Q6PRW6 · XYN_PENCH
- ProteinEndo-1,4-beta-xylanase
- GeneXyn
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids353 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Cold active 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 5.5.
Temperature Dependence
Optimum temperature is 15 degrees Celsius.
Pathway
Glycan degradation; xylan degradation.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 161 | Proton donor | ||||
Sequence: E | ||||||
Active site | 267 | 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
- EC number
- Short namesXylanase
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Penicillium > Penicillium chrysogenum species complex
Accessions
- Primary accessionQ6PRW6
- Secondary accessions
Subcellular Location
Phenotypes & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | 153 | in strain: A3969.2 | ||||
Sequence: V → L | ||||||
Natural variant | 274 | in strain: A3969.2 | ||||
Sequence: S → T |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 2 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for signal, glycosylation, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-23 | |||||
Sequence: MIPNITQLKTAALVMLFAGQALS | ||||||
Glycosylation | 4 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Chain | PRO_0000429663 | 24-353 | Endo-1,4-beta-xylanase | |||
Sequence: GPVESRQASESIDAKFKAHGKKYLGNIADQGTLNGNPKTPAIIKANFGQLSPENSMKWDATEPSQGQFSFAGSDYFVEFAETNGKLIRGHTLVWHSQLPSWVSSITDKTTLTDVMKNHITTVMKQYKGKVYAWDVVNEIFEEDGTLRDSVFSRVLGEDFVRIAFETAREADPEAKLYINDYNLDSATSAKLQGMVSHVKKWIAAGVPIDGIGSQTHLGAGAGAAASGALNALASAGTEEVAVTELDIAGASSTDYVDVVNACLDQPKCVGITVWGVADPDSWRADESPLLFDASYNPKEAYNVSQLLSRQHAFDLYLKLGNLLLSRLHSD | ||||||
Disulfide bond | 285↔291 | |||||
Sequence: CLDQPKC | ||||||
Glycosylation | 325 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
PTM databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 50-330 | GH10 | ||||
Sequence: IADQGTLNGNPKTPAIIKANFGQLSPENSMKWDATEPSQGQFSFAGSDYFVEFAETNGKLIRGHTLVWHSQLPSWVSSITDKTTLTDVMKNHITTVMKQYKGKVYAWDVVNEIFEEDGTLRDSVFSRVLGEDFVRIAFETAREADPEAKLYINDYNLDSATSAKLQGMVSHVKKWIAAGVPIDGIGSQTHLGAGAGAAASGALNALASAGTEEVAVTELDIAGASSTDYVDVVNACLDQPKCVGITVWGVADPDSWRADESPLLFDASYNPKEAYNVSQLL |
Sequence similarities
Belongs to the glycosyl hydrolase 10 (cellulase F) family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length353
- Mass (Da)38,165
- Last updated2004-07-05 v1
- Checksum8C40976394FABD8E