| IED ID | IndEnz0001000173 |
| Enzyme Type ID | amylase000173 |
| Protein Name |
Intracellular maltogenic amylase EC 3.2.1.- |
| Gene Name | bbmA yvdF BSU34620 |
| 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 | MEYAAIHHQPFSTDAYSYDGRTVHIKIRTKKGDADHIRFIWGDPYEYNDGKWSANEQPMRKIAATEMHDYWFAEVVPPFRRLQYAFVVTDDHEDIFFGSSGVCPYNEKTLETIHYYFKFPFVHEADTFQAPEWVKSTVWYQIFPERFANGREDLSPKNALPWGSKDPDVNDFFGGDLQGIVDKLDYLEDLGVNGIYLTPIFSAPSNHKYDTLDYFSIDPHFGDPELFRTLVSQLHQRGMRIMLDAVFNHIGSASPQWQDVVKNGDQSRYKDWFHIHSFPVTDDNYDRFAFTADMPKLNTANPEVQKYLLDIALYWIREFDIDGWRLDVANEVDHVFWKTFRQAVSTEKPDVYILGEIWHSAEPWLRGDEFHAAMNYPFTEPMIEYFADQTISASRMAHRVNAHLMNGMKQANEVMFNLLDSHDTKRLLTRCRNDEKKARALLAFMFAQTGSPCIYYGTEIGLNGENDPLCRKCMVWEKEKQNQDMLQFMKRLIALRKQENTLLTEGHLEWNLLDDKNDFISFSRTLDEKILIYFFNQGNVVQHVSLRELNIDRNKKICDAWTEQPLQHHDVIAVQPGEFLILSAAAPV |
| Enzyme Length | 588 |
| Uniprot Accession Number | O06988 |
| Absorption | |
| Active Site | ACT_SITE 327; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P38940; ACT_SITE 356; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:P38940 |
| Activity Regulation | |
| Binding Site | BINDING 249; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P38940; BINDING 325; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P38940; BINDING 467; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P38940; BINDING 471; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P38940 |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.2.1.- |
| Enzyme Function | 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 (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Binding site (4); Chain (1); Erroneous initiation (2); Metal binding (4); Region (1); Site (1) |
| Keywords | Calcium;Carbohydrate metabolism;Cytoplasm;Glycosidase;Hydrolase;Metal-binding;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9R9H8}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 68,722 |
| Kinetics | |
| Metal Binding | METAL 149; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P38940; METAL 155; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P38940; METAL 174; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P38940; METAL 176; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P38940 |
| Rhea ID | |
| Cross Reference Brenda |