| IED ID | IndEnz0010000005 |
| Enzyme Type ID | esterase000005 |
| Protein Name |
Acetylxylan esterase A EC 3.1.1.72 AXE I Acetylxylan esterase 1 |
| Gene Name | axeA aceA axe-1 axeI |
| Organism | Talaromyces purpureogenus (Soft rot fungus) (Penicillium purpureogenum) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Trichocomaceae Talaromyces Talaromyces sect. Talaromyces Talaromyces purpureogenus (Soft rot fungus) (Penicillium purpureogenum) |
| Enzyme Sequence | MKSLSFSFLVTLFLYLTLSSARTLGKDVNKRVTAGSLQQVTGFGDNASGTLMYIYVPKNLATNPGIVVAIHYCTGTAQAYYTGSPYAQLAEQYGFIVIYPQSPYSGTCWDVSSQAALTHNGGGDSNSIANMVTWTISQYNANTAKVFVTGSSSGAMMTNVMAATYPELFAAATVYSGVGAGCFYSSSNQADAWNSSCATGSVISTPAVWGGIAKNMYSGYSGSRPRMQIYHGSADTTLYPQNYYETCKQWAGVFGYNYDSPQSTLANTPDANYQTTNWGPNLQGIYATGVGHTVPIHGAKDMEWFGFSGSGSSSTTTASATKTSTTSTTSTKTTSSTSSTTTSSTGVAAHWGQCGGSGWTGPTVCESGYTCTYSNAWYSQCL |
| Enzyme Length | 382 |
| Uniprot Accession Number | Q8NJP6 |
| Absorption | |
| Active Site | ACT_SITE 152; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Inactivated by phenylmethylsulfonylfluorid (PMSF), a specific inhibitor of serine esterases. {ECO:0000269|PubMed:17008082}. |
| 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:17008082, ECO:0000269|PubMed:8756392}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. {ECO:0000269|PubMed:8756392}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.3. {ECO:0000269|PubMed:8756392}; |
| Pathway | PATHWAY: Glycan degradation; xylan degradation. |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Domain (1); Glycosylation (2); Propeptide (1); Region (3); Sequence conflict (1); Signal peptide (1) |
| Keywords | Carbohydrate metabolism;Cellulose degradation;Cleavage on pair of basic residues;Direct protein sequencing;Glycoprotein;Hydrolase;Polysaccharide degradation;Secreted;Serine esterase;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8756392}. |
| Modified Residue | |
| Post Translational Modification | PTM: Glycosylated. {ECO:0000269|PubMed:17008082}. |
| Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 40,273 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.1.1.72; |