| IED ID | IndEnz0004000196 |
| Enzyme Type ID | xylanase000196 |
| Protein Name |
Beta-xylosidase EC 3.2.1.37 1,4-beta-D-xylan xylohydrolase Xylan 1,4-beta-xylosidase |
| Gene Name | Xyl5 |
| Organism | Phanerodontia chrysosporium (White-rot fungus) (Sporotrichum pruinosum) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Basidiomycota Agaricomycotina Agaricomycetes Agaricomycetes incertae sedis Polyporales Phanerochaetaceae Phanerodontia Phanerodontia chrysosporium (White-rot fungus) (Sporotrichum pruinosum) |
| Enzyme Sequence | MAYLKVSGTKIVDKDGNEVILRGAGLGGWMNMENFITGYPGCEFQIRAALADVVGQEKSEFFFDKFLEYFFTDADAAFFKSLGLNCIRLPFNYRHFEDDMNPRVLKPEGFKHLDRVIDICAKHGIYTVLDLHTAPGGQNTDWHSDAGTHIAKFWEHKDFQDRVIWLWEELAQHYRDNTWIAGYNPLNEPTDPYQTRLIAWYDRVYAAIRKHDPHHALFLDGNTFASDFSHFGDAEKRWENTAYAIHDYSVFGFPAAPEPYVSSEAQRRRLRRSYEKKREWMDARGLCVWNGEFGPVYARREYEGDLTDSINEERYRVLKDQLEIYNKDRLSWSIWLYKDIGFQGMVHVSRDTPYMTLFRDFLAKKHRLAIDAWGADDSAVRHVYQPLIDLIKQEVKPEHQELYPAPVWKLSDRVGRLARNILVSEFLVREWAEHFRGKSTEELDAIAKSFAFENCLHRDGLNKVLTDNASLVAQGA |
| Enzyme Length | 476 |
| Uniprot Accession Number | W8QRE4 |
| Absorption | |
| Active Site | ACT_SITE 188; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:Q45070; ACT_SITE 292; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:Q45070 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-xylose residues from the non-reducing termini.; EC=3.2.1.37; Evidence={ECO:0000269|PubMed:25300189}; |
| DNA Binding | |
| EC Number | 3.2.1.37 |
| Enzyme Function | FUNCTION: Catalyzes the hydrolysis of xylo-oligomers to xylose units and plays an important role in xylan degradation. Can also perform the transglycosylation of xylose and alcohol. Has no endoglucanase activity. {ECO:0000269|PubMed:25300189}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. {ECO:0000269|PubMed:25300189}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5. Stable from pH 3 to pH 8. {ECO:0000269|PubMed:25300189}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Glycosylation (1) |
| Keywords | Glycoprotein;Glycosidase;Hydrolase;Secreted |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:25300189}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 55,475 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.37; |