IED ID | IndEnz0001000444 |
Enzyme Type ID | amylase000444 |
Protein Name |
Alpha-amylase EC 3.2.1.1 1,4-alpha-D-glucan glucanohydrolase |
Gene Name | |
Organism | Priestia megaterium (Bacillus megaterium) |
Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Priestia Priestia megaterium (Bacillus megaterium) |
Enzyme Sequence | MKGKKWTALALTLPLAASLSTGVDAETVHKGKAPTADKNGVFYEVYVNSFYDANKDGHGDLKGLTQKLDYLNDGNSHTKNDLQVNGIWMMPVNPSPSYHKYDVTDYYNIDPQYGNLQDFRKLMKEADKRDVKVIMDLVVNHTSSEHPWFQAALKDKNSKYRDYYIWADKNTDLNEKGSWGQQVWHKAPNGEYFYGTFWEGMPDLNYDNPEVRKEMINVGKFWLKQGVDGFRLDAALHIFKGQTPEGAKKNILWWNEFRDAMKKENPNVYLTGEVWDQPEVVAPYYQSLDSLFNFDLAGKIVSSVKAGNDQGIATAAAATDELFKSYNPNKIDGIFLTNHDQNRVMSELSGDVNKAKSAASILLTLPGNPYIYYGEEIGMTGEKPDELIREPFRWYEGNGIGQTSWETPVYNKGGNGVSVEAQTKQKDSLLNHYREMIRVRQQHEELVKGTLQSISVDSKEVVAYSRTYKGKSISVYHNISNQPVKVSVAAKGNLIFASEKGAKKVKNQLVIPANRTVLIK |
Enzyme Length | 520 |
Uniprot Accession Number | P20845 |
Absorption | |
Active Site | ACT_SITE 233; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 273; /note=Proton donor; /evidence=ECO:0000250 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.; EC=3.2.1.1; |
DNA Binding | |
EC Number | 3.2.1.1 |
Enzyme Function | |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Chain (1); Metal binding (3); Signal peptide (1); Site (1) |
Keywords | Calcium;Carbohydrate metabolism;Direct protein sequencing;Glycosidase;Hydrolase;Metal-binding;Signal |
Interact With | |
Induction | |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..27 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 58,761 |
Kinetics | |
Metal Binding | METAL 140; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q8A1G3; METAL 203; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q8A1G3; METAL 237; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q8A1G3 |
Rhea ID | |
Cross Reference Brenda | 3.2.1.1; |