TPP1_SCHPO
ID TPP1_SCHPO Reviewed; 817 AA.
AC P78875; Q8TGH5;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Trehalose-phosphatase;
DE EC=3.1.3.12 {ECO:0000305|PubMed:11004189};
DE AltName: Full=Trehalose-6-phosphate phosphatase;
DE Short=TPP;
GN Name=tpp1 {ECO:0000303|PubMed:11004189};
GN ORFNames=SPAC19G12.15c {ECO:0000312|PomBase:SPAC19G12.15c};
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, CATALYTIC ACTIVITY, INDUCTION,
RP AND DISRUPTION PHENOTYPE.
RC STRAIN=972 / ATCC 24843;
RX PubMed=11004189; DOI=10.1128/jb.182.20.5880-5884.2000;
RA Franco A., Soto T., Vicente-Soler J., Guillen P.V., Cansado J., Gacto M.;
RT "Characterization of tpp1(+) as encoding a main trehalose-6P phosphatase in
RT the fission yeast Schizosaccharomyces pombe.";
RL J. Bacteriol. 182:5880-5884(2000).
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 NUCLEOTIDE SEQUENCE [MRNA] OF 124-817.
RC STRAIN=972 / ATCC 24843;
RA Young-Joo J., Chan-Kyu P., Hyang-Sook Y.;
RT "Cloning and characterization of trehalose-6-phosphate phosphatase gene in
RT Schizosaccharomyces pombe.";
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 505-817.
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [5]
RP IDENTIFICATION IN THE TREHALOSE SYNTHASE COMPLEX, AND INTERACTION WITH NTP1
RP AND TPS1.
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).
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 (PubMed:11004189). The disaccharide trehalose serves as a storage
CC carbohydrate that is mobilized during nutrient stress and spore
CC germination (Probable). Together with ntp1, regulates the level of
CC trehalose as a protectant for cell integrity during thermal, osmotic,
CC and oxidative stress (Probable). {ECO:0000269|PubMed:11004189,
CC ECO:0000305|PubMed:11004189}.
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:0000305|PubMed:11004189};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P31688};
CC -!- PATHWAY: Carbohydrate biosynthesis. {ECO:0000305}.
CC -!- SUBUNIT: Component of the trehalose synthase complex that contains at
CC least tps1, ntp1, and tpp1 (Probable). Interacts with tps1
CC (PubMed:12153582). Interacts with ntp1 (PubMed:12153582).
CC {ECO:0000269|PubMed:12153582, ECO:0000305|PubMed:12153582}.
CC -!- INTERACTION:
CC P78875; O42893: ntp1; NbExp=2; IntAct=EBI-26616958, EBI-26616855;
CC P78875; P40387: tps1; NbExp=2; IntAct=EBI-26616958, EBI-26616873;
CC -!- INDUCTION: Induced by thermal stress, and osmotic stress (at protein
CC level) (PubMed:11004189). Induced by oxidative stress
CC (PubMed:11004189). {ECO:0000269|PubMed:11004189}.
CC -!- DISRUPTION PHENOTYPE: Increases cellular trehalose-6-phosphate level
CC during thermal stress. {ECO:0000269|PubMed:11004189}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL77573.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ242743; CAB45142.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB10126.1; -; Genomic_DNA.
DR EMBL; L40359; AAL77573.1; ALT_FRAME; mRNA.
DR EMBL; D89225; BAA13886.1; -; mRNA.
DR PIR; T43659; T43659.
DR RefSeq; NP_594430.1; NM_001019859.2.
DR AlphaFoldDB; P78875; -.
DR SMR; P78875; -.
DR BioGRID; 279033; 75.
DR ComplexPortal; CPX-6423; Trehalose-6-phosphate synthase/phosphatase complex.
DR IntAct; P78875; 2.
DR STRING; 4896.SPAC19G12.15c.1; -.
DR CAZy; GT20; Glycosyltransferase Family 20.
DR MaxQB; P78875; -.
DR PaxDb; P78875; -.
