| IED ID | IndEnz0004000175 |
| Enzyme Type ID | xylanase000175 |
| Protein Name |
Endo-1,4-beta-xylanase 11A Xylanase 11A EC 3.2.1.8 1,4-beta-D-xylan xylanohydrolase 11A |
| Gene Name | XYN11A UMAG_06350 |
| Organism | Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Basidiomycota Ustilaginomycotina Ustilaginomycetes Ustilaginales Ustilaginaceae Ustilago Ustilago maydis (Corn smut fungus) Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus) |
| Enzyme Sequence | MKFATVLAFATAAGAAFASPLASSETTEAGQLSKRQSINYVQNYNGNAANFKYDQHAGTYSTRWTNPPDFVVGLGWSPGNSYRTIKFSGSYSSSSSSYSAVYGWLNNPLTEYYVVENYSYDPCSNSGAQVVGSVTSDGSNYKICKHTQYDQPSIQGTKTFGQYFSVRANKRNSGSVTLSKHFNAWKQHGFANGAANPDFNYQVFATEAFGGTGSASMSVSG |
| Enzyme Length | 221 |
| Uniprot Accession Number | Q4P0L3 |
| Absorption | |
| Active Site | ACT_SITE 111; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10062; ACT_SITE 207; /note=Proton donor; /evidence=ECO:0000250 |
| 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; Evidence={ECO:0000269|PubMed:23889751}; |
| 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. {ECO:0000269|PubMed:23889751}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Glycan degradation; xylan degradation. |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Domain (1); Glycosylation (1); Signal peptide (1) |
| Keywords | Carbohydrate metabolism;Glycoprotein;Glycosidase;Hydrolase;Polysaccharide degradation;Reference proteome;Secreted;Signal;Xylan degradation |
| Interact With | |
| Induction | INDUCTION: Induced in presence of Zea mays leaves and by xylan, and repressed by glucose. SNF1 acts as a positive regulator through the release of glucose repression. {ECO:0000269|PubMed:10882531, ECO:0000269|PubMed:21062173}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22300648, ECO:0000269|PubMed:23889751}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 23,813 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.8; |