Detail Information for IndEnz0004000157
IED ID IndEnz0004000157
Enzyme Type ID xylanase000157
Protein Name Endo-1,4-beta-xylanase 2
Xylanase 2
EC 3.2.1.8
1,4-beta-D-xylan xylanohydrolase 2
Gene Name xyl2
Organism Claviceps purpurea (Ergot fungus) (Sphacelia segetum)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Hypocreomycetidae Hypocreales Clavicipitaceae Claviceps Claviceps purpurea (Ergot fungus) (Sphacelia segetum)
Enzyme Sequence MLYTSIFAAAMAASGAMAAPTTSHGASNCTTLDSFFKSHGKLYWGTAADKNTLMKPGVADFIAKEFGQVTPENSMKFDATEPSRGQFHFDAADYLVDYAEKHDLLIRGHTFLWWSQMPAWVKAIKDKDTLIDVIQTHISTVAGRYKGKIYAWDVVNEIFEQDGSFRKTVYYNLLGEDYVRIAFEAAHKADPKAKLYINDFNLDDPNAAKLKAMIKYVTKWRAAGWPVHGIGSQSHLFAGMGEKSAAAIKMLGAAADEVAITELDITGAPQADYEAVTKGCIDVKNCVGITSWGARDTDSWLASKSPLLFDGNFKPKAAVKAIMAI
Enzyme Length 325
Uniprot Accession Number O74717
Absorption
Active Site ACT_SITE 157; /note=Proton donor; /evidence=ECO:0000250; ACT_SITE 262; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10061
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); Disulfide bond (1); Domain (1); Glycosylation (1); Signal peptide (1)
Keywords Carbohydrate metabolism;Disulfide bond;Glycoprotein;Glycosidase;Hydrolase;Polysaccharide degradation;Secreted;Signal;Xylan degradation
Interact With
Induction INDUCTION: Expressed throughout the entire infection process during in infection of rye tissue. {ECO:0000269|PubMed:18944813}.
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18944813}.
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 35,603
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda