Detail Information for IndEnz0004000116
IED ID IndEnz0004000116
Enzyme Type ID xylanase000116
Protein Name Endo-1,4-beta-xylanase 4
Xylanase 4
EC 3.2.1.8
1,4-beta-D-xylan xylanohydrolase 4
Gene Name XYL4 MGG_08424
Organism Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Pyricularia oryzae)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Sordariomycetidae Magnaporthales Pyriculariaceae Pyricularia Magnaporthe oryzae (Rice blast fungus) (Pyricularia oryzae) Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Pyricularia oryzae)
Enzyme Sequence MVSFTTILVAATAALVAANPVPPSIDEMREIYVKSRDLHARGGTPSSTGTHDGFYYSWWTDNGAQATYTNNAGGSYSITWSGNGNLVGGKGWNPGSARNVTYSANYRPNGNSYLSVYGWTRNPLVEYYVVENFGTYDPSSQASRKGTINVDGATYQVAQSTRTNQPSIDGTRTFQQYWSVRQQKRSSGTVDMKKHFDAWASMGMKLGTHDYQIVATEGYFSSGSSTVTIQR
Enzyme Length 231
Uniprot Accession Number G4NA54
Absorption
Active Site ACT_SITE 126; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10062; ACT_SITE 217; /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. {ECO:0000250}.
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
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
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 25,305
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda