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Protein

Trehalose synthase

Gene

treT

Organism
Rubrobacter xylanophilus (strain DSM 9941 / NBRC 16129)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Synthesizes trehalose from ADP-glucose and glucose. The reaction is reversible, the equilibrium strongly favors trehalose synthesis.1 Publication

Catalytic activityi

NDP-alpha-D-glucose + D-glucose = alpha,alpha-trehalose + NDP.1 Publication

Cofactori

Mg2+By similarity

Enzyme regulationi

Inhibited by 20 mM Fe3+ and Mn2+. Partially inhibited by Zn2+ and Ni2+. Activity is slightly enhanced by 2 mM Fe (3+), Mn (2+), Ca2+ or Li+ and by 20 mM Mg2+, Ca2+ or Li+.1 Publication

Kineticsi

  1. KM=0.8 mM for ADP-glucose1 Publication
  2. KM=1.3 mM for glucose1 Publication
  3. KM=82 mM for trehalose1 Publication
  4. KM=6.8 mM for ADP1 Publication
  1. Vmax=37 µmol/min/mg enzyme for the synthesis of trehalose1 Publication

pH dependencei

Optimum pH is 8.0-10.0.1 Publication

Temperature dependencei

Optimum temperature is 60 degrees Celsius. Active between 20 and 80 degrees Celsius. Half-life at 60 degrees Celsius is 309 hours. Half-life at 70 degrees Celsius is 4.1 hours.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Carbohydrate metabolism, Glucose metabolism

Keywords - Ligandi

Magnesium

Enzyme and pathway databases

BioCyciRXYL266117:GH8O-3035-MONOMER.
BRENDAi2.4.1.245. 10017.

Protein family/group databases

CAZyiGT4. Glycosyltransferase Family 4.

Names & Taxonomyi

Protein namesi
Recommended name:
Trehalose synthaseBy similarity (EC:2.4.1.245)
Alternative name(s):
Trehalose glycosyltransferring synthaseImported
Gene namesi
Name:treTImported
Ordered Locus Names:Rxyl_2973
OrganismiRubrobacter xylanophilus (strain DSM 9941 / NBRC 16129)
Taxonomic identifieri266117 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaRubrobacteriaRubrobacteralesRubrobacteraceaeRubrobacter
Proteomesi
  • UP000006637 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 416416Trehalose synthasePRO_0000405301Add
BLAST

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi266117.Rxyl_2973.

Structurei

3D structure databases

ProteinModelPortaliQ1ARU5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG41088YS. Bacteria.
ENOG410XQX3. LUCA.
HOGENOMiHOG000227006.
KOiK13057.
OMAiQEINSTR.
OrthoDBiEOG6PP9ND.

Family and domain databases

InterProiIPR001296. Glyco_trans_1.
[Graphical view]
PfamiPF00534. Glycos_transf_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q1ARU5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLQRVNPGHK ALADYRSIIR RELYGELQEL AGRLRGARVL HINATSFGGG
60 70 80 90 100
VAEILYTLVP LARDAGLEVE WAIMFGAEPF FNVTKRFHNA LQGADYELTI
110 120 130 140 150
EDRAIYEEYN RRTAQALAES GEEWDIVFVH DPQPALVREF SGGLGEGTRW
160 170 180 190 200
IWRCHIDTST PNRQVLDYLW PYIADYDAQV YTMREYTPPG VEMPGLTLIP
210 220 230 240 250
PAIDPLSPKN MALSRDDASY IVSQFGVDVE RPFLLQVSRF DPWKDPLGVI
260 270 280 290 300
DVYRMVKEEV GEVQLVLVGS MAHDDPEGWD YWYKTVNYAG GDPDIFLFSN
310 320 330 340 350
LTNVGAIEVN AFQSLADVVI QKSIREGFGL VVSEALWKAR PVVASRVGGI
360 370 380 390 400
PMQITAGGGI LIDTIPEAAA ACAKLLSDPE FAREMGRRGK EHVRANFLTP
410
RLLRDDLRLF AKLLGV
Length:416
Mass (Da):46,557
Last modified:July 11, 2006 - v1
Checksum:iF723339BFE3EEDB8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti20 – 201R → H in ACJ76775 (PubMed:18835983).Curated
Sequence conflicti25 – 251G → E in ACJ76775 (PubMed:18835983).Curated
Sequence conflicti42 – 421I → V in ACJ76775 (PubMed:18835983).Curated
Sequence conflicti63 – 631R → L in ACJ76775 (PubMed:18835983).Curated
Sequence conflicti115 – 1151Q → R in ACJ76775 (PubMed:18835983).Curated
Sequence conflicti129 – 1291V → I in ACJ76775 (PubMed:18835983).Curated
Sequence conflicti145 – 1451G → R in ACJ76775 (PubMed:18835983).Curated
Sequence conflicti193 – 1931M → L in ACJ76775 (PubMed:18835983).Curated
Sequence conflicti229 – 2302VE → TG in ACJ76775 (PubMed:18835983).Curated
Sequence conflicti257 – 2571K → R in ACJ76775 (PubMed:18835983).Curated
Sequence conflicti261 – 2611G → P in ACJ76775 (PubMed:18835983).Curated
Sequence conflicti356 – 3561A → S in ACJ76775 (PubMed:18835983).Curated
Sequence conflicti380 – 3801E → D in ACJ76775 (PubMed:18835983).Curated
Sequence conflicti406 – 4061D → E in ACJ76775 (PubMed:18835983).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU881704 Genomic DNA. Translation: ACJ76775.1.
CP000386 Genomic DNA. Translation: ABG05883.1.
RefSeqiWP_011565892.1. NC_008148.1.

Genome annotation databases

EnsemblBacteriaiABG05883; ABG05883; Rxyl_2973.
KEGGirxy:Rxyl_2973.
PATRICi23372756. VBIRubXyl52678_2948.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU881704 Genomic DNA. Translation: ACJ76775.1.
CP000386 Genomic DNA. Translation: ABG05883.1.
RefSeqiWP_011565892.1. NC_008148.1.

3D structure databases

ProteinModelPortaliQ1ARU5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi266117.Rxyl_2973.

Protein family/group databases

CAZyiGT4. Glycosyltransferase Family 4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABG05883; ABG05883; Rxyl_2973.
KEGGirxy:Rxyl_2973.
PATRICi23372756. VBIRubXyl52678_2948.

Phylogenomic databases

eggNOGiENOG41088YS. Bacteria.
ENOG410XQX3. LUCA.
HOGENOMiHOG000227006.
KOiK13057.
OMAiQEINSTR.
OrthoDBiEOG6PP9ND.

Enzyme and pathway databases

BioCyciRXYL266117:GH8O-3035-MONOMER.
BRENDAi2.4.1.245. 10017.

Family and domain databases

InterProiIPR001296. Glyco_trans_1.
[Graphical view]
PfamiPF00534. Glycos_transf_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A unique combination of genetic systems for the synthesis of trehalose in Rubrobacter xylanophilus: properties of a rare actinobacterial TreT."
    Nobre A., Alarico S., Fernandes C., Empadinhas N., da Costa M.S.
    J. Bacteriol. 190:7939-7946(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 9941 / NBRC 16129.

Entry informationi

Entry nameiTRET_RUBXD
AccessioniPrimary (citable) accession number: Q1ARU5
Secondary accession number(s): B8R7Q1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 8, 2011
Last sequence update: July 11, 2006
Last modified: January 20, 2016
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.