A0A384JRP0 · TREA_BOTFB
- ProteinCytosolic neutral trehalase
- GeneTRE1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids727 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Hydrolyzes intracellular trehalose to glucose (PubMed:16946258).
The disaccharide trehalose serves as a storage carbohydrate that is mobilized during conidial germination (PubMed:16946258).
Regulates the level of trehalose as a protectant for cell integrity (PubMed:16946258).
The disaccharide trehalose serves as a storage carbohydrate that is mobilized during conidial germination (PubMed:16946258).
Regulates the level of trehalose as a protectant for cell integrity (PubMed:16946258).
Catalytic activity
- alpha,alpha-trehalose + H2O = alpha-D-glucose + beta-D-glucose
Cofactor
Pathway
Carbohydrate degradation.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 93 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 95 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 97 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 99 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 104 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 280 | substrate | ||||
Sequence: R | ||||||
Binding site | 287-288 | substrate | ||||
Sequence: WD | ||||||
Binding site | 324 | substrate | ||||
Sequence: N | ||||||
Binding site | 333-335 | substrate | ||||
Sequence: RSQ | ||||||
Binding site | 400 | substrate | ||||
Sequence: E | ||||||
Binding site | 449 | substrate | ||||
Sequence: R | ||||||
Binding site | 452 | substrate | ||||
Sequence: G | ||||||
Active site | 454 | Proton donor/acceptor | ||||
Sequence: D | ||||||
Active site | 658 | Proton donor/acceptor | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | alpha,alpha-trehalose-phosphate synthase complex (UDP-forming) | |
Molecular Function | alpha,alpha-trehalase activity | |
Molecular Function | calcium ion binding | |
Biological Process | ascospore formation | |
Biological Process | trehalose catabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCytosolic neutral trehalase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Leotiomycetes > Helotiales > Sclerotiniaceae > Botrytis
Accessions
- Primary accessionA0A384JRP0
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000452801 | 1-727 | Cytosolic neutral trehalase | |||
Sequence: MTSPLRKHRTSSVSSEIDPFAAAHVYYSNDTNQKSFRQARTRTYSSNQGIFSTPISGLEKPKRRGSHDDIGDHGRKFLIQVDSTLEALRKQEDTDDNHQITIEDVGPKSLPLGTATSNGFRRYDIRGTYMLSNLLQELTLAKENGREQIILDESRLNENPVNRLSRLIQGSFWDGLTRRIDGSVIEIAGRDPKDWTDDPRPRIYIPRGAPEQHAYYTKVATDRPEVRLDVCWLPEKITPEVVRDMNSKPGLLAVAMEEVIDPSTGEKTLKGLPFVVPGGRFNELYGWDSYMESLGLIVNDKVHLAKSMVQNFCFCIEHYGKILNATRSYYLCRSQPPFLTDMALRVFDKIKHEPGSLDFLKTAILAAIKEYHSVWTAEPRYDPVTGLSRYRPEGLGVPPETEASHFEHLLAPYAEKYNMTFKEFVDAYNNGRVVEKELDDYFLHDRAVRESGHDTSYRLERVCADLATIDLNSLLYKYEKDIAYTIRTFFQDKLEVPAEFCVGDMTPGQLQTSSMWDRRARGRKLAIDKYLWNKEKGMYFDYNTLKKEQCTYESATTFWAMWAGVASPQQAASLVTNALPKFEAAGGLLSGTEESRGAVGLDRPNRQWDYPYGWAPQQMLAWTGLLRYNYQEDAERLAYKWLFMITTAFVDFNGVVVEKYDVTRVVDPHKVDAEYGNQGSDFKGVAKEGFGWVNASYVYGLQIINAHMRRTLGTLTPWDQYNKAMNL |
Structure
Family & Domains
Sequence
- Sequence statusComplete
- Length727
- Mass (Da)83,085
- Last updated2018-11-07 v1
- ChecksumDB3F46A4F84C92B8
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP009813 EMBL· GenBank· DDBJ | ATZ53256.1 EMBL· GenBank· DDBJ | Genomic DNA |