IED ID | IndEnz0004000110 |
Enzyme Type ID | xylanase000110 |
Protein Name |
Endo-1,4-beta-xylanase 3 Xylanase 3 EC 3.2.1.8 1,4-beta-D-xylan xylanohydrolase 3 |
Gene Name | XYL3 |
Organism | Magnaporthe grisea (Crabgrass-specific blast fungus) (Pyricularia grisea) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Sordariomycetidae Magnaporthales Pyriculariaceae Pyricularia Magnaporthe grisea (Crabgrass-specific blast fungus) (Pyricularia grisea) |
Enzyme Sequence | MQILTWALAALAAIPAVTAAPVETVEASSMDELVERSPNVTLVARGTPSSTGTHNGFYYSHWTDNAGADVTYSMGGGGQFSYTWRNSGNFVGGKGWNPGNAGRVINYSGSYSPQGNSYLAVYGWTRNPLIEYYVVESFGSYNPSSGATNRGSFTSDGSTYDILVSTRYNQPSIDGTKTFQQFWSVRRNKRASGTVTFANHVNAWRNAGLNLGNQWNYQILAVEGYHSSGSASMTVR |
Enzyme Length | 236 |
Uniprot Accession Number | Q92244 |
Absorption | |
Active Site | ACT_SITE 131; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10062; ACT_SITE 223; /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|Ref.2}; |
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|Ref.2}. |
Temperature Dependency | |
PH Dependency | |
Pathway | PATHWAY: Glycan degradation; xylan degradation. |
nucleotide Binding | |
Features | Active site (2); Chain (1); Domain (1); Glycosylation (2); Signal peptide (1) |
Keywords | Carbohydrate metabolism;Direct protein sequencing;Glycoprotein;Glycosidase;Hydrolase;Polysaccharide degradation;Reference proteome;Secreted;Signal;Xylan degradation |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.2}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..45; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 25,555 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |