Detail Information for IndEnz0004000110
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