IED ID | IndEnz0008000472 |
Enzyme Type ID | cellulase000472 |
Protein Name |
Endo-1,4-beta-xylanase B Xylanase B EC 3.2.1.8 |
Gene Name | xynBS9 |
Organism | Streptomyces sp. |
Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Streptomycetales Streptomycetaceae Streptomyces unclassified Streptomyces Streptomyces sp. |
Enzyme Sequence | MHDAPAQRKRRRPGRIGPLPRSSRFARLKLLIASACAALLATLALPPGAAHAQTVTSNQTGNHNGYFYSFWTDAPGTVSATMGSGGNYSTSWRNTGNFVIGKGWSTGGRRTVTYSGSFNPSGNAYLTLYGWSRNPLVEYYIVDNWGTYRPTGTFKGTVTTDGGTYDIYQTTRYNAPSIEGNKTFNQYWSVRQQKRTGGTITTGNHFDAWARAGMQLGSHDYMIMATEGYQSSGSSNITVGGTSGGGGGGGGGGGCTATLSAGERWDDRYNLNVSVSGSSNWTVTMNVPSPATILSTWNITATWPSSQVLVARPNGSGNNFGVTIKHNGNWTWPTVSCSTG |
Enzyme Length | 340 |
Uniprot Accession Number | D7EZJ3 |
Absorption | |
Active Site | ACT_SITE 138; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10062; ACT_SITE 227; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10063 |
Activity Regulation | ACTIVITY REGULATION: Is inhibited by Ag(+) and Hg(2+) in vitro. EDTA and other metal cations such as Na(+), K(+), Ca(2+), Cu(2+), Mg(2+), Fe(3+), and Zn(2+) have no effect on catalytic activity. {ECO:0000269|Ref.1}. |
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|Ref.1}; |
DNA Binding | |
EC Number | 3.2.1.8 |
Enzyme Function | FUNCTION: Endo-acting xylanase which specifically cleaves internal linkages on the xylan backbone, releasing xylooligosaccharides. Is able to hydrolyze oat spelt xylan and birchwood xylan, releasing xylobiose and xylotriose as the major products. {ECO:0000269|Ref.1}. |
Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 60 degrees Celsius. {ECO:0000269|Ref.1}; |
PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6-7. {ECO:0000269|Ref.1}; |
Pathway | PATHWAY: Glycan degradation; xylan degradation. |
nucleotide Binding | |
Features | Active site (2); Chain (1); Domain (2); Region (1); Signal peptide (1) |
Keywords | Carbohydrate metabolism;Glycosidase;Hydrolase;Polysaccharide degradation;Secreted;Signal;Xylan degradation |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..52; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 36,245 |
Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=3741 umol/min/mg enzyme with oat spelt xylan as substrate (at pH 6.5 and 60 degrees Celsius) {ECO:0000269|Ref.1}; Vmax=2320 umol/min/mg enzyme with birchwood xylan as substrate (at pH 6.5 and 60 degrees Celsius) {ECO:0000269|Ref.1}; |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |