Detail Information for IndEnz0004000079
IED ID IndEnz0004000079
Enzyme Type ID xylanase000079
Protein Name Probable endo-1,4-beta-xylanase A
Xylanase A
EC 3.2.1.8
1,4-beta-D-xylan xylanohydrolase A
Gene Name xlnA AFUB_048130
Organism Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Fumigati Neosartorya fumigata (Aspergillus fumigatus) Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus)
Enzyme Sequence MVSFSYLLLACSAIGALAAPVEPETTSFNETALHEFAERAGTPSSTGWNNGYYYSFWTDGGGDVTYTNGAGGSYSVNWRNVGNFVGGKGWNPGSARTINYGGSFNPSGNGYLAVYGWTTNPLIEYYVVESYGTYNPGSGGTFRGTVNTDGGTYNIYTAVRYNAPSIEGTKTFTQYWSVRTSKRTGGTVTMANHFNAWSRLGMNLGTHNYQIVATEGYQSSGSASITVY
Enzyme Length 228
Uniprot Accession Number B0XXF3
Absorption
Active Site ACT_SITE 124; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10062; ACT_SITE 215; /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;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 24,494
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda