Detail Information for IndEnz0008000427
IED ID IndEnz0008000427
Enzyme Type ID cellulase000427
Protein Name Endo-1,4-beta-xylanase 2
Xylanase 2
EC 3.2.1.8
1,4-beta-D-xylan xylanohydrolase 2
Gene Name xyn2
Organism Humicola grisea var. thermoidea
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Sordariomycetidae Sordariales Chaetomiaceae Trichocladium Trichocladium griseum Humicola grisea var. thermoidea
Enzyme Sequence MVSIKSVLAAATAVSSALAAPFDFVPRDNSTALQARQVTPNAEGWHNGYFYSWWSDGGGQVQYTNLEGSRYQVRWRNTGNFVGGKGWNPGTGRTINYGGYFNPQGNGYLAVYGWTRNPLVEYYVIESYGTYNPGSQAQYKGTFYTDGDQYDIFVSTRYNQPSIDGTRTFQQYWSIRKNKRVGGSVNMQNHFNAWQQHGMPLGQHYYQIVATEGYQSSGESDIYVQTH
Enzyme Length 227
Uniprot Accession Number Q9HGE1
Absorption
Active Site ACT_SITE 121; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10062; ACT_SITE 212; /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; Evidence={ECO:0000269|PubMed:11849507};
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|PubMed:11849507}.
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;Direct protein sequencing;Glycoprotein;Glycosidase;Hydrolase;Polysaccharide degradation;Secreted;Signal;Xylan degradation
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11849507}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..36; /evidence=ECO:0000269|PubMed:11849507
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 25,615
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda