| IED ID | IndEnz0001000259 |
| Enzyme Type ID | amylase000259 |
| Protein Name |
Maltogenic alpha-amylase EC 3.2.1.133 Glucan 1,4-alpha-maltohydrolase |
| Gene Name | |
| Organism | Bacillus acidopullulyticus |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus acidopullulyticus |
| Enzyme Sequence | MFREAIYHRPKDNYAYACANGELHIRIRTKKDDMKEVTLVYGDTYEFDDNKWTYSTAHMKKTGSDQLFDYWLASVTPRYKRLRYGFIVNDRKDSTCFTEKGFYPEPPVNDISYYFSFPYVNQADIFQAPEWVKDTVWYQIFPERFANGNKDNDPDGTLPWGSREPEIDNFFGGDLEGVIEHIDYLKELGIGGIYFTPIFKAHSNHKYDTIDYMEIDPQFGTKETLKKLIDVCHKNGIKVMLDAVFNHSGVFFPPFQDVVEKGKNSKYQDWFHIREFPLVMEPRPNYDTFGFTSSMPKFKTENPEVKEYLLEVGRYWVREFDIDGWRLDVANEVSHAFWREFRREVKAIKPDLYILGEIWHDSLPWLRGDQFDAVMNYPLSTNIVNLFANQSVSVKEFVENMSHVIHMYPDTVNEAAFNLVGSHDTPRILTQCGEDVERLKQVFVLLLTFIGTPCIYYGDEIGLTGGQDPGCRKCMEWNPDQQNRELLQHVRKLIQLRSENPLLANEGELTFVPPKNEEDPCLAYTKSNEEKTIMIIINKSKNSVEYPLSFDAAEQTVKNLWNQEQLILQNGQTLELKANDFKILEF |
| Enzyme Length | 586 |
| Uniprot Accession Number | P32818 |
| Absorption | |
| Active Site | ACT_SITE 328; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P38940; ACT_SITE 357; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:P38940 |
| Activity Regulation | |
| Binding Site | BINDING 247; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P38940; BINDING 326; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P38940; BINDING 468; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P38940; BINDING 472; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P38940 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive alpha-maltose residues from the non-reducing ends of the chains.; EC=3.2.1.133; |
| DNA Binding | |
| EC Number | 3.2.1.133 |
| Enzyme Function | FUNCTION: Converts starch into maltose. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Binding site (4); Chain (1); Metal binding (5); Region (1); Site (1) |
| Keywords | Calcium;Carbohydrate metabolism;Glycosidase;Hydrolase;Metal-binding |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 68,520 |
| Kinetics | |
| Metal Binding | METAL 147; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q60053; METAL 152; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q60053; METAL 153; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q60053; METAL 172; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q60053; METAL 174; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q60053 |
| Rhea ID | |
| Cross Reference Brenda |