A7J2C6 · AES1_HYPJE
- ProteinAcetylesterase
- Geneaes1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids348 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
Acetylesterase that acts as an exo-deacetylase (PubMed:24140638).
Shows activity towards naphtyl acetate, triacetin, as well as towards glucose- and xylose acetates (PubMed:18978092, Ref.2). Liberates acetic acid from xylo-oligomers (PubMed:18978092, PubMed:24140638, Ref.2).
Shows activity towards naphtyl acetate, triacetin, as well as towards glucose- and xylose acetates (PubMed:18978092, Ref.2). Liberates acetic acid from xylo-oligomers (PubMed:18978092, PubMed:24140638, Ref.2).
Catalytic activity
- an acetyl ester + H2O = an aliphatic alcohol + acetate + H+
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.23 mM | 4-nitrophenyl acetate |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
20.5 μmol/min/mg | toward 4-nitrophenyl acetate |
pH Dependence
Optimum pH is 5.5.
Temperature Dependence
Optimum temperature is 50 degrees Celsius.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | acetylesterase activity |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAcetylesterase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Hypocreales > Hypocreaceae > Trichoderma
Accessions
- Primary accessionA7J2C6
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-16 | |||||
Sequence: MRSILVIPSFVAVLNA | ||||||
Chain | PRO_5002710640 | 17-348 | Acetylesterase | |||
Sequence: FSLFPKPHDDFKYLITFGDSYTDNGRLGYYGSHQAHGPPPGVMPPEANVTASGGLQWPQYVEASTGATLYDYAIAGATCDNNNVERWAAFMNANYPSIITDEIPSFKADRKTKLYRGVTSANTVYALWIGTNDLSYTGILSDSQVKGTNITTYIDCLWNVFDAIHAAGGRRFVILNNNALQLTGLYRPLSDGGAGDNQFWQNKTLYNQTEYAQKMLEYTTSSNTMIDYGVPFHLLVKNRWPGSKVAVYDIHSLIMDIYNQPSRYLEPPHNVVGYYKHCDVNGTNCLYGPGRLDSYLWYDELHPSNIIASYIAREFLNVVSGRSKYGTYWEHW | ||||||
Glycosylation | 64 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 165 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 218 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 223 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 297 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
N-glycosylated.
Keywords
- PTM
PTM databases
Expression
Induction
Expression is induced by sophorose, cellulose, oat spelt xylan, lactose, and arabinose.
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length348
- Mass (Da)39,158
- Last updated2007-09-11 v1
- ChecksumFB0441DE6021AA4D