| IED ID | IndEnz0001000239 |
| Enzyme Type ID | amylase000239 |
| Protein Name |
Alpha-amylase I EC 3.2.1.1 1,4-alpha-D-glucan glucanohydrolase |
| Gene Name | AMY1 AMY I AAEL006719 |
| Organism | Aedes aegypti (Yellowfever mosquito) (Culex aegypti) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Diptera Nematocera Culicomorpha Culicoidea Culicidae (mosquitos) Culicinae Aedini Aedes Stegomyia Aedes aegypti (Yellowfever mosquito) (Culex aegypti) |
| Enzyme Sequence | MKQLLVILYSALVVTNAQLPGFSFGPSGFGGFSLSNPLFNASFAPANPVDRISDIASRFRDVANNVQRNLPKIPQFTNPLSAFSRFARPTSSSGSTNANSNNNQNFNSNQANEGTSGARNAINEVLNRIPGLSGVPRVPEIPKVPEIPSFGNPSDVFGPFVNSLRNMTNQGINDPGQMFNQVNKFLPDVSRIANSVANYAKSAANSGIWKNISNDIKHEMQNRIESMTQMLSNITSAMKNIAQSLPNLMQDQSLNTTLRNQPFFFPGHSGIVHLFEWKFSDIAEECENVLGPNGYGGVQVSPINEYLVSPSRAWWERYQPISFEIKSRSGNEKQFSDMVKRCMKAGVRIYVDVVVNHMAAPGASAPLYGTAGSTCDPQARDYPGVPFNRSHFHADCQINDYNNATNVRNCELAALPDLDQSNRFVQNKIIQYLNHLLDLGVAGFRMDACKHMRPEDLKSIYVRLKPVNAMFLFPPGARPFIFQEVIDLGTEGVSAKEYTNLGVVTEFNWCIAVGGVFRGTTNADALELLTKNGSAGVLLPSSQALVFVDNHDNQRGHGAGGDSILTYKTKRQYIQAVAFTLATDYGIARVMSSYNFSDPDQGPPQDTVQVIKSPGFAANNSCSNGWVCEHRWPEIRKMIQFKNFVAGSSLDHIQATQNTFAFCRGEKGFIVFNNSENTITQQYHTCLPQGQYCDIISGEVSQSTCTGTVVNVDANGDAEITLPKNSIVAIYVPSRLS |
| Enzyme Length | 737 |
| Uniprot Accession Number | P53354 |
| Absorption | |
| Active Site | ACT_SITE 447; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P04746; ACT_SITE 484; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:P04746 |
| Activity Regulation | |
| Binding Site | BINDING 445; /note=Chloride; /evidence=ECO:0000250|UniProtKB:P56634; BINDING 550; /note=Chloride; /evidence=ECO:0000250|UniProtKB:P56634; BINDING 589; /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:P56634}; |
| 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); Glycosylation (11); Metal binding (4); Region (2); Sequence conflict (31); Signal peptide (1); Site (1) |
| Keywords | Calcium;Carbohydrate metabolism;Chloride;Disulfide bond;Glycoprotein;Glycosidase;Hydrolase;Metal-binding;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..16; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 80,891 |
| Kinetics | |
| Metal Binding | METAL 356; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P56634; METAL 408; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P56634; METAL 417; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P56634; METAL 451; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P56634 |
| Rhea ID | |
| Cross Reference Brenda |