| IED ID | IndEnz0010000393 |
| Enzyme Type ID | esterase000393 |
| Protein Name |
Acetylxylan esterase A EC 3.1.1.72 |
| Gene Name | axeA aceA |
| Organism | Aspergillus awamori (Black koji mold) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus awamori (Black koji mold) |
| Enzyme Sequence | MLLSTHLLFVITTLVTSLLHPIDGHAVKRSGSLQQVTDFGDNPTNVGMYIYVPNNLASNPGIVVAIHYCTGTGPGYYGDSPYATLSEQYGFIVIYPSSPYSGGCWDVSSQATLTHNGGGNSNSIANMVTWTISKYGADSSKVFVTGSSSGAMMTNVMAATYPELFAAATVYSGVSAGCFYSNTNQVDGWNSTCAQGDVITTPEHWASIAEAMYSGYSGSRPRMQIYHGSIDTTLYPQNYYETCKQWAGVFGYDYSAPEKTEANTPQTNYETTIWGDSLQGIFATGVGHTVPIHGDKDMEWFGFA |
| Enzyme Length | 304 |
| Uniprot Accession Number | Q92194 |
| Absorption | |
| Active Site | ACT_SITE 148; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Inactivated by di-isopropylfluorophosphate and phenylmethylsulfonylfluorid (PMSF), a specific inhibitor of serine esterases. {ECO:0000269|PubMed:9291122}. |
| 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|PubMed:9291122}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Activity is decreased at temperatures higher than 40 degrees Celsius. {ECO:0000269|PubMed:9291122}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. Activity is significantly retained from pH 6.0 to 9.0. {ECO:0000269|PubMed:9291122}; |
| Pathway | PATHWAY: Glycan degradation; xylan degradation. |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (11); Chain (1); Glycosylation (1); Helix (9); Signal peptide (1); Turn (3) |
| Keywords | 3D-structure;Carbohydrate metabolism;Cellulose degradation;Direct protein sequencing;Glycoprotein;Hydrolase;Polysaccharide degradation;Secreted;Serine esterase;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..24; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 5X6S; |
| Mapped Pubmed ID | 15848131; 28802264; |
| Motif | |
| Gene Encoded By | |
| Mass | 32,729 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |