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 03-AUG-2022, entry version 125.
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; 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 THR-88; SER-108 AND SER-109, AND
RP 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:
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; CAB52715.1; -; Genomic_DNA.
DR PIR; T38195; T38195.
DR RefSeq; NP_594728.1; NM_001020156.2.
DR AlphaFoldDB; Q9UUI7; -.
DR SMR; Q9UUI7; -.
DR BioGRID; 278393; 29.
DR STRING; 4896.SPAC22F8.05.1; -.
DR CAZy; GT20; Glycosyltransferase Family 20.
DR iPTMnet; Q9UUI7; -.
DR MaxQB; Q9UUI7; -.
DR PaxDb; Q9UUI7; -.
DR PRIDE; Q9UUI7; -.
DR EnsemblFungi; SPAC22F8.05.1; SPAC22F8.05.1:pep; SPAC22F8.05.
DR GeneID; 2541903; -.
DR KEGG; spo:SPAC22F8.05; -.
DR PomBase; SPAC22F8.05; -.
DR VEuPathDB; FungiDB:SPAC22F8.05; -.
DR eggNOG; KOG1050; Eukaryota.
DR HOGENOM; CLU_002351_2_1_1; -.
DR InParanoid; Q9UUI7; -.
DR OMA; NWKRDDV; -.
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; 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..891
FT /note="Putative alpha,alpha-trehalose-phosphate synthase
FT [UDP-forming] 100 kDa subunit"
FT /id="PRO_0000122513"
FT REGION 88..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 132..613
FT /note="Glycosyltransferase"
FT COMPBIAS 106..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 88
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
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
