| IED ID | IndEnz0001000419 |
| Enzyme Type ID | amylase000419 |
| Protein Name |
Cytoplasmic alpha-amylase EC 3.2.1.1 1,4-alpha-D-glucan glucanohydrolase |
| Gene Name | amyA STM1963 |
| Organism | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Salmonella Salmonella enterica (Salmonella choleraesuis) Salmonella enterica I Salmonella typhimurium Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) |
| Enzyme Sequence | MKNPTLLQYFHWYYPDGGKLWSELAERADGLNDIGINMVWLPPACKGASGGYSVGYDTYDLFDLGEFDQKGTIATKYGDKRQLLTAIDALKKNNIAVLLDVVVNHKMGADEKERIRVQRVNQDDRTQIDDNIIECEGWTRYTFPARAGQYSNFIWDYHCFSGIDHIENPDEDGIFKIVNDYTGDGWNDQVDDEMGNFDYLMGENIDFRNHAVTEEIKYWARWVMEQTHCDGFRLDAVKHIPAWFYKEWIEHVQAVAPKPLFIVAEYWSHEVDKLQTYIDQVDGKTMLFDAPLQMKFHEASRQGAEYDMRHIFTGTLVEADPFHAVTLVANHDTQPLQALEAPVEPWFKPLAYALILLRENGVPSVFYPDLYGASYEDSGENGETCRVDMPVINQLDRLILARQRFAHGIQTLFFDHPNCIAFSRSGTEENPGCVVVLSNGDDGEKTLLLGDNYANKTWRDFLGNRDEYVVTNDQGEATFFCNAGSVSVWVIEDV |
| Enzyme Length | 494 |
| Uniprot Accession Number | P26613 |
| Absorption | |
| Active Site | ACT_SITE 235; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 265; /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; Evidence={ECO:0000250|UniProtKB:P06279}; |
| 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); Sequence conflict (1); Site (1) |
| Keywords | Calcium;Carbohydrate metabolism;Cytoplasm;Glycosidase;Hydrolase;Metal-binding;Reference proteome;Sodium |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P26612}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 56,522 |
| Kinetics | |
| Metal Binding | METAL 104; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P00692; METAL 198; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P00692; METAL 239; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P00692 |
| Rhea ID | |
| Cross Reference Brenda |