A0R4M9 · OTSA_MYCS2
- ProteinTrehalose-6-phosphate synthase
- GeneotsA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids503 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in the production of glycogen and alpha-glucan via the TreS-Pep2 branch involved in the biosynthesis of maltose-1-phosphate (M1P), and probably in the osmoprotection via the biosynthesis of trehalose (PubMed:27513637, Ref.4). Catalyzes the transfer of glucose from UDP-glucose (UDP-Glc) to glucose-6-phosphate (Glc-6-P) to form trehalose-6-phosphate (Ref.4). ADP-Glc, CDP-Glc, GDP-Glc and TDP-Glc are also glucosyl donors, however, when the pyrimidine sugar nucleotides (CDP-Glc, TDP-Glc and UDP-Glc) are used as substrates, there is an absolute requirement for a high molecular weight polyanion for activity (Ref.4).
Catalytic activity
- ADP-alpha-D-glucose + D-glucose 6-phosphate = ADP + alpha,alpha-trehalose 6-phosphate + H+
- CDP-alpha-D-glucose + D-glucose 6-phosphate = alpha,alpha-trehalose 6-phosphate + CDP + H+
- D-glucose 6-phosphate + GDP-alpha-D-glucose = alpha,alpha-trehalose 6-phosphate + GDP + H+
- D-glucose 6-phosphate + TDP-alpha-D-glucose = alpha,alpha-trehalose 6-phosphate + H+ + TDP
Activity regulation
Stimulated by the polynucleotide FII (physiological activator), and by chondroitin sulfate (CS) and heparin. Activation by the polyanion is inhibited by high salt concentration as well as by high concentrations of mononucleoside phosphates.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
40 μM | UDP-Glc | in the presence of polyanion | ||||
1 mM | Glc-6-P | with UDP-Glc in the presence of polyanion | ||||
2 mM | Glc-6-P | with GDP-Glc in the presence of polyanion |
pH Dependence
Optimum pH is 7.
Temperature Dependence
About 60% of the activity is lost in the absence of FII after 10 minutes at 40 degrees Celsius, but only 35% in the presence of FII.
Pathway
Glycan biosynthesis; trehalose biosynthesis.
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 22 | D-glucose 6-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 42-43 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: GG | ||||||
Binding site | 94 | D-glucose 6-phosphate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Site | 103 | Involved in alpha anomer selectivity | ||||
Sequence: W | ||||||
Binding site | 148 | D-glucose 6-phosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Site | 173 | Involved in alpha anomer selectivity | ||||
Sequence: I | ||||||
Binding site | 290 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 295 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 328 | D-glucose 6-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 393-397 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: LVAKE |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | alpha,alpha-trehalose-phosphate synthase (GDP-forming) activity | |
Molecular Function | alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity | |
Biological Process | trehalose biosynthetic process |
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameTrehalose-6-phosphate synthase
- EC number
- Short namesTPS
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Mycobacteriaceae > Mycolicibacterium
Accessions
- Primary accessionA0R4M9
- Secondary accessions
Proteomes
Phenotypes & Variants
Disruption phenotype
Cells lacking this gene do not accumulate ADP-glucose, however combined inactivation of both glgM and ostA accumulates ADP-glucose.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000348910 | 1-503 | Trehalose-6-phosphate synthase | |||
Sequence: MSPESGHETISGTSDFVVVANRLPVDLERLPDGTTRWKRSPGGLVTALEPLLRKRRGSWIGWAGVADSDEEPIVQDGLQLHPVRLSADDVAKYYEGFSNATLWPLYHDLIVKPEYHREWWDRYVEVNRRFAEATARAAAEGATVWIQDYQLQLVPKMLRMLRPDVTIGFFLHIPFPPVELFMQMPWRTEIVEGLLGADLVGFHLPGGAQNFLVLSRRLVGANTSRASIGVRSRFGEVQVGFRTVKVGAFPISIDSAELDGKARNRAIRQRARQIRAELGNPRKIMLGVDRLDYTKGIDVRLRALSELLEEKRIKRDDTVLVQLATPSRERVESYIAMREDIERQVGHINGEYGEVGHPIVHYLHRPIPRDELIAFFVAADVMLVTPLRDGMNLVAKEYVACRSDLGGALVLSEFTGAAAELRQAYLVNPHDLEGVKDKIEAAVNQNPEEGKRRMRALRRQVLAHDVDRWARSFLDALAATGETGDSGVTGESTPAPESDSGSF |
Proteomic databases
Interaction
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 481-503 | Disordered | ||||
Sequence: GETGDSGVTGESTPAPESDSGSF | ||||||
Compositional bias | 485-503 | Polar residues | ||||
Sequence: DSGVTGESTPAPESDSGSF |
Sequence similarities
Belongs to the glycosyltransferase 20 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length503
- Mass (Da)56,280
- Last updated2007-01-09 v1
- Checksum3D4B5CE2E6DA5ACF
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 485-503 | Polar residues | ||||
Sequence: DSGVTGESTPAPESDSGSF |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000480 EMBL· GenBank· DDBJ | ABK71484.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP001663 EMBL· GenBank· DDBJ | AFP42165.1 EMBL· GenBank· DDBJ | Genomic DNA |