A0A4Q4ZFG6 · A0A4Q4ZFG6_9PEZI
- ProteinAlpha-glucuronidase
- GeneaguA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids839 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
Function
function
Alpha-glucuronidase 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. Releases 4-O-methylglucuronic acid from xylan.
Catalytic activity
- an alpha-D-glucuronoside + H2O = an alcohol + D-glucuronate
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 299 | Proton donor | ||||
Sequence: E | ||||||
Active site | 378 | Proton acceptor | ||||
Sequence: D | ||||||
Active site | 406 | Proton acceptor | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | alpha-glucuronidase activity | |
Biological Process | xylan catabolic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAlpha-glucuronidase
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Xylariomycetidae > Xylariales > Xylariales incertae sedis > Monosporascus
Accessions
- Primary accessionA0A4Q4ZFG6
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-15 | |||||
Sequence: MRAIWILASLGLVTA | ||||||
Chain | PRO_5021019592 | 16-839 | Alpha-glucuronidase | |||
Sequence: EDGLNGWLRYARLPSGMLRHAKVLTNIIALNTSEVSPVFTAGKELQKGIQGVLGQKLEVTHEGLHDRQAKSSILVGTIEAYAETGSASDIPELEEDGFWLNTEGDGVEIVGQNERGALYGAFEYLSMIAQGNFSEVAYATNPSAPIRWVNQWDNMDGTIERGYAGLSIFFENNITVSNLTRVYEYARLLSSIRVNGIIVNNVNANPILLSPENMAGLGRIADAMRPWGIQIGVSLNFASPQTLGGLGTYDPFDESVIAWWTDITDKLYEHVPDMVGYLVKANSEGQPGPLTYNRTLADGANLFAKALQPYGGIVMFRAFVYDHHLSHENWYNDRANGQMEFFKDLDGAFEDNVVIQIKYGPMDFQVREPPSPLFAHLPNTASAIELQVSQEYYGQQCHLVYIPPLWRTILDYDLRVGGQKSVIGTDILSGKTFNKKLSGYAAVVNVGLNTTWLGTHLAMSNLYAYGRLAWDPTNDDVRMLQDWTRLTFGFDETVLETITKMSMVSWPAYENYTGNLGIQTLTDITGPHYGPNPASHDGNGWGMWTRANEHSIGMDRTVWNGTRNAGHYPPEIAAMYEKVETTPDELLLWFHHVPYTQRLKNGNTVIQHFYDAHYAGAETAFGFPAQWAALEGKIDRQRFEETLFRLEYQAGHAIVWRDAINQFYFNKSSIPDAHGRVGNYPWRVEAEDMELDGYRVTAVTPFEAASGLRIVQTVDNSTAASVRATLDFPAGVYDLAVAYYDLYEGQASYELSLNNRSLGTWVGDLENRLGYTLTRGIDGHSATRITFRDVEIQKGDVVRIETQPHGRETAPLDYIAVLPKGVVE |
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 21-139 | Alpha glucuronidase N-terminal | ||||
Sequence: GWLRYARLPSGMLRHAKVLTNIIALNTSEVSPVFTAGKELQKGIQGVLGQKLEVTHEGLHDRQAKSSILVGTIEAYAETGSASDIPELEEDGFWLNTEGDGVEIVGQNERGALYGAFEY | ||||||
Domain | 146-467 | Glycosyl hydrolase family 67 catalytic | ||||
Sequence: GNFSEVAYATNPSAPIRWVNQWDNMDGTIERGYAGLSIFFENNITVSNLTRVYEYARLLSSIRVNGIIVNNVNANPILLSPENMAGLGRIADAMRPWGIQIGVSLNFASPQTLGGLGTYDPFDESVIAWWTDITDKLYEHVPDMVGYLVKANSEGQPGPLTYNRTLADGANLFAKALQPYGGIVMFRAFVYDHHLSHENWYNDRANGQMEFFKDLDGAFEDNVVIQIKYGPMDFQVREPPSPLFAHLPNTASAIELQVSQEYYGQQCHLVYIPPLWRTILDYDLRVGGQKSVIGTDILSGKTFNKKLSGYAAVVNVGLNTTW | ||||||
Domain | 469-691 | Glycosyl hydrolase family 67 C-terminal | ||||
Sequence: GTHLAMSNLYAYGRLAWDPTNDDVRMLQDWTRLTFGFDETVLETITKMSMVSWPAYENYTGNLGIQTLTDITGPHYGPNPASHDGNGWGMWTRANEHSIGMDRTVWNGTRNAGHYPPEIAAMYEKVETTPDELLLWFHHVPYTQRLKNGNTVIQHFYDAHYAGAETAFGFPAQWAALEGKIDRQRFEETLFRLEYQAGHAIVWRDAINQFYFNKSSIPDAHGR |
Sequence similarities
Belongs to the glycosyl hydrolase 67 family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length839
- Mass (Da)93,578
- Last updated2019-07-31 v1
- Checksum9B6DB1B6BB5C25AE
Keywords
- Technical term