TRET_THELN
ID TRET_THELN Reviewed; 412 AA.
AC Q7LYW5; H3ZP64;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Trehalose synthase;
DE EC=2.4.1.245;
DE AltName: Full=Trehalose glycosyltransferring synthase {ECO:0000303|PubMed:15364950};
GN Name=treT {ECO:0000303|PubMed:15364950}; ORFNames=OCC_03547;
OS Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=523849;
RN [1] {ECO:0000312|EMBL:AAG45391.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 51850 / DSM 5473 / JCM 8560 / NS-C;
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 51850 / DSM 5473 / JCM 8560 / NS-C;
RX PubMed=22493191; DOI=10.1128/jb.00123-12;
RA Gardner A.F., Kumar S., Perler F.B.;
RT "Genome sequence of the model hyperthermophilic archaeon Thermococcus
RT litoralis NS-C.";
RL J. Bacteriol. 194:2375-2376(2012).
RN [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBUNIT, AND INDUCTION.
RX PubMed=15364950; DOI=10.1074/jbc.m404955200;
RA Qu Q., Lee S.J., Boos W.;
RT "TreT, a novel trehalose glycosyltransferring synthase of the
RT hyperthermophilic archaeon Thermococcus litoralis.";
RL J. Biol. Chem. 279:47890-47897(2004).
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.
CC {ECO:0000269|PubMed:15364950}.
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 Evidence={ECO:0000269|PubMed:15364950};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:15364950};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.14 mM for ADP-glucose {ECO:0000269|PubMed:15364950};
CC KM=6.2 mM for glucose {ECO:0000269|PubMed:15364950};
CC KM=11.5 mM for trehalose {ECO:0000269|PubMed:15364950};
CC Vmax=160 umol/min/mg enzyme toward ADP-glucose
CC {ECO:0000269|PubMed:15364950};
CC Vmax=220 umol/min/mg enzyme toward glucose
CC {ECO:0000269|PubMed:15364950};
CC Vmax=17 umol/min/mg enzyme toward trehalose
CC {ECO:0000269|PubMed:15364950};
CC pH dependence:
CC Optimum pH is 6.5. Only 13% of activity is retained at pH 7.5.
CC {ECO:0000269|PubMed:15364950};
CC Temperature dependence:
CC Optimum temperature is 90 degrees Celsius. 65% of activity remains at
CC 100 degrees Celsius. {ECO:0000269|PubMed:15364950};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15364950}.
CC -!- INDUCTION: By maltose, less efficiently by trehalose, and even less
CC efficiently by sucrose. {ECO:0000269|PubMed:15364950}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC Glycosyltransferase 4 subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF307053; AAG45391.1; -; Genomic_DNA.
DR EMBL; CP006670; EHR78231.1; -; Genomic_DNA.
DR RefSeq; WP_004068720.1; NC_022084.1.
DR AlphaFoldDB; Q7LYW5; -.
DR SMR; Q7LYW5; -.
DR STRING; 523849.OCC_03547; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR EnsemblBacteria; EHR78231; EHR78231; OCC_03547.
DR GeneID; 16548946; -.
DR KEGG; tlt:OCC_03547; -.
DR HOGENOM; CLU_045353_0_0_2; -.
DR OMA; FDPWKDL; -.
DR OrthoDB; 83551at2157; -.
DR BioCyc; MetaCyc:MON-14090; -.
DR Proteomes; UP000015502; 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 1: Evidence at protein level;
KW Carbohydrate metabolism; Glucose metabolism; Glycosyltransferase;
KW Magnesium; Transferase.
FT CHAIN 1..412
FT /note="Trehalose synthase"
FT /id="PRO_0000405302"
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
