Detail Information for IndEnz0001000239
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