G4RK44 · TPSP_THETK
- ProteinBifunctional trehalose-6-phosphate synthase/phosphatase
- Genetpsp
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids731 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Bifunctional enzyme which catalyzes the transfer of glucose from UDP-alpha-D-glucose to glucose-6-phosphate to form trehalose-6-phosphate (Tre6P) and removes the phosphate from Tre6P to produce free trehalose.
Miscellaneous
Part of an operon with putative glycosyltransferase TTX_1305 and putative membrane protein TTX_1304.1.
Catalytic activity
- D-glucose 6-phosphate + UDP-alpha-D-glucose = alpha,alpha-trehalose 6-phosphate + H+ + UDP
Cofactor
Temperature Dependence
Active at 80 degrees Celsius.
Pathway
Glycan biosynthesis; trehalose biosynthesis.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 9 | D-glucose 6-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 25-26 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: GG | ||||||
Binding site | 89 | D-glucose 6-phosphate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 143 | D-glucose 6-phosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 276 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 281 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 314 | D-glucose 6-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 379-383 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: LVAKE | ||||||
Active site | 503 | Nucleophile | ||||
Sequence: D | ||||||
Binding site | 503 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 503-505 | alpha,alpha-trehalose 6-phosphate (UniProtKB | ChEBI) | ||||
Sequence: DYD | ||||||
Binding site | 505 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 684 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity | |
Molecular Function | metal ion binding | |
Molecular Function | trehalose-phosphatase activity | |
Biological Process | trehalose biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameBifunctional trehalose-6-phosphate synthase/phosphatase
Including 2 domains:
- Recommended nameAlpha,alpha-trehalose-phosphate synthase [UDP-forming]
- EC number
- Alternative names
- Recommended nameTrehalose-6-phosphate phosphatase
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageArchaea > Thermoproteota > Thermoprotei > Thermoproteales > Thermoproteaceae > Thermoproteus
Accessions
- Primary accessionG4RK44
- Secondary accessions
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000424542 | 1-731 | Bifunctional trehalose-6-phosphate synthase/phosphatase | |||
Sequence: MRLIVVSNRLPVTISPSGEIRESVGGLATAMKSFLGAVNGGRELGLEEVVWVGWSGVPSERESNDLRERLRGMGLEPVPLSSEEVEGFYEGFSNSTLWPLFHGFSEYATYEEKHWRAYRGVNEKYAKAVVALARPGDLVWIHDYHLMLAPAIVREAAEVGVGFFLHIPFPPAELLQLLPSEWRREILEGLLGSDLVGFHTYEYSANFSRSVVRFLGYKVEMGAIAVGHRRVRVGVFPIGIDFDRFYNSSQDPSVVEEMAKLREMLGRAKVVFSIDRLDYTKGVLRRVAAWERFLREHPEWRGRAVFVLVVVPSRTGVPMYEEMKRQIDREVGRINGELGELNWVPIVYLYRFIPSPTLMALYNIADVALITPLRDGMNLVAKEFVASKRDCRGVLILSELAGASKELAEALVINPNDVGGTAEAIAEALSMSEDEQCRRIRAMQERLRMRDVVRWGTDFIYSLISAKSAREEVEKALRYMEELSVDKLKSDFAKAKRRLLLLDYDGTLVPHYPYPHMAVPDGDLLELLSRLAALPETAVYVVSGRGRDFLDGWLGRLPVGLVAEHGFFLKHPGGEWKSLGKVDPSWRQYAKGIMEDFASNVPGSFVEVKEAGIAWHYRNADETIAEKAVVELIDALSNALAGSGLSILRGKKVVEVRPAGYTKGTAAKMLLDELSPDFVFVAGDDETDEGMFEVAPQSAYTVKVGPGPTLAKFRVGDYRGLRSLLEQLRPP |
Proteomic databases
Interaction
Subunit
May interact with the putative glycosyltransferase (GT) TTX_1305. TTX_1305 is required for the trehalose-6-phosphate synthase activity of tpsp.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-464 | Alpha,alpha-trehalose-phosphate synthase | ||||
Sequence: MRLIVVSNRLPVTISPSGEIRESVGGLATAMKSFLGAVNGGRELGLEEVVWVGWSGVPSERESNDLRERLRGMGLEPVPLSSEEVEGFYEGFSNSTLWPLFHGFSEYATYEEKHWRAYRGVNEKYAKAVVALARPGDLVWIHDYHLMLAPAIVREAAEVGVGFFLHIPFPPAELLQLLPSEWRREILEGLLGSDLVGFHTYEYSANFSRSVVRFLGYKVEMGAIAVGHRRVRVGVFPIGIDFDRFYNSSQDPSVVEEMAKLREMLGRAKVVFSIDRLDYTKGVLRRVAAWERFLREHPEWRGRAVFVLVVVPSRTGVPMYEEMKRQIDREVGRINGELGELNWVPIVYLYRFIPSPTLMALYNIADVALITPLRDGMNLVAKEFVASKRDCRGVLILSELAGASKELAEALVINPNDVGGTAEAIAEALSMSEDEQCRRIRAMQERLRMRDVVRWGTDFIYSLI | ||||||
Region | 465-731 | Trehalose-6-phosphate phosphatase | ||||
Sequence: SAKSAREEVEKALRYMEELSVDKLKSDFAKAKRRLLLLDYDGTLVPHYPYPHMAVPDGDLLELLSRLAALPETAVYVVSGRGRDFLDGWLGRLPVGLVAEHGFFLKHPGGEWKSLGKVDPSWRQYAKGIMEDFASNVPGSFVEVKEAGIAWHYRNADETIAEKAVVELIDALSNALAGSGLSILRGKKVVEVRPAGYTKGTAAKMLLDELSPDFVFVAGDDETDEGMFEVAPQSAYTVKVGPGPTLAKFRVGDYRGLRSLLEQLRPP |
Sequence similarities
In the N-terminal section; belongs to the glycosyltransferase 20 family.
In the C-terminal section; belongs to the trehalose phosphatase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length731
- Mass (Da)81,699
- Last updated2011-12-14 v1
- ChecksumD51D6D0B97A49FE4
Sequence caution
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ621287 EMBL· GenBank· DDBJ | CAF18468.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation | |
FN869859 EMBL· GenBank· DDBJ | CCC81939.1 EMBL· GenBank· DDBJ | Genomic DNA |