O94163 · XYNF1_ASPOR
- ProteinEndo-1,4-beta-xylanase F1
- GenexynF1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids327 (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
pH Dependence
Optimum pH is 5.0.
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 | 155 | Proton donor | ||||
Sequence: E | ||||||
Active site | 263 | Nucleophile | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
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 F1
- EC number
- Short namesXylanase F1
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Circumdati
Accessions
- Primary accessionO94163
- Secondary accessions
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-19 | |||||
Sequence: MVHLKALASGTLFASLASS | ||||||
Chain | PRO_0000393191 | 20-327 | Endo-1,4-beta-xylanase F1 | |||
Sequence: AVISRQAAASINDAFVAHGKKYFGTCSDQALLQNSQNEAIVRADFGQLTPENSMKWDALEPSQGSFSFAGADFLADYAKTNNKLVRGHTLVWHSQLPSWVQGITDKDTLTEVIKNHITTIMQRYKGQIYAWDVVNEIFDEDGTLRDSVFSQVLGEDFVRIAFETAREADPNAKLYINDYNLDSADYAKTKGMVSYVKKWLDAGVPIDGIGSQSHYSANGFPVSGAKGALTALASTGVSEVAVTELDIEGASSESYLEVVNACLDVSSCVGITVWGVSDKDSWRSSTSPLLFDSNYQAKDAYNAIIDAL | ||||||
Disulfide bond | 281↔287 | |||||
Sequence: CLDVSSC |
Keywords
- PTM
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 45-326 | GH10 | ||||
Sequence: CSDQALLQNSQNEAIVRADFGQLTPENSMKWDALEPSQGSFSFAGADFLADYAKTNNKLVRGHTLVWHSQLPSWVQGITDKDTLTEVIKNHITTIMQRYKGQIYAWDVVNEIFDEDGTLRDSVFSQVLGEDFVRIAFETAREADPNAKLYINDYNLDSADYAKTKGMVSYVKKWLDAGVPIDGIGSQSHYSANGFPVSGAKGALTALASTGVSEVAVTELDIEGASSESYLEVVNACLDVSSCVGITVWGVSDKDSWRSSTSPLLFDSNYQAKDAYNAIIDA |
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.
- Length327
- Mass (Da)35,402
- Last updated1999-05-01 v1
- Checksum38B2F6374BAD3D0A
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 190 | in Ref. 2; BAE65852 | ||||
Sequence: N → D | ||||||
Sequence conflict | 209 | in Ref. 2; BAE65852 | ||||
Sequence: K → Q |
Keywords
- Technical term