Q96WK6 · TPS1_ZYGRO
- ProteinAlpha,alpha-trehalose-phosphate synthase [UDP-forming]
- GeneTPS1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids485 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Synthase catalytic subunit of the trehalose synthase complex that catalyzes the production of trehalose from glucose-6-phosphate and UDP-alpha-D-glucose in a two step process.
Catalytic activity
- D-glucose 6-phosphate + UDP-alpha-D-glucose = alpha,alpha-trehalose 6-phosphate + UDP + H+
Pathway
Carbohydrate biosynthesis.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 99 | D-glucose 6-phosphate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 153 | D-glucose 6-phosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 290 | UDP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 290 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 295 | UDP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 295 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 328 | D-glucose 6-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 367 | UDP (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 367 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 389-397 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: DGMNLVSYE | ||||||
Binding site | 393-397 | UDP (UniProtKB | ChEBI) | ||||
Sequence: LVSYE |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | alpha,alpha-trehalose-phosphate synthase complex (UDP-forming) | |
Cellular Component | cytosol | |
Molecular Function | alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity | |
Molecular Function | trehalose synthase activity | |
Molecular Function | trehalose-phosphatase activity | |
Biological Process | cellular response to heat | |
Biological Process | trehalose biosynthetic process | |
Biological Process | trehalose metabolism in response to stress |
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameAlpha,alpha-trehalose-phosphate synthase [UDP-forming]
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Zygosaccharomyces
Accessions
- Primary accessionQ96WK6
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000122503 | 1-485 | Alpha,alpha-trehalose-phosphate synthase [UDP-forming] | |||
Sequence: MTVSKKDSGKTSPGNIVVVSNRLPVTISKNAMGKYEYKFSSGGLVTALQGLKKTSTFQWYGWPSLEIPDDEKPVVKKDLLEKFNAIPIFLSDEIADLHYNGFSNSILWPLFHYHPGEINFDENAWLAYNEANATFASEICGNLQDNDLVWVHDYHLMLLPEMLSAHIQRKGLKNIKLGWFLHTPFPSSEIYRILPVRQEILNGVLSCDLIGFHTYDYARHFLSSIQRCLNVNTLPNGVEYQGRFVNVGAFPIGIDVDTFKEGLQKENVKQRIRTLQERFKGCKIMVGVDRLDYIKGVPQKLHAMEVFLNEHPEWIGKVVLVQLAIPSRGDVEEYQYLRSVVNELVGRINGQFGTIEFVPIHFMHKSIPFEELISLYAVSDACIVSSTRDGMNLVSYEYIACRKKGSLILSEFTGAAQSLNGALIVNPWNTDELSDSINEALTLPDEKKDSNWEKLYKYISKYTSAYWGENFVHELNATGTIKTGQ |
Expression
Induction
Repressed by salt stress.
Structure
Sequence
- Sequence statusComplete
- Length485
- Mass (Da)55,022
- Last updated2001-12-01 v1
- ChecksumDBDD486C7AF4A8CF