D7EZJ3 · XYNB_STRSQ
- ProteinEndo-1,4-beta-xylanase B
- GenexynBS9
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids340 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
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.
Catalytic activity
Activity regulation
Is inhibited by Ag+ and Hg2+ in vitro. EDTA and other metal cations such as Na+, K+, Ca2+, Cu2+, Mg2+, Fe3+, and Zn2+ have no effect on catalytic activity.
Kinetics
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
3741 μmol/min/mg | 6.5 | 60 | with oat spelt xylan as substrate | ||
2320 μmol/min/mg | 6.5 | 60 | with birchwood xylan as substrate |
pH Dependence
Optimum pH is 6-7.
Temperature Dependence
Optimum temperature is 60 degrees Celsius.
Pathway
Glycan degradation; xylan degradation.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 138 | Nucleophile | ||||
Sequence: E | ||||||
Active site | 227 | Proton donor | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | endo-1,4-beta-xylanase activity | |
Molecular Function | polysaccharide binding | |
Biological Process | xylan catabolic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameEndo-1,4-beta-xylanase B
- EC number
- Short namesXylanase B
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Kitasatosporales > Streptomycetaceae > Streptomyces
Accessions
- Primary accessionD7EZJ3
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-52 | |||||
Sequence: MHDAPAQRKRRRPGRIGPLPRSSRFARLKLLIASACAALLATLALPPGAAHA | ||||||
Chain | PRO_0000424417 | 53-340 | Endo-1,4-beta-xylanase B | |||
Sequence: QTVTSNQTGNHNGYFYSFWTDAPGTVSATMGSGGNYSTSWRNTGNFVIGKGWSTGGRRTVTYSGSFNPSGNAYLTLYGWSRNPLVEYYIVDNWGTYRPTGTFKGTVTTDGGTYDIYQTTRYNAPSIEGNKTFNQYWSVRQQKRTGGTITTGNHFDAWARAGMQLGSHDYMIMATEGYQSSGSSNITVGGTSGGGGGGGGGGGCTATLSAGERWDDRYNLNVSVSGSSNWTVTMNVPSPATILSTWNITATWPSSQVLVARPNGSGNNFGVTIKHNGNWTWPTVSCSTG |
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-20 | Disordered | ||||
Sequence: MHDAPAQRKRRRPGRIGPLP | ||||||
Domain | 54-239 | GH11 | ||||
Sequence: TVTSNQTGNHNGYFYSFWTDAPGTVSATMGSGGNYSTSWRNTGNFVIGKGWSTGGRRTVTYSGSFNPSGNAYLTLYGWSRNPLVEYYIVDNWGTYRPTGTFKGTVTTDGGTYDIYQTTRYNAPSIEGNKTFNQYWSVRQQKRTGGTITTGNHFDAWARAGMQLGSHDYMIMATEGYQSSGSSNITV | ||||||
Domain | 248-340 | CBM2 | ||||
Sequence: GGGGGGGCTATLSAGERWDDRYNLNVSVSGSSNWTVTMNVPSPATILSTWNITATWPSSQVLVARPNGSGNNFGVTIKHNGNWTWPTVSCSTG |
Sequence similarities
Belongs to the glycosyl hydrolase 11 (cellulase G) family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length340
- Mass (Da)36,245
- Last updated2010-08-10 v1
- Checksum84EBAF44059CCCB3