| IED ID | IndEnz0004000064 |
| Enzyme Type ID | xylanase000064 |
| Protein Name |
Endo-1,4-beta-xylanase B Xylanase B EC 3.2.1.8 1,4-beta-D-xylan xylanohydrolase B |
| Gene Name | xlnB |
| Organism | Streptomyces lividans |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Streptomycetales Streptomycetaceae Streptomyces Streptomyces lividans |
| Enzyme Sequence | MNLLVQPRRRRRGPVTLLVRSAWAVALAALAALMLPGTAQADTVVTTNQEGTNNGYYYSFWTDSQGTVSMNMGSGGQYSTSWRNTGNFVAGKGWANGGRRTVQYSGSFNPSGNAYLALYGWTSNPLVEYYIVDNWGTYRPTGEYKGTVTSDGGTYDIYKTTRVNKPSVEGTRTFDQYWSVRQSKRTGGTITTGNHFDAWARAGMPLGNFSYYMIMATEGYQSSGSSSINVGGTGGGDSGGGDNGGGGGGCTATVSAGQKWGDRYNLDVSVSGASDWTVTMNVPSPAKVLSNWNVNASYPSAQTLTARLNGSGNNWGATIQANANWTWPSVSCSAG |
| Enzyme Length | 335 |
| Uniprot Accession Number | P26515 |
| Absorption | |
| Active Site | ACT_SITE 128; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10062; ACT_SITE 218; /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: Contributes to hydrolyze hemicellulose, the major component of plant cell-walls. XLNA and XLNB seem to act sequentially on the substrate to yield xylobiose and xylose as carbon sources. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Glycan degradation; xylan degradation. |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (12); Chain (1); Domain (2); Helix (1); Region (2); Signal peptide (1); Turn (1) |
| Keywords | 3D-structure;Carbohydrate metabolism;Direct protein sequencing;Glycosidase;Hydrolase;Polysaccharide degradation;Secreted;Signal;Xylan degradation |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..41; /evidence=ECO:0000269|PubMed:1743521 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 5EJ3; |
| Mapped Pubmed ID | 27387012; |
| Motif | |
| Gene Encoded By | |
| Mass | 35,575 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |