| IED ID | IndEnz0012000002 |
| Enzyme Type ID | hemicellulase000002 |
| Protein Name |
Endo-1,4-beta-xylanase A Xylanase A EC 3.2.1.8 1,4-beta-D-xylan xylanohydrolase A Endo-1,4-beta-xylanase I Xylanase I |
| Gene Name | xynA |
| Organism | Aspergillus niger |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Circumdati Aspergillus niger |
| Enzyme Sequence | MKVTAAFAGLLVTAFAAPVPEPVLVSRSAGINYVQNYNGNLGDFTYDESAGTFSMYWEDGVSSDFVVGLGWTTGSSKAITYSAEYSASGSSSYLAVYGWVNYPQAEYYIVEDYGDYNPCSSATSLGTVYSDGSTYQVCTDTRTNEPSITGTSTFTQYFSVRESTRTSGTVTVANHFNFWAQHGFGNSDFNYQVMAVEAWSGAGSASVTISS |
| Enzyme Length | 211 |
| Uniprot Accession Number | P55329 |
| Absorption | |
| Active Site | ACT_SITE 106; /note=Nucleophile; ACT_SITE 197; /note=Proton donor |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.; EC=3.2.1.8; |
| DNA Binding | |
| EC Number | 3.2.1.8 |
| Enzyme Function | FUNCTION: Endo-1,4-beta-xylanase 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. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 3.0.; |
| Pathway | PATHWAY: Glycan degradation; xylan degradation. |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (14); Chain (1); Disulfide bond (1); Domain (1); Helix (3); Signal peptide (1); Turn (3) |
| Keywords | 3D-structure;Carbohydrate metabolism;Disulfide bond;Glycosidase;Hydrolase;Polysaccharide degradation;Secreted;Signal;Xylan degradation |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..27 |
| Structure 3D | X-ray crystallography (4) |
| Cross Reference PDB | 1T6G; 1UKR; 2QZ2; 6QE8; |
| Mapped Pubmed ID | 15166216; 17983355; 31263766; |
| Motif | |
| Gene Encoded By | |
| Mass | 22,642 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.8; |