Detail Information for IndEnz0004000132
IED ID IndEnz0004000132
Enzyme Type ID xylanase000132
Protein Name Endo-1,4-beta-xylanase B
Xylanase B
EC 3.2.1.8
1,4-beta-D-xylan xylanohydrolase B
Gene Name xynB
Organism Talaromyces purpureogenus (Soft rot fungus) (Penicillium purpureogenum)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Trichocomaceae Talaromyces Talaromyces sect. Talaromyces Talaromyces purpureogenus (Soft rot fungus) (Penicillium purpureogenum)
Enzyme Sequence MKVTAAFAGLLATTLAAPATELVTRSINYVQNYNGNLGAFSYNEGAGTFSMYWQQGVSNDFVVGLGRSTGSSNPITYSASYSASGGSYLAVYGWVNSPQAEYHVVEAYGNYNPCSSGSATNLGTVSSDGGTYQVCTDTRVNQPSITGTSTFTQFFSVRQGSRTSGTVTIANHFNFWAKHGFGNSNFNYQVVAVEAWSGTGTASVTVSA
Enzyme Length 208
Uniprot Accession Number Q96W72
Absorption
Active Site ACT_SITE 101; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 194; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10063
Activity Regulation ACTIVITY REGULATION: N-bromosuccinimide completely inhibits the catalytic activity. {ECO:0000269|PubMed:7640003}.
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:12137954, ECO:0000269|PubMed:7640003};
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:7640003}.
Temperature Dependency BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. {ECO:0000269|PubMed:7640003};
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 3.5. {ECO:0000269|PubMed:7640003};
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;Secreted;Signal;Xylan degradation
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12137954}.
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 21,869
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda