IED ID | IndEnz0010001115 |
Enzyme Type ID | esterase001115 |
Protein Name |
Acetylxylan esterase A EC 3.1.1.72 |
Gene Name | axeA aceA |
Organism | Aspergillus ficuum |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus ficuum |
Enzyme Sequence | MLSTHLLFLATTLLTSLFHPIAAHVAKRSGSLQQITDFGDNPTGVGMYIYVPNNLASNPGIVVAIHYCTGTGPGYYSNSPYATLSEQYGFIVIYPSSPYSGGCWDVSSQATLTHNGGGNSNSIANMVTWTISEYGADSKKVYVTGSSSGAMMTNVMAATYPELFAAGTVYSGVSAGCFYSDTNQVDGWNSTCAQGDVITTPEHWASIAEAMYPGYSGSRPKMQIYHGSVDTTLYPQNYYETCKQWAGVFGYDYSAPESTEANTPQTNYETTIWGDNLQGIFATGVGHTVPIHGDKDMEWFGFA |
Enzyme Length | 303 |
Uniprot Accession Number | Q96W96 |
Absorption | |
Active Site | ACT_SITE 147; /note=Charge relay system; /evidence=ECO:0000250 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Deacetylation of xylans and xylo-oligosaccharides.; EC=3.1.1.72; |
DNA Binding | |
EC Number | 3.1.1.72 |
Enzyme Function | FUNCTION: Acetylxylan esterase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Degrades acetylated xylans by cleaving acetyl side groups from the hetero-xylan backbone. {ECO:0000269|Ref.1}. |
Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Thermal stability decreased at temperatures above 40 degrees Celsius. {ECO:0000269|Ref.1}; |
PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. {ECO:0000269|Ref.1}; |
Pathway | PATHWAY: Glycan degradation; xylan degradation. |
nucleotide Binding | |
Features | Active site (1); Chain (1); Glycosylation (1); Signal peptide (1) |
Keywords | Carbohydrate metabolism;Cellulose degradation;Glycoprotein;Hydrolase;Polysaccharide degradation;Secreted;Serine esterase;Signal |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
Modified Residue | |
Post Translational Modification | PTM: Glycosylated. {ECO:0000269|Ref.1}. |
Signal Peptide | SIGNAL 1..23; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 32,591 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |