G0RA32 · XYN3_HYPJQ
- ProteinEndo-1,4-beta-xylanase 3
- Genexyn3
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids347 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
Glycoside hydrolase involved in the hydrolysis of xylan, a major plant cell wall hemicellulose made up of 1,4-beta-linked D-xylopyranose residues. Catalyzes the endohydrolysis of the main-chain 1,4-beta-glycosidic bonds connecting the xylose subunits yielding various xylooligosaccharides and xylose. Produces xylobiose and xylotriose as the main degradation products.
Catalytic activity
Pathway
Glycan degradation; xylan degradation.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 176 | Proton donor | ||||
Sequence: E | ||||||
Active site | 282 | 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
Names & Taxonomy
Protein names
- Recommended nameEndo-1,4-beta-xylanase 3
- EC number
- Short namesXylanase 3
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Hypocreales > Hypocreaceae > Trichoderma
Accessions
- Primary accessionG0RA32
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for signal, propeptide, modified residue, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-16 | |||||
Sequence: MKANVILCLLAPLVAA | ||||||
Propeptide | PRO_0000436705 | 17-45 | ||||
Sequence: LPTETIHLDPELAALRANLTERTADLWDR | ||||||
Modified residue | 46 | Pyrrolidone carboxylic acid | ||||
Sequence: Q | ||||||
Chain | PRO_5003408236 | 46-347 | Endo-1,4-beta-xylanase 3 | |||
Sequence: QASQSIDQLIKRKGKLYFGTATDRGLLQREKNAAIIQADLGQVTPENSMKWQSLENNQGQLNWGDADYLVNFAQQNGKSIRGHTLIWHSQLPAWVNNINNADTLRQVIRTHVSTVVGRYKGKIRAWDVVNEIFNEDGTLRSSVFSRLLGEEFVSIAFRAARDADPSARLYINDYNLDRANYGKVNGLKTYVSKWISQGVPIDGIGSQSHLSGGGGSGTLGALQQLATVPVTELAITELDIQGAPTTDYTQVVQACLSVSKCVGITVWGISDKDSWRASTNPLLFDANFNPKPAYNSIVGILQ | ||||||
Disulfide bond | 300↔306 | |||||
Sequence: CLSVSKC |
Post-translational modification
Not glycosylated.
Keywords
- PTM
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 46-345 | GH10 | ||||
Sequence: QASQSIDQLIKRKGKLYFGTATDRGLLQREKNAAIIQADLGQVTPENSMKWQSLENNQGQLNWGDADYLVNFAQQNGKSIRGHTLIWHSQLPAWVNNINNADTLRQVIRTHVSTVVGRYKGKIRAWDVVNEIFNEDGTLRSSVFSRLLGEEFVSIAFRAARDADPSARLYINDYNLDRANYGKVNGLKTYVSKWISQGVPIDGIGSQSHLSGGGGSGTLGALQQLATVPVTELAITELDIQGAPTTDYTQVVQACLSVSKCVGITVWGISDKDSWRASTNPLLFDANFNPKPAYNSIVGI |
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.
- Length347
- Mass (Da)38,076
- Last updated2011-10-19 v1
- Checksum1AD305498D0216CF
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
GL985057 EMBL· GenBank· DDBJ | EGR52056.1 EMBL· GenBank· DDBJ | Genomic DNA |