| 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 |