPS3; NbExp=7; IntAct=EBI-19440, EBI-19448;
CC P31688; P38427: TSL1; NbExp=3; IntAct=EBI-19440, EBI-19638;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- INDUCTION: By heat shock. Repressed by glucose.
CC -!- MISCELLANEOUS: Present with 22700 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the
CC glycosyltransferase 20 family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the trehalose
CC phosphatase family. {ECO:0000305}.
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DR EMBL; X70694; CAA50025.1; -; Genomic_DNA.
DR EMBL; Z46796; CAA86796.1; -; Genomic_DNA.
DR EMBL; Z74370; CAA98893.1; -; Genomic_DNA.
DR EMBL; X58858; CAA41661.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11920.1; -; Genomic_DNA.
DR PIR; S48761; S48761.
DR RefSeq; NP_010359.1; NM_001180382.1.
DR AlphaFoldDB; P31688; -.
DR SMR; P31688; -.
DR BioGRID; 32129; 601.
DR ComplexPortal; CPX-582; Trehalose-6-phosphate synthase/phosphatase complex, tps3 variant.
DR ComplexPortal; CPX-583; Trehalose-6-phosphate synthase/phosphatase complex, tsl1 variant.
DR DIP; DIP-823N; -.
DR IntAct; P31688; 10.
DR MINT; P31688; -.
DR STRING; 4932.YDR074W; -.
DR CAZy; GT20; Glycosyltransferase Family 20.
DR iPTMnet; P31688; -.
DR MaxQB; P31688; -.
DR PaxDb; P31688; -.
DR PRIDE; P31688; -.
DR EnsemblFungi; YDR074W_mRNA; YDR074W; YDR074W.
DR GeneID; 851646; -.
DR KEGG; sce:YDR074W; -.
DR SGD; S000002481; TPS2.
DR VEuPathDB; FungiDB:YDR074W; -.
DR eggNOG; KOG1050; Eukaryota.
DR GeneTree; ENSGT00940000167933; -.
DR HOGENOM; CLU_002351_3_0_1; -.
DR InParanoid; P31688; -.
DR OMA; HINPWDM; -.
DR BioCyc; MetaCyc:YDR074W-MON; -.
DR BioCyc; YEAST:YDR074W-MON; -.
DR BRENDA; 2.4.1.15; 984.
DR BRENDA; 3.1.3.12; 984.
DR SABIO-RK; P31688; -.
DR PRO; PR:P31688; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P31688; protein.
DR GO; GO:0005946; C:alpha,alpha-trehalose-phosphate synthase complex (UDP-forming); IPI:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0003825; F:alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity; IBA:GO_Central.
DR GO; GO:0004805; F:trehalose-phosphatase activity; IMP:SGD.
DR GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
DR GO; GO:0031505; P:fungal-type cell wall organization; IBA:GO_Central.
DR GO; GO:0010508; P:positive regulation of autophagy; IMP:SGD.
DR GO; GO:0005992; P:trehalose biosynthetic process; IMP:SGD.
DR GO; GO:0070413; P:trehalose metabolism in response to stress; IMP:SGD.
DR CDD; cd03788; GT20_TPS; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR001830; Glyco_trans_20.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006379; HAD-SF_hydro_IIB.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR003337; Trehalose_PPase.
DR PANTHER; PTHR10788; PTHR10788; 1.
DR Pfam; PF00982; Glyco_transf_20; 1.
DR Pfam; PF02358; Trehalose_PPase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01484; HAD-SF-IIB; 1.
DR TIGRFAMs; TIGR00685; T6PP; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Hydrolase; Reference proteome;
KW Stress response.
FT CHAIN 1..896
FT /note="Trehalose-phosphatase"
FT /id="PRO_0000122509"
FT REGION 1..554
FT /note="Glycosyltransferase"
FT CONFLICT 48
FT /note="F -> Y (in Ref. 1; CAA50025)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="N -> D (in Ref. 1; CAA50025)"
FT /evidence="ECO:0000305"
FT CONFLICT 542
FT /note="Q -> K (in Ref. 1; CAA50025)"
FT /evidence="ECO:0000305"
FT CONFLICT 546
FT /note="N -> D (in Ref. 1; CAA50025)"
FT /evidence="ECO:0000305"
FT CONFLICT 549
FT /note="M -> V (in Ref. 1; CAA50025)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 896 AA; 102976 MW; E349672CCCDA9349 CRC64;
MTTTAQDNSP KKRQRIINCV TQLPYKIQLG ESNDDWKISA TTGNSALFSS LEYLQFDSTE
YEQHVVGWTG EITRTERNLF TREAKEKPQD LDDDPLYLTK EQINGLTTTL QDHMKSDKEA
KTDTTQTAPV TNNVHPVWLL RKNQSRWRNY AEKVIWPTFH YILNPSNEGE QEKNWWYDYV
KFNEAYAQKI GEVYRKGDII WIHDYYLLLL PQLLRMKFND ESIIIGYFHH APWPSNEYFR
CLPRRKQILD GLVGANRICF QNESFSRHFV SSCKRLLDAT AKKSKNSSNS DQYQVSVYGG
DVLVDSLPIG VNTTQILKDA FTKDIDSKVL SIKQAYQNKK IIIGRDRLDS VRGVVQKLRA
FETFLAMYPE WRDQVVLIQV SSPTANRNSP QTIRLEQQVN ELVNSINSEY GNLNFSPVQH
YYMRIPKDVY LSLLRVADLC LITSVRDGMN TTALEYVTVK SHMSNFLCYG NPLILSEFSG
SSNVLKDAIV VNPWDSVAVA KSINMALKLD KEEKSNLESK LWKEVPTIQD WTNKFLSSLK
EQASSNDDME RKMTPALNRP VLLENYKQAK RRLFLFDYDG TLTPIVKDPA AAIPSARLYT
ILQKLCADPH NQIWIISGRD QKFLNKWLGG KLPQLGLSAE HGCFMKDVSC QDWVNLTEKV
DMSWQVRVNE VMEEFTTRTP GSFIERKKVA LTWHYRRTVP ELGEFHAKEL KEKLLSFTDD
FDLEVMDGKA NIEVRPRFVN KGEIVKRLVW HQHGKPQDML KGISEKLPKD EMPDFVLCLG
DDFTDEDMFR QLNTIETCWK EKYPDQKNQW GNYGFYPVTV GSASKKTVAK AHLTDPQQVL
ETLGLLVGDV SLFQSAGTVD LDSRGHVKNS ESSLKSKLAS KAYVMKRSAS YTGAKV
