ID   TRET_PYRFU              Reviewed;         412 AA.
AC   Q9HH00; E7FI30; Q7LYC8;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Trehalose synthase {ECO:0000250|UniProtKB:Q7LYW5, ECO:0000312|EMBL:AAL81866.1};
DE            EC=2.4.1.245;
DE   AltName: Full=Trehalose glycosyltransferring synthase {ECO:0000250|UniProtKB:Q7LYW5};
GN   Name=treT {ECO:0000250|UniProtKB:Q7LYW5}; OrderedLocusNames=PF1742;
OS   Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=186497;
RN   [1] {ECO:0000312|EMBL:AAG45375.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1
RC   {ECO:0000269|PubMed:11115105};
RX   PubMed=11115105; DOI=10.1046/j.1365-2958.2000.02161.x;
RA   Diruggiero J., Dunn D., Maeder D.L., Holley-Shanks R., Chatard J.,
RA   Horlacher R., Robb F.T., Boos W., Weiss R.B.;
RT   "Evidence of recent lateral gene transfer among hyperthermophilic
RT   archaea.";
RL   Mol. Microbiol. 38:684-693(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA   Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA   DiRuggiero J., Robb F.T.;
RT   "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT   horikoshii inferred from complete genomic sequences.";
RL   Genetics 152:1299-1305(1999).
CC   -!- FUNCTION: Synthesizes trehalose from ADP-glucose and glucose. Has a
CC       much lower activity toward UDP-glucose and GDP-glucose. The reaction is
CC       reversible, the equilibrium strongly favors trehalose synthesis (By
CC       similarity). {ECO:0000250|UniProtKB:Q7LYW5}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an NDP-alpha-D-glucose + D-glucose = a ribonucleoside 5'-
CC         diphosphate + alpha,alpha-trehalose + H(+); Xref=Rhea:RHEA:47416,
CC         ChEBI:CHEBI:4167, ChEBI:CHEBI:15378, ChEBI:CHEBI:16551,
CC         ChEBI:CHEBI:57930, ChEBI:CHEBI:76533; EC=2.4.1.245;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q7LYW5};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q7LYW5}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC       Glycosyltransferase 4 subfamily. {ECO:0000305}.
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DR   EMBL; AF307052; AAG45375.1; -; Genomic_DNA.
DR   EMBL; AE009950; AAL81866.1; -; Genomic_DNA.
DR   RefSeq; WP_004068720.1; NC_003413.1.
DR   AlphaFoldDB; Q9HH00; -.
DR   SMR; Q9HH00; -.
DR   STRING; 186497.PF1742; -.
DR   CAZy; GT4; Glycosyltransferase Family 4.
DR   PRIDE; Q9HH00; -.
DR   EnsemblBacteria; AAL81866; AAL81866; PF1742.
DR   GeneID; 16548946; -.
DR   KEGG; pfu:PF1742; -.
DR   PATRIC; fig|186497.12.peg.1811; -.
DR   eggNOG; arCOG01407; Archaea.
DR   HOGENOM; CLU_045353_0_0_2; -.
DR   OMA; FDPWKDL; -.
DR   OrthoDB; 83551at2157; -.
DR   PhylomeDB; Q9HH00; -.
DR   Proteomes; UP000001013; Chromosome.
DR   GO; GO:0102986; F:trehalose synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR001296; Glyco_trans_1.
DR   Pfam; PF00534; Glycos_transf_1; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Glucose metabolism; Glycosyltransferase;
KW   Magnesium; Reference proteome; Transferase.
FT   CHAIN           1..412
FT                   /note="Trehalose synthase"
FT                   /id="PRO_0000405299"
SQ   SEQUENCE   412 AA;  48017 MW;  6A5338298A6B5CEA CRC64;
     MYEVTKFGGE GKRLEDYREI IGDEALEAIK AKAENLKDKS FVHVNSTSFG GGVAEILHNL
     VPLMRDVGID ARWFVIEGTN EFFNVTKSFH NALQGNKELR LTEEMKKLYL EINKKNAEDI
     DLTQFDYVLI HDPQPAPLIE FYEKRQPWIW RCHIDLSDPN LEFWKFLRQF VEKYDRYIFH
     MEEYVQEDLN QEKVVIMPPS IDPLSEKNME LSESEILKTL ERFDVDPERP IITQVARFDP
     WKGVFDVIDV YRKVKEKIPE VQLLLVGVMA HDDPEGWIYF EKTLRKIGED YDIKVLTNLT
     GVHAREVNAF QRASDVILQM SIREGFGLTV TEAMWKEKPV VGRAVGGIKL QIVDGKTGFL
     VKDVNDAIEK TLYLLEHKDV AQEMGKNAKE RIKENFIITK HLERYLDLLN SF