| IED ID | IndEnz0008000461 |
| Enzyme Type ID | cellulase000461 |
| 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 xynB |
| Organism | Botryotinia fuckeliana (strain B05.10) (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) Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis cinerea) |
| Enzyme Sequence | MVSASSLLLAASAIAGVFSAPAAAPVSENLNVLQERALTSSATGTSGGYYYSFWTDGSGGVTYSNGDNGQYAVSWTGNKGNFVGGKGWAVGSERSISYTGSYKPNGNSYLSVYGWTTFPLIEYYIVEDFGTYDPSSAATEIGSVTSDGSTYKILETTRTNQPSIQGTATFKQYWSVRTSKRTSGTVTTANHFAAWKKLGLTLGSTYDYQIVAVEGYQSGSASITVS |
| Enzyme Length | 226 |
| Uniprot Accession Number | B3VSG7 |
| Absorption | |
| Active Site | ACT_SITE 122; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10062; ACT_SITE 214; /note=Proton donor; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Significantly inhibited by the wheat xylanase inhibiting protein I (XIP-I) and the proteinaceous endoxylanase Triticum aestivum xylanase inhibitors I (TAXI-I), whereas no inhibition is detected with TAXI-II. {ECO:0000269|PubMed:16185656}. |
| 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:16185656}; |
| 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:16185656}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is between 38 and 42 degrees Celsius. {ECO:0000269|PubMed:16185656}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.5-5.0. {ECO:0000269|PubMed:16185656}; |
| Pathway | PATHWAY: Glycan degradation; xylan degradation. |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Domain (1); Signal peptide (1) |
| Keywords | Carbohydrate metabolism;Direct protein sequencing;Glycosidase;Hydrolase;Polysaccharide degradation;Secreted;Signal;Xylan degradation |
| Interact With | |
| Induction | INDUCTION: Shows constitutive expression during the early stage of tobacco leaves infection. {ECO:0000269|PubMed:16185656}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16185656}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..36; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 23,856 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=10 mg/ml for low viscosity xylan {ECO:0000269|PubMed:16185656}; Vmax=0.5 umol/min/mg enzyme toward xylose {ECO:0000269|PubMed:16185656}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |