TPSX_SCHPO
ID TPSX_SCHPO Reviewed; 944 AA.
AC O14081;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Putative alpha,alpha-trehalose-phosphate synthase [UDP-forming] 106 kDa subunit;
DE EC=2.4.1.15;
DE AltName: Full=Trehalose-6-phosphate synthase;
DE AltName: Full=UDP-glucose-glucosephosphate glucosyltransferase;
GN ORFNames=SPAC2E11.16c, SPACUNK4.16c;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141; SER-145; SER-149;
RP SER-150; SER-163; SER-177 AND THR-189, AND IDENTIFICATION BY MASS
RP 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:
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 -!- SIMILARITY: In the N-terminal section; belongs to the
CC glycosyltransferase 20 family. {ECO:0000305}.
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DR EMBL; CU329670; CAA20146.1; -; Genomic_DNA.
DR PIR; T41711; T41711.
DR RefSeq; NP_593962.1; NM_001019389.2.
DR AlphaFoldDB; O14081; -.
DR SMR; O14081; -.
DR BioGRID; 278957; 19.
DR STRING; 4896.SPACUNK4.16c.1; -.
DR CAZy; GT20; Glycosyltransferase Family 20.
DR iPTMnet; O14081; -.
DR SwissPalm; O14081; -.
DR MaxQB; O14081; -.
DR PaxDb; O14081; -.
DR PRIDE; O14081; -.
DR EnsemblFungi; SPACUNK4.16c.1; SPACUNK4.16c.1:pep; SPACUNK4.16c.
DR GeneID; 2542498; -.
DR KEGG; spo:SPACUNK4.16c; -.
DR PomBase; SPACUNK4.16c; -.
DR VEuPathDB; FungiDB:SPACUNK4.16c; -.
DR eggNOG; KOG1050; Eukaryota.
DR HOGENOM; CLU_002351_2_2_1; -.
DR InParanoid; O14081; -.
DR OMA; REASIVW; -.
DR PhylomeDB; O14081; -.
DR PRO; PR:O14081; -.
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:0003825; F:alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity; ISO:PomBase.
DR GO; GO:0004805; F:trehalose-phosphatase activity; IEA:UniProt.
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; 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.
PE 1: Evidence at protein level;
KW Glycosyltransferase; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..944
FT /note="Putative alpha,alpha-trehalose-phosphate synthase
FT [UDP-forming] 106 kDa subunit"
FT /id="PRO_0000122512"
FT REGION 73..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..652
FT /note="Glycosyltransferase"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 150
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 189
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 944 AA; 106818 MW; D9B48874CCCB1A8A CRC64;
MGRILIAHLF LPSSVGFSFD TVPHDEVGSK FMQKEESKDW IADTPLDESA IVSEEESDDD
SLLSDLPEEI DSTNAQSNIA TPSPGTVAAA ISGIQPPPKT PSSDSPSLEN SLSNLNDLFK
SRGRHMAFSK NDGTNLSLPP SRHQSPPPSS VLASQRHHRR HDSELEEFAR RASRSLSFSM
NGTPQRRMTF DAEAWKNVIF KIKPSSFGNA SFYNAISAAT RSKQFDDHLF VGTCGIPTDS
LPDSLKERIS HDYITEHSSL VVYPTDTDFV GHYNHYCKNI LWPTFHYQIP DNPKSKAYED
HSWANYVKVN KAFADTIVDN YEQDDMIWIN DYHLLLVPEM VRERLPRAKI GFFLHIPFPS
SEVFRCLATR QEILKGMLGA NILGFQIPEF AYHFLQTCSR LVNIDIRKNG VVSFENRQID
VIALPISIDP GFIDRCLASP PVEHWAKVLQ DRFRGKHIIL SHDKLDPIRG LRSKLISFER
FLQKYPEYRE NTILLQVAPE SLQDSEHLPH ISDIVTRINS AYSNIASRHV PVILLRQKLG
YAQFLALMMI SDALIDNSLR EGISLTSHQF IYVQRKRHRP LILSEFVGSA SILNDNAIIV
NPWDYSKTAE AFRTALTMSE EECQKRNKAM CNLILRHDAA SWAVTFQSLI KESWKEQIDM
QRIPAFTAQL IKEPYQNAQK RLILLYFEGT ISTWGSQYHN VMTSLQRTIN LLNMLTSDPK
NTVYVFSALS CQELEQLFQR VPKLGIVAEN GCFVRSPPKG DATMPVSKKE IAELWKNKVL
GTDLTWMKTV SEIFEYYAER TTGAYVENKD ATVILHLREA EDDEAAMWAA KECCESVNNF
NVPCSATIQN DMVVCRSNKV SKRLAAEDIY SANGGDYDFI FAASNDPDDD TVFSWMKNFK
QSKKEVVPFT FSVCVSEHGN STNADAESSG VFGFLQALEK VYSA