DR EnsemblFungi; SPAC19G12.15c.1; SPAC19G12.15c.1:pep; SPAC19G12.15c.
DR GeneID; 2542577; -.
DR KEGG; spo:SPAC19G12.15c; -.
DR PomBase; SPAC19G12.15c; tpp1.
DR VEuPathDB; FungiDB:SPAC19G12.15c; -.
DR eggNOG; KOG1050; Eukaryota.
DR HOGENOM; CLU_002351_3_0_1; -.
DR InParanoid; P78875; -.
DR OMA; DSVCRDG; -.
DR PhylomeDB; P78875; -.
DR PRO; PR:P78875; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005946; C:alpha,alpha-trehalose-phosphate synthase complex (UDP-forming); IDA:PomBase.
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: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; IBA:GO_Central.
DR GO; GO:0005993; P:trehalose catabolic process; IDA:ComplexPortal.
DR GO; GO:0005991; P:trehalose metabolic process; IMP: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; 2.
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 Hydrolase; Reference proteome.
FT CHAIN 1..817
FT /note="Trehalose-phosphatase"
FT /id="PRO_0000122508"
FT REGION 1..547
FT /note="Glycosyltransferase"
FT CONFLICT 124..135
FT /note="QWNSGERSTEYV -> GTRNGVRSR (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 279
FT /note="R -> S (in Ref. 3; AAL77573)"
FT /evidence="ECO:0000305"
FT CONFLICT 494
FT /note="E -> G (in Ref. 3; AAL77573)"
FT /evidence="ECO:0000305"
FT CONFLICT 498
FT /note="N -> Y (in Ref. 3; AAL77573)"
FT /evidence="ECO:0000305"
FT CONFLICT 513
FT /note="E -> A (in Ref. 3; AAL77573)"
FT /evidence="ECO:0000305"
FT CONFLICT 536
FT /note="N -> Y (in Ref. 3; AAL77573)"
FT /evidence="ECO:0000305"
FT CONFLICT 693..696
FT /note="ENGA -> REWS (in Ref. 3; AAL77573)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 817 AA; 93878 MW; 23CFD2533505CCBA CRC64;
MSVYGKIPST SFEHENTFEL SGDLLDPEEL KSLGVSGRII YVLRHLPFKS SINEETREWD
LSGRRGATTM YSSMNWLANS TYWQTTLVGW TGVIPTVSEK EENKDAVTRL DSQDVKRFEE
TYSQWNSGER STEYVPVWLP GPEKGSETII NETRSQQSRW LAYAENVIRP LIHYKYWPSS
EVDENEEQWW RDYVKMNHAF ADKICEIYKP GDFIIVQDYS LFLVPQLIRN KIDDAVIGFY
HHHPFPSSEI ARCFPRRRAI LRSVLGADFI GFEDYSYARH FISCCSRVLD LEIGHDWVNL
NGNKVTVRAI TVGIDVPRII RSSGNVSVSE KLEELNKRYE NMKVILGRDR LDELYGVPQK
LRSFQRFLRT YPEWRKKVVL IQITISSAFK HPKLLSSIKK LVQAINQEFG TDDYTPVHHV
EEQLEPADYF ALLTRADALF INSIREGVSN LALEYVVCQR DRYGMVLLSE FTATSAMLHD
VPLINPWDYN ECAEIISNAL STPLERRKMI ERESYKQVTT HTMQSWTSSL IRSLANKLAA
TKTDQRIPTL TPEHALSVYS KASKRLFMMD YDGTLTPIVR DPNAAVPSKK LLDNLATLAA
DPKNQVWIIS GRDQQFLRNW MDDIKGLGLS AEHGSFVRKP HSTTWINLAE LLDMSWKKEV
RRIFQYYTDR TQGSSIEEKR CAMTWHYRKA DPENGAFQAL ECEALLEELV CSKYDVEIMR
GKANLEVRPS SINKGGIVKQ ILSSYPEDSL PSFIFCAGDD RTDEDMFRSL HKNTRINKET
SFAVTIGSDK KLSIADWCIA DPANVIDILA DLANFTN
