Reviewed,
UniProtKB/Swiss-Prot Q9R9H8 (BBMA2_BACSU)
Last modified
June 16, 2009.
Version 41.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Intracellular maltogenic amylase EC=3.2.1.- | ||
| Gene names |
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| Organism | Bacillus subtilis | ||
| Taxonomic identifier | 1423 [NCBI] | ||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 588 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Hydrolyzes beta-cyclodextrin to maltose and glucose, soluble starch to maltose and glucose, and pullulan to panose with trace amounts of maltose and glucose. It is also able to hydrolyze acarbose. Can also exhibit a transglycosylation activity transferring glucose or maltose to another moiety of sugars by forming alpha-(1,6)- and alpha-(1,3)-glycosidic linkages upon the hydrolysis of substrate at concentrations of 5% or higher. Ref.1 |
| Subunit structure | Monomer or homodimer; in equilibrium. Ref.1 |
| Subcellular location | |
| Sequence similarities | Belongs to the glycosyl hydrolase 13 family. BbmA subfamily. |
| biophysicochemical properties | pH dependence: Optimum pH is 7.0. Stable at pH 6.0 and about 80% of the enzyme activity remained between pH 7.0 and pH 8.0. Temperature dependence: Optimum temperature is 40-45 degrees Celsius. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Carbohydrate metabolism |
| Cellular component | Cytoplasm |
| Molecular function | Glycosidase Hydrolase |
| Gene Ontology (GO) | |
| Biological process | carbohydrate metabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | cation binding Inferred from electronic annotation. Source: InterPro hydrolase activity, acting on glycosyl bondsInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "Molecular characterization of a dimeric intracellular maltogenic amylase of Bacillus subtilis SUH4-2." Cho H.-Y., Kim Y.-W., Kim T.-J., Lee H.-S., Kim D.-Y., Kim J.-W., Lee Y.-W., Leed S.-B., Park K.-H. Biochim. Biophys. Acta 1478:333-340(2000) [PubMed: 10825545] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, SUBUNIT. Strain: SUH4-2. |
Cross-references
Sequence databases | |
|---|---|
| AF115340 Genomic DNA. Translation: AAF23874.1. Different initiation. | |
3D structure databases | |
| HSSP | HSSP built from PDB template 1SMA based on UniProtKB O69007. |
| ModBase | Search... |
Protein family/group databases | |
| CAZy | CBM34. Carbohydrate-Binding Module Family 34. GH13. Glycoside Hydrolase Family 13. |
Family and domain databases | |
| InterPro | IPR006047. Glyco_hydro_13_cat. IPR006589. Glyco_hydro_13_sub_cat. IPR013781. Glyco_hydro_sg_catalytic. IPR013783. Ig-like_fold. [Graphical view] |
| Gene3D | G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit. G3DSA:2.60.40.10. Ig-like_fold. 1 hit. |
| Pfam | PF00128. Alpha-amylase. 1 hit. [Graphical view] |
| SMART | SM00642. Aamy. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | BBMA2_BACSU | ||||||||
| Accession | Primary (citable) accession number: Q9R9H8 | ||||||||
| Entry history |
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| 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 |

Clusters with


