Detail Information for IndEnz0001000020
IED ID IndEnz0001000020
Enzyme Type ID amylase000020
Protein Name Alpha-amylase A
EC 3.2.1.1
1,4-alpha-D-glucan glucanohydrolase
Gene Name Amy-p AmyA CG18730
Organism Drosophila melanogaster (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 melanogaster subgroup Drosophila melanogaster (Fruit fly)
Enzyme Sequence MFLAKSIVCLALLAVANAQFDTNYASGRSGMVHLFEWKWDDIAAECENFLGPNGYAGVQVSPVNENAVKDSRPWWERYQPISYKLETRSGNEEQFASMVKRCNAVGVRTYVDVVFNHMAADGGTYGTGGSTASPSSKSYPGVPYSSLDFNPTCAISNYNDANEVRNCELVGLRDLNQGNSYVQDKVVEFLDHLIDLGVAGFRVDAAKHMWPADLAVIYGRLKNLNTDHGFASGSKAYIVQEVIDMGGEAISKSEYTGLGAITEFRHSDSIGKVFRGKDQLQYLTNWGTAWGFAASDRSLVFVDNHDNQRGHGAGGADVLTYKVPKQYKMASAFMLAHPFGTPRVMSSFSFTDTDQGPPTTDGHNIASPIFNSDNSCSGGWVCEHRWRQIYNMVAFRNTVGSDEIQNWWDNGSNQISFSRGSRGFVAFNNDNYDLNSSLQTGLPAGTYCDVISGSKSGSSCTGKTVTVGSDGRASINIGSSEDDGVLAIHVNAKL
Enzyme Length 494
Uniprot Accession Number P08144
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); Modified residue (1); Natural variant (18); Signal peptide (1); Site (1)
Keywords Calcium;Carbohydrate metabolism;Chloride;Disulfide bond;Glycosidase;Hydrolase;Metal-binding;Pyrrolidone carboxylic acid;Reference proteome;Signal
Interact With
Induction
Subcellular Location
Modified Residue MOD_RES 19; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000250
Post Translational Modification
Signal Peptide SIGNAL 1..18
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 100784; 10364829; 10429831; 10429832; 10545459; 10552037; 10626037; 10655221; 10690430; 10742051; 11040291; 11139506; 11139510; 11163960; 11298976; 11319264; 11404335; 11483574; 11606707; 11862451; 12072480; 12136021; 12424525; 12618415; 12626737; 1335624; 1374789; 1385266; 14629045; 14745539; 15166145; 15204079; 15466469; 15483321; 1560824; 1582561; 1582562; 16118662; 1616481; 16387879; 16547107; 16593815; 1684329; 16906161; 16907832; 1699840; 1699842; 1702542; 17167051; 17246342; 17246356; 17246358; 17246437; 1736311; 18562639; 1900365; 19079581; 19494137; 20609461; 2108305; 21084378; 21963537; 23071443; 23459416; 23525904; 23964241; 24463528; 24670639; 2468332; 24956222; 2496682; 25284780; 25409104; 25472843; 25913403; 26440885; 26526100; 27312592; 27894253; 28567756; 29066546; 29141990; 2989084; 3016645; 30372516; 3038675; 30399425; 30566533; 30633769; 31398343; 31722958; 31915294; 32663363; 33717711; 33723074; 33773104; 33951964; 33978737; 34066348; 34120097; 3498932; 3924727; 4627711; 5348624; 5586609; 6035670; 6170292; 6180326; 6187335; 6413453; 7505762; 7526389; 7713409; 7841458; 7857669; 7899073; 8031578; 8080656; 8100789; 825413; 8325486; 8349118; 8483161; 8536970; 8575929; 8583899; 8798339; 8882500; 8896375; 9181432; 9211732; 9287427; 9321417; 9533124; 9611206; 9618501; 9656489; 9819559; 9872956;
Motif
Gene Encoded By
Mass 53,746
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 3.2.1.1;