ID   TPS1_ENCCU              Reviewed;         459 AA.
AC   Q8SSL2;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   27-MAR-2024, entry version 92.
DE   RecName: Full=Alpha,alpha-trehalose-phosphate synthase [UDP-forming];
DE            EC=2.4.1.15 {ECO:0000250|UniProtKB:Q00764};
DE   AltName: Full=General glucose sensor subunit 1;
DE   AltName: Full=Trehalose synthase complex catalytic subunit TPS1;
DE   AltName: Full=Trehalose-6-phosphate synthase;
DE   AltName: Full=UDP-glucose-glucosephosphate glucosyltransferase;
GN   Name=TPS1; OrderedLocusNames=ECU01_0800;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11157783; DOI=10.1101/gr.164301;
RA   Peyret P., Katinka M.D., Duprat S., Duffieux F., Barbe V., Barbazanges M.,
RA   Weissenbach J., Saurin W., Vivares C.P.;
RT   "Sequence and analysis of chromosome I of the amitochondriate intracellular
RT   parasite Encephalitozoon cuniculi (Microspora).";
RL   Genome Res. 11:198-207(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=16691553; DOI=10.1002/pmic.200500796;
RA   Brosson D., Kuhn L., Delbac F., Garin J., Vivares C.P., Texier C.;
RT   "Proteomic analysis of the eukaryotic parasite Encephalitozoon cuniculi
RT   (microsporidia): a reference map for proteins expressed in late sporogonial
RT   stages.";
RL   Proteomics 6:3625-3635(2006).
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. Can function independently
CC       of the complex (By similarity). {ECO:0000250|UniProtKB:Q00764}.
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:0000250|UniProtKB:Q00764};
CC   -!- SUBUNIT: Component of the trehalose synthase complex.
CC       {ECO:0000250|UniProtKB:Q00764}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q00764}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in late sporogonial stages.
CC       {ECO:0000269|PubMed:16691553}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 20 family.
CC       {ECO:0000305}.
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DR   EMBL; AL391737; CAD24950.1; -; Genomic_DNA.
DR   RefSeq; XP_965915.1; XM_960822.1.
DR   AlphaFoldDB; Q8SSL2; -.
DR   SMR; Q8SSL2; -.
DR   STRING; 284813.Q8SSL2; -.
DR   CAZy; GT20; Glycosyltransferase Family 20.
DR   VEuPathDB; MicrosporidiaDB:ECU01_0800; -.
DR   HOGENOM; CLU_002351_7_2_1; -.
DR   InParanoid; Q8SSL2; -.
DR   OMA; RTIWPLF; -.
DR   OrthoDB; 1023at2759; -.
DR   Proteomes; UP000000819; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003825; F:alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity; IEA:UniProtKB-EC.
DR   GO; GO:0005992; P:trehalose biosynthetic process; IEA:InterPro.
DR   CDD; cd03788; GT20_TPS; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   InterPro; IPR001830; Glyco_trans_20.
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   Cytoplasm; Glycosyltransferase; Reference proteome; Stress response;
KW   Transferase.
FT   CHAIN           1..459
FT                   /note="Alpha,alpha-trehalose-phosphate synthase [UDP-
FT                   forming]"
FT                   /id="PRO_0000381753"
FT   BINDING         86
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /evidence="ECO:0000250|UniProtKB:Q92410"
FT   BINDING         140
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /evidence="ECO:0000250|UniProtKB:Q92410"
FT   BINDING         262
FT                   /ligand="UDP"
FT                   /ligand_id="ChEBI:CHEBI:58223"
FT                   /evidence="ECO:0000250|UniProtKB:Q92410"
FT   BINDING         262
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q92410"
FT   BINDING         267
FT                   /ligand="UDP"
FT                   /ligand_id="ChEBI:CHEBI:58223"
FT                   /evidence="ECO:0000250|UniProtKB:Q92410"
FT   BINDING         267
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q92410"
FT   BINDING         300
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /evidence="ECO:0000250|UniProtKB:Q92410"
FT   BINDING         361..369
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q92410"
FT   BINDING         365..369
FT                   /ligand="UDP"
FT                   /ligand_id="ChEBI:CHEBI:58223"
FT                   /evidence="ECO:0000250|UniProtKB:Q92410"
SQ   SEQUENCE   459 AA;  52575 MW;  4691E0E97F948AA3 CRC64;
     MKLLVVSNRL PLTVKKSKDG FEYTKTSGGL VTGLRGISDK IRFMWLGNIS GVELDEEEKK
     VIRKDCWEKF HSIPVFIDPV LNSNSYDGFC NAILWPIIHS FKDDVAFTIK DYNAYVEYNT
     IFCEEICKIV EDGDIVWVHD YHLMILPEML RKKSDKSFKI MFFLHAQFPP AEIMETLACR
     REIVSGMAHS DLIAFHSFDY AINFDDTCRA NKVEVRSKLD AIPIGIDPAM FRSALKEEKT
     VERIKELREM FRGRKILLGV DRTDYIKGMP HRVKGFQRFL EKHPEFLDNV VFLQVGVPSR
     TSVKEYSSYI TKMNELVSET NSKFGSIESV HLYFLNKSVD FNELCALYAV SDMLLVTSLQ
     DGMNLVALEY ISCQNENNGV LLLSSNAGAS TTLPAAVEVN SWNTEEIADG IHRAITMSLE
     ERTERHEINR KAVDTFTSVE WAEKNLDGLC DDWRESLML
//