| IED ID | IndEnz0001000902 |
| Enzyme Type ID | amylase000902 |
| Protein Name |
Alpha-amylase 1 EC 3.2.1.1 |
| Gene Name | Amy35 Amy1 GF18844 |
| Organism | Drosophila ananassae (Fruit fly) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Diptera Brachycera Muscomorpha Eremoneura Cyclorrhapha Schizophora Acalyptratae Ephydroidea Drosophilidae (pomace flies) Drosophilinae Drosophilini Drosophila (fruit flies) Sophophora melanogaster group ananassae subgroup ananassae species complex Drosophila ananassae (Fruit fly) |
| Enzyme Sequence | MFLAKSIVCLALLAVANAQFNTNYASGRSGMVHLFEWKWDDIAAECENFLGPYGYAGVQVSPVNENAVKDSRPWWERYQPISYKLVTRSGNEEQFASMVRRCNNVGVRIYVDVVFNHMAANGGTYGTGGSTASPSSKSYPGVPFSSLDFNPTCAISNYNDANQVRNCELVGLRDLNQGNSYVQEKIVEFLNHLIDLGVAGFRVDAAKHMWPADLGVIYGSLKNLNTDHGFESGAKAYIVQEVIDMGGEAISKSEYTGLGAITEFRHSDSIGKAFRGKNQLQYLVNWGVSWGFAASDRSLVFVDNHDNQRGHGAGGADVLTYKVPKQYKMASAFMLAHPFGTPRVMSSFSFTDTDQGPPTTDGQNIASPSFNSDNSCSGGWVCEHRWKQIYNMVGFRNAVGSDAIQNWWDNGSNQIAFSRGSKGFVAFNNDNYDLNSSVQTGLPAGTYCDVISGSKSGSSCTGKTVTVGSDGRANISIGSSEDDGVLAIHVNAKL |
| Enzyme Length | 494 |
| Uniprot Accession Number | Q23835 |
| Absorption | |
| Active Site | ACT_SITE 204; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P04746; ACT_SITE 241; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:P04746 |
| Activity Regulation | |
| Binding Site | BINDING 202; /note=Chloride; /evidence=ECO:0000250|UniProtKB:P04746; BINDING 304; /note=Chloride; /evidence=ECO:0000250|UniProtKB:P04746; BINDING 343; /note=Chloride; /evidence=ECO:0000250|UniProtKB:P04746 |
| 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 (4); Metal binding (4); Natural variant (1); Region (1); Sequence conflict (6); Signal peptide (1); Site (1) |
| Keywords | Calcium;Carbohydrate metabolism;Chloride;Disulfide bond;Glycosidase;Hydrolase;Metal-binding;Reference proteome;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 53,575 |
| Kinetics | |
| Metal Binding | METAL 116; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P04746; METAL 165; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P04746; METAL 174; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P04746; METAL 208; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P04746 |
| Rhea ID | |
| Cross Reference Brenda |