TPS2_SCHPO
ID TPS2_SCHPO Reviewed; 849 AA.
AC O14145;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Trehalose-phosphatase;
DE EC=3.1.3.12 {ECO:0000250|UniProtKB:P31688};
DE AltName: Full=Trehalose synthase complex catalytic subunit tps2;
DE AltName: Full=Trehalose-6-phosphate phosphatase;
DE Short=TPP;
GN Name=tps2; ORFNames=SPAC3G6.09c;
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 [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 [2]
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).
CC -!- FUNCTION: Phosphatase catalytic subunit of the trehalose synthase
CC complex that catalyzes the production of trehalose from glucose-6-
CC phosphate and UDP-glucose in a two step process.
CC {ECO:0000250|UniProtKB:P31688}.
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:0000250|UniProtKB:P31688};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P31688};
CC -!- PATHWAY: Carbohydrate biosynthesis. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
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; CU329670; CAB16285.1; -; Genomic_DNA.
DR PIR; T38728; T38728.
DR RefSeq; NP_594975.1; NM_001020406.2.
DR AlphaFoldDB; O14145; -.
DR SMR; O14145; -.
DR BioGRID; 279541; 24.
DR STRING; 4896.SPAC3G6.09c.1; -.
DR CAZy; GT20; Glycosyltransferase Family 20.
DR iPTMnet; O14145; -.
DR MaxQB; O14145; -.
DR PaxDb; O14145; -.
DR PRIDE; O14145; -.
DR EnsemblFungi; SPAC3G6.09c.1; SPAC3G6.09c.1:pep; SPAC3G6.09c.
DR GeneID; 2543109; -.
DR KEGG; spo:SPAC3G6.09c; -.
DR PomBase; SPAC3G6.09c; tps2.
DR VEuPathDB; FungiDB:SPAC3G6.09c; -.
DR eggNOG; KOG1050; Eukaryota.
DR HOGENOM; CLU_002351_3_0_1; -.
DR InParanoid; O14145; -.
DR OMA; RMAYYSI; -.
DR PhylomeDB; O14145; -.
DR PRO; PR:O14145; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005946; C:alpha,alpha-trehalose-phosphate synthase complex (UDP-forming); ISO:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0003825; F:alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004805; F:trehalose-phosphatase activity; ISO:PomBase.
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:0005992; P:trehalose biosynthetic process; ISO:PomBase.
DR GO; GO:0070413; P:trehalose metabolism in response to stress; IBA:GO_Central.
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 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Magnesium; Metal-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..849
FT /note="Trehalose-phosphatase"
FT /id="PRO_0000316232"
FT REGION 1..558
FT /note="Glycosyltransferase"
FT /evidence="ECO:0000250"
SQ SEQUENCE 849 AA; 96341 MW; 6C7F74E43A6EBDFD CRC64;
MPSGAQGNTQ SAAYKRIVNV SRNFQFKAAL NKDTREWTFQ HRSSGTALYS AIASLGDPSS
PWDAVYVASP GPVQISEGND HTVETKIDEA AVVHRSSSIV ISPEDQEIFL KKATEYYRKK
NIEADIVPVW GKVQRVPQAK SSSATITPSV SNKLSTAYQS IKSEALKDGP MYADSVLWDV
LHYRIPTLDG YQQHNLWKNF TRWSQYFADN IVSNYRPGDL ILIHDYSLFL LPRLIRKQLS
DAPIVFFLHA PFCTSEVFRC LSKRAEILKG VLASNVIAMQ TDSYTRHFLS TCSNVLGLET
TSTHIDTSDG FRVVVFSSHV SIDVPRVYSR CNSKPVSLKI QQLKSLYPSD KKLIVGRDQL
TKACGVTHKL RAFRELLIHF PKWRGHVVLI QITSLPVGNN YSNEELKKTE NLVAQINSEF
GSLDYTPVIH FHQLLDPDEY YALLSVANIA CVSSVRDSMN TMALEYVACQ QKNKGSLILS
EFSGTAELLL SAYLVNPYDY SRFAETINYC LNMTEKERER RFSSLWKQAT SQSSQQWIYK
LINRAAYEVK ALESHMTTPL LTYNILIKPY RNAKRRLFLL DYDGTLIESA RNSIDAVPTD
RLLRTLKRLA SDSRNIVWIL SGRSQKFMEE WMGDISELGL SSEHGSAIRP PLAGSWSSCA
ENLDLSWKDT VRDFFQYYVE RTPGSYIEEK KHSISWCYQN ANTTYSKFQS LECQTNLEDM
LKHYDVEISP AKSFLEVHPN YLNKGSIVRR ILKRSGSVDF VFCAGDDKTD ENMFEVFLPT
AFSNSHLIDE IDSTEYSGSH HTDDNSDANK VENVKVATFR VHIGLTDKPT LSDYHLPAPR
DLGELLHNL
