ID   TPS1_ZYGRO              Reviewed;         485 AA.
AC   Q96WK6;
DT   06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   24-JAN-2024, entry version 61.
DE   RecName: Full=Alpha,alpha-trehalose-phosphate synthase [UDP-forming];
DE            EC=2.4.1.15 {ECO:0000305|PubMed:12748054};
DE   AltName: Full=Trehalose-6-phosphate synthase;
DE   AltName: Full=UDP-glucose-glucosephosphate glucosyltransferase;
GN   Name=TPS1 {ECO:0000303|PubMed:12748054};
GN   Synonyms=ZrTPS1 {ECO:0000303|PubMed:12748054};
OS   Zygosaccharomyces rouxii (Candida mogii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Zygosaccharomyces.
OX   NCBI_TaxID=4956;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
RC   STRAIN=KACC 30010;
RX   PubMed=12748054; DOI=10.1016/s1567-1356(03)00035-7;
RA   Kwon H.B., Yeo E.T., Hahn S.E., Bae S.C., Kim D.Y., Byun M.O.;
RT   "Cloning and characterization of genes encoding trehalose-6-phosphate
RT   synthase (TPS1) and trehalose-6-phosphate phosphatase (TPS2) from
RT   Zygosaccharomyces rouxii.";
RL   FEMS Yeast Res. 3:433-440(2003).
CC   -!- FUNCTION: Synthase catalytic subunit of the trehalose synthase complex
CC       that catalyzes the production of trehalose from glucose-6-phosphate and
CC       UDP-alpha-D-glucose in a two step process.
CC       {ECO:0000269|PubMed:12748054}.
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         Evidence={ECO:0000305|PubMed:12748054};
CC   -!- PATHWAY: Carbohydrate biosynthesis. {ECO:0000305}.
CC   -!- INDUCTION: Repressed by salt stress. {ECO:0000269|PubMed:12748054}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 20 family.
CC       {ECO:0000305}.
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DR   EMBL; AF276078; AAK69413.1; -; mRNA.
DR   AlphaFoldDB; Q96WK6; -.
DR   SMR; Q96WK6; -.
DR   CAZy; GT20; Glycosyltransferase Family 20.
DR   eggNOG; KOG1050; Eukaryota.
DR   GO; GO:0003825; F:alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity; IEA:UniProtKB-EC.
DR   GO; GO:0102986; F:trehalose synthase activity; IGI:UniProtKB.
DR   GO; GO:0005992; P:trehalose biosynthetic process; IGI:UniProtKB.
DR   CDD; cd03788; GT20_TPS; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   InterPro; IPR001830; Glyco_trans_20.
DR   InterPro; IPR012766; Trehalose_OtsA.
DR   NCBIfam; TIGR02400; trehalose_OtsA; 1.
DR   PANTHER; PTHR10788:SF106; BCDNA.GH08860; 1.
DR   PANTHER; PTHR10788; TREHALOSE-6-PHOSPHATE SYNTHASE; 1.
DR   Pfam; PF00982; Glyco_transf_20; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   1: Evidence at protein level;
KW   Glycosyltransferase; Transferase.
FT   CHAIN           1..485
FT                   /note="Alpha,alpha-trehalose-phosphate synthase [UDP-
FT                   forming]"
FT                   /id="PRO_0000122503"
FT   BINDING         99
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /evidence="ECO:0000250|UniProtKB:Q92410"
FT   BINDING         153
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /evidence="ECO:0000250|UniProtKB:Q92410"
FT   BINDING         290
FT                   /ligand="UDP"
FT                   /ligand_id="ChEBI:CHEBI:58223"
FT                   /evidence="ECO:0000250|UniProtKB:Q92410"
FT   BINDING         290
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q92410"
FT   BINDING         295
FT                   /ligand="UDP"
FT                   /ligand_id="ChEBI:CHEBI:58223"
FT                   /evidence="ECO:0000250|UniProtKB:Q92410"
FT   BINDING         295
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q92410"
FT   BINDING         328
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /evidence="ECO:0000250|UniProtKB:Q92410"
FT   BINDING         367
FT                   /ligand="UDP"
FT                   /ligand_id="ChEBI:CHEBI:58223"
FT                   /evidence="ECO:0000250|UniProtKB:Q92410"
FT   BINDING         367
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q92410"
FT   BINDING         389..397
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q92410"
FT   BINDING         393..397
FT                   /ligand="UDP"
FT                   /ligand_id="ChEBI:CHEBI:58223"
FT                   /evidence="ECO:0000250|UniProtKB:Q92410"
SQ   SEQUENCE   485 AA;  55022 MW;  DBDD486C7AF4A8CF CRC64;
     MTVSKKDSGK TSPGNIVVVS NRLPVTISKN AMGKYEYKFS SGGLVTALQG LKKTSTFQWY
     GWPSLEIPDD EKPVVKKDLL EKFNAIPIFL SDEIADLHYN GFSNSILWPL FHYHPGEINF
     DENAWLAYNE ANATFASEIC GNLQDNDLVW VHDYHLMLLP EMLSAHIQRK GLKNIKLGWF
     LHTPFPSSEI YRILPVRQEI LNGVLSCDLI GFHTYDYARH FLSSIQRCLN VNTLPNGVEY
     QGRFVNVGAF PIGIDVDTFK EGLQKENVKQ RIRTLQERFK GCKIMVGVDR LDYIKGVPQK
     LHAMEVFLNE HPEWIGKVVL VQLAIPSRGD VEEYQYLRSV VNELVGRING QFGTIEFVPI
     HFMHKSIPFE ELISLYAVSD ACIVSSTRDG MNLVSYEYIA CRKKGSLILS EFTGAAQSLN
     GALIVNPWNT DELSDSINEA LTLPDEKKDS NWEKLYKYIS KYTSAYWGEN FVHELNATGT
     IKTGQ
//