| IED ID | IndEnz0001000404 |
| Enzyme Type ID | amylase000404 |
| Protein Name |
Oligo-1,6-glucosidase 1 EC 3.2.1.10 Dextrin 6-alpha-D-glucanohydrolase Oligosaccharide alpha-1,6-glucosidase 1 Sucrase-isomaltase 1 Isomaltase 1 |
| Gene Name | malL yvdL BSU34560 |
| Organism | Bacillus subtilis (strain 168) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus subtilis group Bacillus subtilis Bacillus subtilis subsp. subtilis Bacillus subtilis (strain 168) |
| Enzyme Sequence | MSEWWKEAVVYQIYPRSFYDANGDGFGDLQGVIQKLDYIKNLGADVIWLSPVFDSPQDDNGYDISDYKNMYEKFGTNEDMFQLIDEVHKRGMKIVMDLVVNHTSDEHAWFAESRKSKDNPYRDYYLWKDPKPDGSEPNNWGSIFSGSAWTYDEGTGQYYLHYFSKKQPDLNWENEAVRREVYDVMRFWMDRGVDGWRMDVIGSISKYTDFPDYETDHSRSYIVGRYHSNGPRLHEFIQEMNREVLSHYDCMTVGEANGSDIEEAKKYTDASRQELNMIFTFEHMDIDKEQNSPNGKWQIKPFDLIALKKTMTRWQTGLMNVGWNTLYFENHDQPRVISRWGNDRKLRKECAKAFATVLHGMKGTPFIYQGEEIGMVNSDMPLEMYDDLEIKNAYRELVVENKTMSEKEFVKAVMIKGRDHARTPMQWDAGKHAGFTAGDPWIPVNSRYQDINVKESLEDQDSIFFYYQKLIQLRKQYKIMIYGDYQLLQENDPQVFSYLREYRGEKLLVVVNLSEEKALFEAPPELIHERWKVLISNYPQERADLKSISLKPYEAVMGISI |
| Enzyme Length | 561 |
| Uniprot Accession Number | O06994 |
| Absorption | |
| Active Site | ACT_SITE 199; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 255; /note=Proton donor; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->6)-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by alpha-amylase, and in isomaltose.; EC=3.2.1.10; Evidence={ECO:0000269|PubMed:10229946, ECO:0000269|PubMed:24015933, ECO:0000269|PubMed:9573215}; |
| DNA Binding | |
| EC Number | 3.2.1.10 |
| Enzyme Function | FUNCTION: Hydrolyzes various disaccharides such as sucrose, maltose, and isomaltose with different efficiencies. Also hydrolyzes longer maltodextrins from maltotriose up to maltohexaose, but not maltoheptaose, palatinose, isomaltotriose, or isomaltotetraose. {ECO:0000269|PubMed:10229946}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 42 degrees Celsius. {ECO:0000269|PubMed:10229946}; |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (23); Chain (1); Helix (27); Metal binding (5); Site (1); Turn (7) |
| Keywords | 3D-structure;Calcium;Cytoplasm;Glycosidase;Hydrolase;Metal-binding;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (5) |
| Cross Reference PDB | 4M56; 4M8U; 4MAZ; 4MB1; 5WCZ; |
| Mapped Pubmed ID | 29563521; |
| Motif | |
| Gene Encoded By | |
| Mass | 66,081 |
| Kinetics | |
| Metal Binding | METAL 20; /note="Calcium"; /evidence="ECO:0000269|PubMed:24015933, ECO:0007744|PDB:4M8U, ECO:0007744|PDB:4MB1"; METAL 22; /note="Calcium"; /evidence="ECO:0000269|PubMed:24015933, ECO:0007744|PDB:4M8U, ECO:0007744|PDB:4MB1"; METAL 24; /note="Calcium"; /evidence="ECO:0000269|PubMed:24015933, ECO:0007744|PDB:4M8U, ECO:0007744|PDB:4MB1"; METAL 26; /note="Calcium; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:24015933, ECO:0007744|PDB:4M8U, ECO:0007744|PDB:4MB1"; METAL 28; /note="Calcium"; /evidence="ECO:0000269|PubMed:24015933, ECO:0007744|PDB:4M8U, ECO:0007744|PDB:4MB1" |
| Rhea ID | |
| Cross Reference Brenda |