P12614 (BGLS_AGRSA) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 31, 2011.
Version 65.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Beta-glucosidase EC=3.2.1.21 Alternative name(s): Amygdalase Beta-D-glucoside glucohydrolase Cellobiase Gentiobiase | ||
| Gene names |
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| Organism | Agrobacterium sp. (strain ATCC 21400) | ||
| Taxonomic identifier | 74562 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Rhizobium/Agrobacterium group › Agrobacterium |
Protein attributes
| Sequence length | 459 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Catalytic activity | Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose. |
| Sequence similarities | Belongs to the glycosyl hydrolase 1 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Carbohydrate metabolism Cellulose degradation Polysaccharide degradation |
| Molecular function | Glycosidase Hydrolase |
| 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 cation bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "Structure and transcription analysis of the gene encoding a cellobiase from Agrobacterium sp. strain ATCC 21400." Wakarchuk W.W., Greenberg N.M., Kilburn D.G., Miller R.C. Jr., Warren R.A.J. J. Bacteriol. 170:301-307(1988) [PubMed: 2826395] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Unequivocal demonstration of the involvement of a glutamate residue as a nucleophile in the mechanism of a 'retaining' glycosidase." Withers S.G., Warren R.A.J., Street I.P., Rupitz K., Kempton J.B., Aebersold R. J. Am. Chem. Soc. 112:5887-5889(1990) Cited for: ACTIVE SITE GLU-359. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | M19033 Genomic DNA. Translation: AAA22085.1. |
| PIR | GLAG. A28673. |
3D structure databases | |
| ProteinModelPortal | P12614. |
| ModBase | Search... |
Protein family/group databases | |
| CAZy | GH1. Glycoside Hydrolase Family 1. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| InterPro | IPR001360. Glyco_hydro_1. IPR018120. Glyco_hydro_1_AS. IPR017736. Glyco_hydro_1_beta-glucosidase. IPR013781. Glyco_hydro_subgr_catalytic. IPR017853. Glycoside_hydrolase_SF. [Graphical view] |
| Gene3D | G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit. |
| PANTHER | PTHR10353. Glyco_hydro_1. 1 hit. |
| Pfam | PF00232. Glyco_hydro_1. 1 hit. [Graphical view] |
| PRINTS | PR00131. GLHYDRLASE1. |
| SUPFAM | SSF51445. Glyco_hydro_cat. 1 hit. |
| TIGRFAMs | TIGR03356. BGL. 1 hit. |
| PROSITE | PS00572. GLYCOSYL_HYDROL_F1_1. 1 hit. PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | BGLS_AGRSA | ||||||||
| Accession | Primary (citable) accession number: P12614 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Glycosyl hydrolases Classification of glycosyl hydrolase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

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