Detail Information for IndEnz0004000223
IED ID IndEnz0004000223
Enzyme Type ID xylanase000223
Protein Name Endo-1,4-beta-xylanase
Xylanase
EC 3.2.1.8
1,4-beta-D-xylan xylanohydrolase
PVX
Gene Name
Organism Byssochlamys spectabilis (Paecilomyces variotii)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Thermoascaceae Paecilomyces Byssochlamys spectabilis (Paecilomyces variotii)
Enzyme Sequence GTTPNSEGWHDGYYYSWWSDGGGDSTYTNNSGGTYEITWGNGGNLVGGKGWNPGLNARAIHFTGVYQPNGTSYLSVYGWTRNPLVEYYIVENFGSSNPSSGSTDLGTVSCDGSTYTLGQSTRYNAPSIDGTQTFNQYWSVRQDKRSSGTVQTGCHFDAWASAGLNVTGDHYYQIVATEGYFSSGYARITVADVG
Enzyme Length 194
Uniprot Accession Number P81536
Absorption
Active Site ACT_SITE 86; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10062; ACT_SITE 178; /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
Temperature Dependency BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Thermostable.;
PH Dependency
Pathway PATHWAY: Glycan degradation; xylan degradation.
nucleotide Binding
Features Active site (2); Beta strand (13); Chain (1); Disulfide bond (1); Domain (1); Helix (1); Modified residue (1); Turn (2)
Keywords 3D-structure;Acetylation;Carbohydrate metabolism;Direct protein sequencing;Disulfide bond;Glycosidase;Hydrolase;Polysaccharide degradation;Xylan degradation
Interact With
Induction
Subcellular Location
Modified Residue MOD_RES 1; /note=N-acetylglycine; /evidence=ECO:0000269|PubMed:10623548
Post Translational Modification
Signal Peptide
Structure 3D X-ray crystallography (1)
Cross Reference PDB 1PVX;
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 20,947
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda