TRET_RUBXD
ID TRET_RUBXD Reviewed; 416 AA.
AC Q1ARU5; B8R7Q1;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Trehalose synthase {ECO:0000250|UniProtKB:Q7LYW5};
DE EC=2.4.1.245;
DE AltName: Full=Trehalose glycosyltransferring synthase {ECO:0000312|EMBL:ACJ76775.1};
GN Name=treT {ECO:0000312|EMBL:ACJ76775.1}; OrderedLocusNames=Rxyl_2973;
OS Rubrobacter xylanophilus (strain DSM 9941 / NBRC 16129 / PRD-1).
OC Bacteria; Actinobacteria; Rubrobacteria; Rubrobacterales; Rubrobacteraceae;
OC Rubrobacter.
OX NCBI_TaxID=266117;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ACJ76775.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18835983; DOI=10.1128/jb.01055-08;
RA Nobre A., Alarico S., Fernandes C., Empadinhas N., da Costa M.S.;
RT "A unique combination of genetic systems for the synthesis of trehalose in
RT Rubrobacter xylanophilus: properties of a rare actinobacterial TreT.";
RL J. Bacteriol. 190:7939-7946(2008).
RN [2] {ECO:0000312|EMBL:ABG05883.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9941 / NBRC 16129 / PRD-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., da Costa M.S.,
RA Rainey F.A., Empadinhas N., Jolivet E., Battista J.R., Richardson P.;
RT "Complete sequence of Rubrobacter xylanophilus DSM 9941.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Synthesizes trehalose from ADP-glucose and glucose. The
CC reaction is reversible, the equilibrium strongly favors trehalose
CC synthesis. {ECO:0000269|PubMed:18835983}.
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:18835983};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q7LYW5};
CC -!- ACTIVITY REGULATION: Inhibited by 20 mM Fe(3+) and Mn(2+). Partially
CC inhibited by Zn(2+) and Ni(2+). Activity is slightly enhanced by 2 mM
CC Fe (3+), Mn (2+), Ca(2+) or Li(+) and by 20 mM Mg(2+), Ca(2+) or Li(+).
CC {ECO:0000269|PubMed:18835983}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.8 mM for ADP-glucose {ECO:0000269|PubMed:18835983};
CC KM=1.3 mM for glucose {ECO:0000269|PubMed:18835983};
CC KM=82 mM for trehalose {ECO:0000269|PubMed:18835983};
CC KM=6.8 mM for ADP {ECO:0000269|PubMed:18835983};
CC Vmax=37 umol/min/mg enzyme for the synthesis of trehalose
CC {ECO:0000269|PubMed:18835983};
CC pH dependence:
CC Optimum pH is 8.0-10.0. {ECO:0000269|PubMed:18835983};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius. Active between 20 and 80
CC degrees Celsius. Half-life at 60 degrees Celsius is 309 hours. Half-
CC life at 70 degrees Celsius is 4.1 hours.
CC {ECO:0000269|PubMed:18835983};
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; EU881704; ACJ76775.1; -; Genomic_DNA.
DR EMBL; CP000386; ABG05883.1; -; Genomic_DNA.
DR RefSeq; WP_011565892.1; NC_008148.1.
DR AlphaFoldDB; Q1ARU5; -.
DR SMR; Q1ARU5; -.
DR STRING; 266117.Rxyl_2973; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR EnsemblBacteria; ABG05883; ABG05883; Rxyl_2973.
DR KEGG; rxy:Rxyl_2973; -.
DR eggNOG; COG0438; Bacteria.
DR HOGENOM; CLU_045353_0_0_11; -.
DR OMA; FDPWKDL; -.
DR OrthoDB; 694191at2; -.
DR PhylomeDB; Q1ARU5; -.
DR BRENDA; 2.4.1.245; 10017.
DR Proteomes; UP000006637; 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; Reference proteome; Transferase.
FT CHAIN 1..416
FT /note="Trehalose synthase"
FT /id="PRO_0000405301"
FT CONFLICT 20
FT /note="R -> H (in Ref. 1; ACJ76775)"
FT /evidence="ECO:0000305"
FT CONFLICT 25
FT /note="G -> E (in Ref. 1; ACJ76775)"
FT /evidence="ECO:0000305"
FT CONFLICT 42
FT /note="I -> V (in Ref. 1; ACJ76775)"
FT /evidence="ECO:0000305"
FT CONFLICT 63
FT /note="R -> L (in Ref. 1; ACJ76775)"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="Q -> R (in Ref. 1; ACJ76775)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="V -> I (in Ref. 1; ACJ76775)"
FT /evidence="ECO:0000305"
FT CONFLICT 145
FT /note="G -> R (in Ref. 1; ACJ76775)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="M -> L (in Ref. 1; ACJ76775)"
FT /evidence="ECO:0000305"
FT CONFLICT 229..230
FT /note="VE -> TG (in Ref. 1; ACJ76775)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="K -> R (in Ref. 1; ACJ76775)"
FT /evidence="ECO:0000305"
FT CONFLICT 261
FT /note="G -> P (in Ref. 1; ACJ76775)"
FT /evidence="ECO:0000305"
FT CONFLICT 356
FT /note="A -> S (in Ref. 1; ACJ76775)"
FT /evidence="ECO:0000305"
FT CONFLICT 380
FT /note="E -> D (in Ref. 1; ACJ76775)"
FT /evidence="ECO:0000305"
FT CONFLICT 406
FT /note="D -> E (in Ref. 1; ACJ76775)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 416 AA; 46557 MW; F723339BFE3EEDB8 CRC64;
MLQRVNPGHK ALADYRSIIR RELYGELQEL AGRLRGARVL HINATSFGGG VAEILYTLVP
LARDAGLEVE WAIMFGAEPF FNVTKRFHNA LQGADYELTI EDRAIYEEYN RRTAQALAES
GEEWDIVFVH DPQPALVREF SGGLGEGTRW IWRCHIDTST PNRQVLDYLW PYIADYDAQV
YTMREYTPPG VEMPGLTLIP PAIDPLSPKN MALSRDDASY IVSQFGVDVE RPFLLQVSRF
DPWKDPLGVI DVYRMVKEEV GEVQLVLVGS MAHDDPEGWD YWYKTVNYAG GDPDIFLFSN
LTNVGAIEVN AFQSLADVVI QKSIREGFGL VVSEALWKAR PVVASRVGGI PMQITAGGGI
LIDTIPEAAA ACAKLLSDPE FAREMGRRGK EHVRANFLTP RLLRDDLRLF AKLLGV
