Q9HEZ1 · XYNA_PHACH
- ProteinEndo-1,4-beta-xylanase A
- GenexynA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids408 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
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.
Catalytic activity
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
3.2 mg/ml | birchwood xylan |
pH Dependence
Optimum pH is 4.5.
Temperature Dependence
Optimum temperature is 70 degrees Celsius.
Pathway
Glycan degradation; xylan degradation.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 222 | Proton donor | ||||
Sequence: E | ||||||
Active site | 327 | Nucleophile | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | cellulose binding | |
Molecular Function | endo-1,4-beta-xylanase activity | |
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 A
- EC number
- Short namesXylanase A
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Basidiomycota > Agaricomycotina > Agaricomycetes > Polyporales > Phanerochaetaceae > Phanerodontia
Accessions
- Primary accessionQ9HEZ1
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-19 | |||||
Sequence: MKLSASFAALALLLPFVQA | ||||||
Chain | PRO_5000419219 | 20-408 | Endo-1,4-beta-xylanase A | |||
Sequence: QSPVWGQCGGIGWTGPTTCTAGNVCQEYSAYYSQCIPASQATSVTSVSTAPNPPPTSHTSTSSAPSGASTSTAKLNTLAKAKGKLYFGTATDNGELSDTAYTAILDDNTMFGQITPANSMKWDATEPQQGQFTFSGGDQIANLAKSNGMLLRGHNCVWYNQLPSWVSNGKFTAAQLTSIIQNHCSTLVTHYKGQVYAWDVVNEPFNDDGSWRTDVFYNTLGTSYVQIALEAARAADPDAKLYINEYNIEYAGAKATSLLNLVKTLKAASVPLDGIGFQSHFIVGQVPTGLQSQLTTFAAQGVEVAITELDIRMTLPSTPALLAQQKTDYSNVIKACASVEACVGVTVWDWTDKYSWVPNTFSGQGAACPWDQNFVRKPAYDGIAIGFGN | ||||||
Disulfide bond | 355↔361 | |||||
Sequence: CASVEAC |
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 20-55 | CBM1 | ||||
Sequence: QSPVWGQCGGIGWTGPTTCTAGNVCQEYSAYYSQCI | ||||||
Region | 64-89 | Disordered | ||||
Sequence: TSVSTAPNPPPTSHTSTSSAPSGAST | ||||||
Domain | 88-405 | GH10 | ||||
Sequence: STSTAKLNTLAKAKGKLYFGTATDNGELSDTAYTAILDDNTMFGQITPANSMKWDATEPQQGQFTFSGGDQIANLAKSNGMLLRGHNCVWYNQLPSWVSNGKFTAAQLTSIIQNHCSTLVTHYKGQVYAWDVVNEPFNDDGSWRTDVFYNTLGTSYVQIALEAARAADPDAKLYINEYNIEYAGAKATSLLNLVKTLKAASVPLDGIGFQSHFIVGQVPTGLQSQLTTFAAQGVEVAITELDIRMTLPSTPALLAQQKTDYSNVIKACASVEACVGVTVWDWTDKYSWVPNTFSGQGAACPWDQNFVRKPAYDGIAIG |
Sequence similarities
Belongs to the glycosyl hydrolase 10 (cellulase F) family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length408
- Mass (Da)43,571
- Last updated2001-03-01 v1
- Checksum4BD5FBD22F6666A0