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 |