Reviewed,
UniProtKB/Swiss-Prot P96513 (AMYB_BACFI)
Last modified
January 19, 2010.
Version 56.
History...
Clusters with 100%,
90%,
50% identity |
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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-amylase EC=3.2.1.2 Alternative name(s): 1,4-alpha-D-glucan maltohydrolase |
| Organism | Bacillus firmus |
| Taxonomic identifier | 1399 [NCBI] |
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 468 AA. |
| Sequence status | Fragment. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Catalytic activity | Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains. |
| Sequence similarities | Belongs to the glycosyl hydrolase 14 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Carbohydrate metabolism Polysaccharide degradation |
| Domain | Signal |
| Molecular function | Glycosidase Hydrolase |
| PTM | Disulfide bond |
| Gene Ontology (GO) | |
| Biological process | polysaccharide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | beta-amylase activity Inferred from electronic annotation. Source: EC cation bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 36 | 36 | Potential | ||||||||
| Chain | 37 – ›468 | ›432 | Beta-amylase | PRO_0000001455 | |||||||
Sites | |||||||||||
| Active site | 198 | 1 | By similarity | ||||||||
| Active site | 394 | 1 | By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 118 ↔ 126 | By similarity | |||||||||
Experimental info | |||||||||||
| Non-terminal residue | 468 | 1 | |||||||||
Sequences
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References
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AB000264 Genomic DNA. Translation: BAA19075.1. |
3D structure databases | |
| SMR | P96513. Positions 35-466. |
| ModBase | Search... |
Protein family/group databases | |
| CAZy | CBM25. Carbohydrate-Binding Module Family 25. GH14. Glycoside Hydrolase Family 14. |
Enzyme and pathway databases | |
| BRENDA | 3.2.1.2. 20639. |
Family and domain databases | |
| InterPro | IPR001554. Glyco_hydro_14. IPR018238. Glyco_hydro_14_CS. IPR000125. Glyco_hydro_14A_bac. IPR017853. Glyco_hydro_catalytic_core. IPR013781. Glyco_hydro_sg_catalytic. [Graphical view] |
| Gene3D | G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit. |
| Pfam | PF01373. Glyco_hydro_14. 1 hit. [Graphical view] |
| PRINTS | PR00750. BETAAMYLASE. PR00841. GLHYDLASE14A. |
| PROSITE | PS00506. BETA_AMYLASE_1. 1 hit. PS00679. BETA_AMYLASE_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | AMYB_BACFI | ||||||||
| Accession | Primary (citable) accession number: P96513 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
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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