| IED ID | IndEnz0004000067 |
| Enzyme Type ID | xylanase000067 |
| 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 |
| Organism | Botryotinia fuckeliana (Noble rot fungus) (Botrytis cinerea) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Leotiomycetes Helotiales Sclerotiniaceae Botrytis Botryotinia fuckeliana (Noble rot fungus) (Botrytis cinerea) |
| Enzyme Sequence | MVSASSLLLAASAIAGVFSAPAAAPVSENLNVLQERALTSSATGTSGGYYYSFWTDGSGGVTYSNGANGQYAVSWTGNKGNFVGGKGWAVGSERSISYTGSYKPNGNSYLSVYGWTTSPLIEYYIVEDFGTYDPSSAATEIGSVTSDGSTYKILETTRTNQPSVQGTATFKQYWSVRTSKRTSGTVTTANHFAAWKKLGLTLGSTYNYQIVAVEGYQSSGSASITVS |
| Enzyme Length | 227 |
| Uniprot Accession Number | Q2LMP0 |
| Absorption | |
| Active Site | ACT_SITE 122; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10062; ACT_SITE 214; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10063 |
| 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. Required for planr infection and the appearance of secondary lesions. {ECO:0000269|PubMed:16404950}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Glycan degradation; xylan degradation. |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Domain (1); Signal peptide (1) |
| Keywords | Carbohydrate metabolism;Glycosidase;Hydrolase;Polysaccharide degradation;Secreted;Signal;Virulence;Xylan degradation |
| Interact With | |
| Induction | INDUCTION: Expression is maximal when xylan is the only carbon source, and repressed by glucose. Expression is detected from the beginning of tomato leaves infection in the just-inoculated leaves, and the level sof transcript increased between 24 and 48 hours postinfection simultaneously with the appearance of visible lesions on the leaves. {ECO:0000269|PubMed:16404950}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..19; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 23,824 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.8; |