| IED ID | IndEnz0001000443 |
| Enzyme Type ID | amylase000443 |
| Protein Name |
Alpha-amylase EC 3.2.1.1 1,4-alpha-D-glucan glucanohydrolase |
| Gene Name | |
| Organism | Phaedon cochleariae (Mustard beetle) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Coleoptera Polyphaga Cucujiformia Chrysomeloidea Chrysomelidae (leaf beetles) Chrysomelinae Chrysomelini Phaedon Phaedon cochleariae (Mustard beetle) |
| Enzyme Sequence | MFLTSVLILCSLAALSLGQKNNNFAPGRNTIVHLFEWHWDDIANECENFLGPKGFAGVQISPPAENTVIGDRPWWERYQPISYALNTRSGDESALASMIRRCNNAGVRIYVDAVFNHMSATSGIGTGGSSCDVEPSASPAVPYGSGDFHGRCTSNNYQDPNNIRNCWLSGLPDLDQSKDYVRDKILEYLNHLVDLGVAGFRVDAAKHMWPADLQVIYGRVKDLNTDHGFSQGSRPFFYQEVIDLGGEGVSKNEYTGFGTVLEFKYGTELGNAFQGNNALHNLENWGPAWGLLEGTDAVVFIDNHDNQRTGSGAILTYKNPRPYKMAIGFMLAHPYGTTRIMSSFSFDYNDQGPPTQGPGFNSVRNLHQWVGGANTGWRQILRVMVGFRNAVDGTSISNWWSDGNQQIAFGRGDKGFVAFTLAGDINGNLQTSLPAGSYCDIVSGKLENGSCTGKTVNVDGNGQAYITLSSGEDDGFLAIHVGAKV |
| Enzyme Length | 485 |
| Uniprot Accession Number | O97396 |
| Absorption | |
| Active Site | ACT_SITE 203; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P56634; ACT_SITE 240; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:P56634 |
| Activity Regulation | |
| Binding Site | BINDING 201; /note=Chloride; /evidence=ECO:0000250|UniProtKB:P56634; BINDING 303; /note=Chloride; /evidence=ECO:0000250|UniProtKB:P56634; BINDING 339; /note=Chloride; /evidence=ECO:0000250|UniProtKB:P56634 |
| 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:P04746}; |
| DNA Binding | |
| EC Number | 3.2.1.1 |
| Enzyme Function | |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Binding site (3); Chain (1); Disulfide bond (3); Glycosylation (1); Metal binding (4); Modified residue (1); Signal peptide (1); Site (1) |
| Keywords | Calcium;Carbohydrate metabolism;Chloride;Digestion;Disulfide bond;Glycoprotein;Glycosidase;Hydrolase;Metal-binding;Pyrrolidone carboxylic acid;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. |
| Modified Residue | MOD_RES 19; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000250|UniProtKB:P56634 |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 52,832 |
| Kinetics | |
| Metal Binding | METAL 116; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P56634; METAL 164; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P56634; METAL 173; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P56634; METAL 207; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P56634 |
| Rhea ID | |
| Cross Reference Brenda |