Detail Information for IndEnz0004000073
IED ID IndEnz0004000073
Enzyme Type ID xylanase000073
Protein Name Endo-1,4-beta-xylanase 6
Xylanase 6
EC 3.2.1.8
1,4-beta-D-xylan xylanohydrolase 6
Gene Name XYN6
Organism Aspergillus niger
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 niger
Enzyme Sequence MKVTAAFAGLLVTALAAPAPEPVLVSRSAGINYVQNYNGNLGDFTYDESAGTFSMYWEDGVSSDFVVGLGWTTGSSNPITYSADYSASGSSSYLAVYGWDNYPQAEYYIVEDYGDYNPCSSATSLGTVYSDGSTYQVCTDTRTNEPSITGTSTFTQYFSVRESTRTSGTVTVANHFNFWAQHGFGNSDFNYQVVAVEAWSGAGSASVTISS
Enzyme Length 211
Uniprot Accession Number Q6QJ75
Absorption
Active Site ACT_SITE 106; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10062; ACT_SITE 197; /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, ECO:0000269|Ref.1}.
Temperature Dependency
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 3.5. {ECO:0000269|Ref.1};
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;Secreted;Signal;Xylan degradation
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..16; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 22,561
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda