P29094 (O16G_BACTR) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 74.
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: Oligo-1,6-glucosidase EC=3.2.1.10 Alternative name(s): Dextrin 6-alpha-D-glucanohydrolase Oligosaccharide alpha-1,6-glucosidase Sucrase-isomaltase Short name=Isomaltase | ||
| Gene names |
| ||
| Organism | Bacillus thermoglucosidasius (Geobacillus thermoglucosidasius) | ||
| Taxonomic identifier | 1426 [NCBI] | ||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Geobacillus![]() |
Protein attributes
| Sequence length | 562 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Catalytic activity | Hydrolysis of (1->6)-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by alpha-amylase, and in isomaltose. |
| Subcellular location | |
| Sequence similarities | Belongs to the glycosyl hydrolase 13 family. |
| Biophysicochemical properties | Temperature dependence: Extremely thermostable. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Molecular function | Glycosidase Hydrolase |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological_process | carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | cation binding Inferred from electronic annotation. Source: InterPro oligo-1,6-glucosidase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
| ||||||||||||||||||
References
| [1] | "Proline residues responsible for thermostability occur with high frequency in the loop regions of an extremely thermostable oligo-1,6-glucosidase from Bacillus thermoglucosidasius KP1006." Watanabe K., Chishiro K., Kitamura K., Suzuki Y. J. Biol. Chem. 266:24287-24294(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-12, TEMPERATURE DEPENDENCE. Strain: KP1006. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | D10487 Genomic DNA. Translation: BAA01368.1. |
| PIR | A41707. |
3D structure databases | |
| ProteinModelPortal | P29094. |
| SMR | P29094. Positions 1-560. |
| ModBase | Search... |
Protein family/group databases | |
| CAZy | GH13. Glycoside Hydrolase Family 13. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| Gene3D | 2.60.40.1180. 1 hit. 3.20.20.80. 2 hits. |
| InterPro | IPR015902. Glyco_hydro_13. IPR013780. Glyco_hydro_13_b. IPR006047. Glyco_hydro_13_cat_dom. IPR006589. Glyco_hydro_13_sub_cat_dom. IPR013781. Glyco_hydro_catalytic_dom. IPR017853. Glycoside_hydrolase_SF. [Graphical view] |
| PANTHER | PTHR10357. PTHR10357. 1 hit. |
| Pfam | PF00128. Alpha-amylase. 1 hit. [Graphical view] |
| SMART | SM00642. Aamy. 1 hit. [Graphical view] |
| SUPFAM | SSF51445. Glyco_hydro_cat. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | O16G_BACTR | ||||||||
| Accession | Primary (citable) accession number: P29094 | ||||||||
| Entry history |
| ||||||||
| 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 |

Clusters with
