Detail Information for IndEnz0004000219
IED ID IndEnz0004000219
Enzyme Type ID xylanase000219
Protein Name Probable 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 xynG xynG1 AO090001000111
Organism Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Circumdati Aspergillus oryzae (Yellow koji mold) Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Enzyme Sequence MVSFSSLLLAVSAVSGALAAPGDSTLVELAKRAITSSETGTNNGYYYSFWTNGGGDVEYTNGNGGQYSVKWTNCDNFVAGKGWNPGSAKTVTYSGEWESNSNSYVSLYGWTQNPLVEYYIVDKYGDYDPSTGATELGTVESDGGTYKIYKTTRENAPSIEGTSTFNQYWSVRQSGRVGGTITAQNHFDAWANVGLQLGTHNYMILATEGYKSSGSATITVE
Enzyme Length 221
Uniprot Accession Number P87037
Absorption
Active Site ACT_SITE 117; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10062; ACT_SITE 208; /note=Proton donor; /evidence=ECO:0000250
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); 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:0000269|PubMed:16672490}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..19; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 23,746
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda