Reviewed,
UniProtKB/Swiss-Prot P29090 (BGL3_ASPWE)
Last modified
June 16, 2009.
Version 37.
History...
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Beta-glucosidase A-3 EC=3.2.1.21 Alternative name(s): Gentiobiase Cellobiase Beta-D-glucoside glucohydrolase |
| Organism | Aspergillus wentii |
| Taxonomic identifier | 5066 [NCBI] |
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus |
Protein attributes
| Sequence length | 63 AA. |
| Sequence status | Fragment. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Catalytic activity | Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose. |
| Pathway | |
| Sequence similarities | Belongs to the glycosyl hydrolase 3 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Carbohydrate metabolism Cellulose degradation Polysaccharide degradation |
| Molecular function | Glycosidase Hydrolase |
| PTM | Glycoprotein |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | cellulose catabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | beta-glucosidase activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | ‹1 – ›63 | ›63 | Beta-glucosidase A-3 | PRO_0000210776 | |||||
Sites | |||||||||
| Active site | 12 | 1 | |||||||
Amino acid modifications | |||||||||
| Glycosylation | 48 | 1 | N-linked (GlcNAc...) | ||||||
| Glycosylation | 56 | 1 | N-linked (GlcNAc...) | ||||||
Experimental info | |||||||||
| Non-terminal residue | 1 | 1 | |||||||
| Non-terminal residue | 63 | 1 | |||||||
Sequences
References
| [1] | "Isolation and structure of a tryptic glycopeptide from the active site of beta-glucosidase A3 from Aspergillus wentii." Bause E., Legler G. Biochim. Biophys. Acta 626:459-465(1980) [PubMed: 6783081] [Abstract] Cited for: PROTEIN SEQUENCE. |
Cross-references
Sequence databases | |
|---|---|
| PIR | A29171. |
3D structure databases | |
| ModBase | Search... |
Protein family/group databases | |
| CAZy | GH3. Glycoside Hydrolase Family 3. |
Enzyme and pathway databases | |
| BRENDA | 3.2.1.21. 215346. |
Family and domain databases | |
| InterPro | IPR019800. Glyco_hydro_3_AS. IPR001764. Glyco_hydro_3_N. [Graphical view] |
| Pfam | PF00933. Glyco_hydro_3. 1 hit. [Graphical view] |
| PROSITE | PS00775. GLYCOSYL_HYDROL_F3. Partial match. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | BGL3_ASPWE | ||||||||
| Accession | Primary (citable) accession number: P29090 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||
Relevant documents
| Glycosyl hydrolases Classification of glycosyl hydrolase families and list of entries |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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