P40387 · TPS1_SCHPO
- ProteinAlpha,alpha-trehalose-phosphate synthase [UDP-forming]
- Genetps1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids513 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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 (PubMed:8021171).
The disaccharide trehalose serves as a storage carbohydrate that is mobilized during nutrient stress and spore germination (PubMed:8021171, PubMed:9729425).
Together with ntp1, regulates the level of trehalose as a protectant for cell integrity during thermal and osmotic stress (PubMed:8021171, PubMed:9495778).
The disaccharide trehalose serves as a storage carbohydrate that is mobilized during nutrient stress and spore germination (PubMed:8021171, PubMed:9729425).
Together with ntp1, regulates the level of trehalose as a protectant for cell integrity during thermal and osmotic stress (PubMed:8021171, PubMed:9495778).
Catalytic activity
- D-glucose 6-phosphate + UDP-alpha-D-glucose = alpha,alpha-trehalose 6-phosphate + H+ + UDP
Pathway
Carbohydrate biosynthesis.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 104 | D-glucose 6-phosphate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 158 | D-glucose 6-phosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 294 | UDP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 294 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 299 | UDP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 299 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 332 | D-glucose 6-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 393-401 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: DGMNLVSYE | ||||||
Binding site | 397-401 | UDP (UniProtKB | ChEBI) | ||||
Sequence: LVSYE |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | alpha,alpha-trehalose-phosphate synthase complex (UDP-forming) | |
Cellular Component | cytosol | |
Cellular Component | nucleus | |
Molecular Function | alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity | |
Biological Process | ascospore formation | |
Biological Process | cellular response to heat | |
Biological Process | trehalose biosynthetic process | |
Biological Process | trehalose metabolic process | |
Biological Process | trehalose metabolism in response to stress |
Keywords
- Molecular function
- Biological process
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 > Taphrinomycotina > Schizosaccharomycetes > Schizosaccharomycetales > Schizosaccharomycetaceae > Schizosaccharomyces
Accessions
- Primary accessionP40387
- Secondary accessions
Proteomes
Organism-specific databases
Phenotypes & Variants
Disruption phenotype
Abolishes cytoplasmic neutral trehalase activation during thermal stress; activation during osmotic stress is normal (PubMed:9729425).
Decreases cellular trehalose 6-phosphate level in stationary phase and during thermal stress (PubMed:8021171).
Sensitive to heat shock and osmotic stress (PubMed:9495778).
Decreases cellular trehalose 6-phosphate level in stationary phase and during thermal stress (PubMed:8021171).
Sensitive to heat shock and osmotic stress (PubMed:9495778).
Variants
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The viewer provides 3 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000122500 | 1-513 | Alpha,alpha-trehalose-phosphate synthase [UDP-forming] | |||
Sequence: MSDAHDTIKSLTGDASNSRRLIVVSNRLPITIKRKDNGTYDFSMSSGGLVSALSGLKKLMTFQWLGWCGQEIPEDEKPMIIQRLQDECSAIPVFLDDETADRHYNGFSNSILWPLFHYHPGEINFDEENWEAYRAANYAFAEAIVKNLQDGDLIWVQDYHLMVLPQMLRELIGDKFKDIKIGFFLHTPFPSSEIYRVLPVRNEILEGVLNCDLVGFHTYDYARHFLSACSRILNLSTLPNGVEYNGQMVSVGTFPIGIDPEKFSDALKSDVVKDRIASIERRLQGVKVIVGVDRLDYIKGVPQKFHAFEVFLEQYPEWVGKVVLVQVAVPSRQDVEEYQNLRAVVNELVGRINGRFGTVEYTPIHFLHKSVRFEELVALYNVSDVCLITSTRDGMNLVSYEYICTQQERHGALILSEFAGAAQSLNGSIVINPWNTEELANSIHDALTMPEKQREANENKLFRYVNKYTSQFWGQSFVGELQRIQHYSHPHPRRTNPILRTKSAQVLSMNSSS | ||||||
Modified residue | 40 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 503 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Induction
By thermal stress.
Interaction
Subunit
Homomer (PubMed:12153582).
Component of the trehalose synthase complex that contains at least tps1, ntp1 and tpp1 (PubMed:12153582).
Interacts with tpp1 (PubMed:12153582).
Interacts with ntp1; the interaction is independent of stress conditions (PubMed:12153582, PubMed:12943532, PubMed:15965643).
Component of the trehalose synthase complex that contains at least tps1, ntp1 and tpp1 (PubMed:12153582).
Interacts with tpp1 (PubMed:12153582).
Interacts with ntp1; the interaction is independent of stress conditions (PubMed:12153582, PubMed:12943532, PubMed:15965643).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P40387 | ntp1 O42893 | 3 | EBI-26616873, EBI-26616855 | |
BINARY | P40387 | tpp1 P78875 | 2 | EBI-26616873, EBI-26616958 |
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length513
- Mass (Da)58,493
- Last updated2001-08-14 v2
- Checksum9FC247B626CE2B00
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 277 | in Ref. 1; CAA82861 | ||||
Sequence: A → R |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Z29971 EMBL· GenBank· DDBJ | CAA82861.1 EMBL· GenBank· DDBJ | Genomic DNA | Frameshift | |
CU329670 EMBL· GenBank· DDBJ | CAB95998.1 EMBL· GenBank· DDBJ | Genomic DNA |