Entry sw:TPSY_SCHPO

ID   TPSY_SCHPO              Reviewed;         891 AA.
AC   Q9UUI7;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   30-NOV-2016, entry version 97.
DE   RecName: Full=Putative alpha,alpha-trehalose-phosphate synthase [UDP-forming] 100 kDa subunit;
DE            EC=2.4.1.15;
DE   AltName: Full=Trehalose-6-phosphate synthase;
DE   AltName: Full=UDP-glucose-glucosephosphate glucosyltransferase;
GN   ORFNames=SPAC22F8.05;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; 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.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-88; SER-108 AND SER-109,
RP   AND 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   -!- CATALYTIC ACTIVITY: UDP-glucose + D-glucose 6-phosphate = UDP +
CC       alpha,alpha-trehalose 6-phosphate.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the
CC       glycosyltransferase 20 family. {ECO:0000305}.
DR   EMBL; CU329670; CAB52715.1; -; Genomic_DNA.
DR   PIR; T38195; T38195.
DR   RefSeq; NP_594728.1; NM_001020156.2.
DR   ProteinModelPortal; Q9UUI7; -.
DR   BioGrid; 278393; 28.
DR   MINT; MINT-4714293; -.
DR   CAZy; GT20; Glycosyltransferase Family 20.
DR   iPTMnet; Q9UUI7; -.
DR   MaxQB; Q9UUI7; -.
DR   PRIDE; Q9UUI7; -.
DR   EnsemblFungi; SPAC22F8.05.1; SPAC22F8.05.1:pep; SPAC22F8.05.
DR   GeneID; 2541903; -.
DR   KEGG; spo:SPAC22F8.05; -.
DR   EuPathDB; FungiDB:SPAC22F8.05; -.
DR   PomBase; SPAC22F8.05; -.
DR   HOGENOM; HOG000179930; -.
DR   InParanoid; Q9UUI7; -.
DR   KO; K16055; -.
DR   OrthoDB; EOG092C0LDC; -.
DR   PhylomeDB; Q9UUI7; -.
DR   PRO; PR:Q9UUI7; -.
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; IDA:PomBase.
DR   GO; GO:0003825; F:alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity; ISO:PomBase.
DR   GO; GO:0016311; P:dephosphorylation; IEA:GOC.
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; GT1_TPS; 1.
DR   Gene3D; 3.40.50.1000; -; 2.
DR   InterPro; IPR001830; Glyco_trans_20.
DR   InterPro; IPR023214; HAD-like_dom.
DR   InterPro; IPR003337; Trehalose_PPase.
DR   Pfam; PF00982; Glyco_transf_20; 1.
DR   Pfam; PF02358; Trehalose_PPase; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Glycosyltransferase; Phosphoprotein;
KW   Reference proteome; Transferase.
FT   CHAIN         1    891       Putative alpha,alpha-trehalose-phosphate
FT                                synthase [UDP-forming] 100 kDa subunit.
FT                                /FTId=PRO_0000122513.
FT   REGION      132    613       Glycosyltransferase.
FT   MOD_RES      88     88       Phosphothreonine.
FT                                {ECO:0000269|PubMed:18257517}.
FT   MOD_RES     108    108       Phosphoserine.
FT                                {ECO:0000269|PubMed:18257517}.
FT   MOD_RES     109    109       Phosphoserine.
FT                                {ECO:0000269|PubMed:18257517}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT       669    866       ipfam:Trehalose_PPase [T]
FT   MYHIT       173    612       ipfam:Glyco_transf_20 [T]
SQ   SEQUENCE   891 AA;  100661 MW;  7F74688CCBFC45B9 CRC64;
     MGRQFICSIY LPYTINFHLD ELEGNHESHP AITHQEKVTQ THRDSVKIDD ILTRLSISKS
     ESGQATPVLT PQLEGMNDYF SLGPSKRTGG SMTPGLGAMS PIPGSGRSSP LYTQPRSRAT
     SPSRVRQADR FAAPGIGAGA LPIRRKRRDS LAKSVALFES ARWSVERGVV GNSGLFHAVD
     AAVRDHGLQN PLWVGLLGMP TESLSEKTKN AISGALLVKH QSLVVYTSDS NFEGHYNHYC
     RKILWPSLHY QHNEIFSFFH EESNWDDYVA VNRAFADALI KNYKTGDTIW VNDYHLLLVP
     NMVRERIPSA IIGLFIHVSF PSSEVFRCFA RRKELLQGML GSNLIGFQTE EYKRHFLQSC
     SRVLYAESTF DRILLDDRYI DVYAHPIGAD PVLVDKWLEN PETLEVKEVL EKRYANLNIF
     VGCDKMDPIR GIREKLLAFE QFLYDNPEYQ KNTILIQTST FTEEQKEYGV AISDIVTRIN
     SAFGDFSLDH LPVTILSSDL SYPQYLALLS VADAFIVTSL REGMSLTCHE FILTQRQKKS
     PLIVSEFIGC ASMFSNGAFI VNPWSTLELS LSMKKALTLS TNERNQRYSN CLDVVLTHSA
     SNWVTGFETK LKKSWTSQQK RDFSRLPRFT LNFIGNRYDH AKKRLLILNF DGNAVTWEGR
     HEFVDFHYGY MVSILSKLIA DDRNIVYIAS CLEEDELESL FMHVPGVGLI AENGCYVLPH
     YAENVHQSWI RLYKKQQMDW REPLHDIIQY YSERTPGSSL IDHGFAMEFN YVKAENRENG
     LRSAGELASS INETQHGCRA VPLDGRVLCE PTTISKATAA NYIMTHLIKN PEELDLILVA
     GNNRTDESVF AWANKSKVSS FTVSMGVGNT EAKAYTDGIP SFFNVLNSLC A
//