| IED ID | IndEnz0001000152 |
| Enzyme Type ID | amylase000152 |
| Protein Name |
Oligo-1,6-glucosidase EC 3.2.1.10 Dextrin 6-alpha-D-glucanohydrolase Oligosaccharide alpha-1,6-glucosidase Sucrase-isomaltase Isomaltase |
| Gene Name | malL |
| Organism | Parageobacillus thermoglucosidasius (Geobacillus thermoglucosidasius) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Parageobacillus Parageobacillus thermoglucosidasius (Geobacillus thermoglucosidasius) |
| Enzyme Sequence | MERVWWKEAVVYQIYPRSFYDSNGDGIGDIRGIIAKLDYLKELGVDVVWLSPVYKSPNDDNGYDISDYRDIMDEFGTMADWKTMLEEMHKRGIKLVMDLVVNHTSDEHPWFIESRKSKDNPYRDYYIWRPGKNGKEPNNWESVFSGSAWEYDEMTGEYYLHLFSKKQPDLNWENPKVRREVYEMMKFWLDKGVDGFRMDVINMISKVPELPDGEPQSGKKYASGSRYYMNGPRVHEFLQEMNREVLSKYDIMTVGETPGVTPKEGILYTDPSRRELNMVFQFEHMDLDSGPGGKWDIRPWSLADLKKTMTKWQKELEGKGWNSLYLNNHDQPRAVSRFGDDGKYRVESAKMLATFLHMMQGTPYIYQGEEIGMTNVRFPSIEDYRDIETLNMYKERVEEYGEDPQEVMEKIYYKGRDNARTPMQWDDSENAGFTAGTPWIPVNPNYKEINVKAALEDPNSVFHYYKKLIQLRKQHDIIVYGTYDLILEDDPYIYRYTRTLGNEQLIVITNFSEKTPVFRLPDHIIYKTKELLISNYDVDEAEELKEIRLRPWEARVYKIRLP |
| Enzyme Length | 562 |
| Uniprot Accession Number | P29094 |
| Absorption | |
| Active Site | ACT_SITE 199; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 256; /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; |
| DNA Binding | |
| EC Number | 3.2.1.10 |
| Enzyme Function | |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Extremely thermostable. {ECO:0000269|PubMed:1761534}; |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Metal binding (4); Site (1) |
| Keywords | Calcium;Cytoplasm;Direct protein sequencing;Glycosidase;Hydrolase;Metal-binding |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 66,505 |
| Kinetics | |
| Metal Binding | METAL 21; /note=Calcium; /evidence=ECO:0000250|UniProtKB:O06994; METAL 23; /note=Calcium; /evidence=ECO:0000250|UniProtKB:O06994; METAL 25; /note=Calcium; /evidence=ECO:0000250|UniProtKB:O06994; METAL 29; /note=Calcium; /evidence=ECO:0000250|UniProtKB:O06994 |
| Rhea ID | |
| Cross Reference Brenda |