Detail Information for IndEnz0004000172
IED ID IndEnz0004000172
Enzyme Type ID xylanase000172
Protein Name Endo-1,4-beta-xylanase B
Xylanase B
EC 3.2.1.8
1,4-beta-D-xylan xylanohydrolase B
Endo-1,4-beta-xylanase G1
Xylanase G1
Gene Name xlnB xynB xynG1 AKAW_10131
Organism Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus awamori var. kawachi)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus kawachii (White koji mold) (Aspergillus awamori var. kawachi) Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus awamori var. kawachi)
Enzyme Sequence MLTKNLLLCFAAAKAVLAVPHDSVVERSDALHKLSERSTPSSTGENNGYYYSFWTDGGGDVTYTNGNAGSYSVEWSNVGNFVGGKGWNPGSAKDITYSGTFTPSGNGYLSVYGWTTDPLIEYYIVESYGDYNPGSGGTYKGTVTSDGSVYDIYTATRTNAPSIQGTATFTQYWSVRQNKRVGGTVTTSNHFNAWAKLGMNLGTHNYQILATEGYQSSGSSSITIQ
Enzyme Length 225
Uniprot Accession Number P48824
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;
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); Sequence conflict (3); Signal peptide (1)
Keywords Carbohydrate metabolism;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 24,182
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda