O74932 · TPS1_YARLI
- ProteinAlpha,alpha-trehalose-phosphate synthase [UDP-forming]
- GeneTPS1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids469 (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 (PubMed:21931609).
The disaccharide trehalose serves as a storage carbohydrate that is mobilized during spore germination (PubMed:21931609).
The disaccharide trehalose serves as a storage carbohydrate that is mobilized during spore germination (PubMed:21931609).
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 | 87 | D-glucose 6-phosphate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 141 | D-glucose 6-phosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 279 | UDP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 279 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 284 | UDP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 284 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 317 | D-glucose 6-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 378-386 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: DGMNLVSYE | ||||||
Binding site | 382-386 | UDP (UniProtKB | ChEBI) | ||||
Sequence: LVSYE |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | alpha,alpha-trehalose-phosphate synthase complex (UDP-forming) | |
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 desiccation | |
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
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Dipodascaceae > Yarrowia
Accessions
- Primary accessionO74932
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000122501 | 1-469 | Alpha,alpha-trehalose-phosphate synthase [UDP-forming] | |||
Sequence: MPNVLVISNRLPVTISREEDGTYKYTMSSGGLVTALSGLKQSTTFQWFGWPGLEIPEKDKPRLINDLETMFSCVPVFMDDDLADLHYNGFSNSILWPLFHYHPGEMNFDQVAWEAYTQANRLFAKKVASIVKPGDIVWVHDYHLMLLPEMLREECENNSALDGLKIGFFLHTPFPSSEIYRILPVRKEVLTGVLSCNLIGFHTYDYARHFLSSVSRILDLETMPNGTYYKGRHVVVGAFPIGIDVNKFLEGCKRPAVQERIAQLQDKFKGIKVVVGVDRLDYIKGVPQKLHAFEVFLSEHPEWIGKVVLVQVAVPSRGLVEEYQNLRAVVNELVGRINGMFGTVEFTPIHFMHRSVDFNELIALYSISDVCFVSSTRDGMNLVSYEYVACQTEKHGSLILSEFTGAAQSLNGALIVNPWNTEDMAEALYDSLTFSPEKKAENHRKLFKYVSKYTSQHWGEAFVSELKRC |
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length469
- Mass (Da)53,259
- Last updated1998-11-01 v1
- ChecksumBCA5A82B98B0F23E
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ011032 EMBL· GenBank· DDBJ | CAA09463.1 EMBL· GenBank· DDBJ | mRNA | ||
CR382131 EMBL· GenBank· DDBJ | CAG79544.1 EMBL· GenBank· DDBJ | Genomic DNA |