Detail Information for IndEnz0001000582
IED ID IndEnz0001000582
Enzyme Type ID amylase000582
Protein Name Alpha-amylase-related protein
EC 3.2.1.1
Gene Name Amyrel CG8221
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 MFKFALTLTLCLAGSLSLAQHNPHWWGNRNTIVHLFEWKWSDIAQECESFLGPRGFAGVQVSPVNENILSAGRPWWERYQPISYKLTTRSGNEEEFGDMVRRCNDVGVRIYVDVLLNHMSGDFDGVAVGTAGTEAEPSKKSFPGVPYTAQDFHPTCEITDWNDRFQVQQCELVGLKDLDQSSDWVRSKLIEFLDHLIELGVAGFRVDAAKHMASEDLEYIYSSLSNLNIDHGFPHNSRPFIFQEVIDHGHETVSRDEYKDLGAVTEFRFSEEIGNAFRGNNALKWLQSWGTDWGFLPSGQALTFVDNHDNQRDAGAVLNYKSPRQYKMATAFHLAYPYGISRVMSSFAFDDHDTPPPQDAQERIISPEFDADGACVNGWICEHRWRQIYAMVGFKNAVRDTEITGWWDNGDNQISFCRGNKGFLAINNNLYDLSQDLNTCLPAGTYCDVISGSLIDGSCTGKSVTVNENGYGYIHIGSDDFDGVLALHVDAKV
Enzyme Length 493
Uniprot Accession Number O18408
Absorption
Active Site ACT_SITE 207; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P04746; ACT_SITE 244; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:P04746
Activity Regulation
Binding Site BINDING 205; /note=Chloride; /evidence=ECO:0000250|UniProtKB:P56634; BINDING 307; /note=Chloride; /evidence=ECO:0000250|UniProtKB:P56634; BINDING 342; /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 (5); Metal binding (4); Modified residue (1); Sequence conflict (15); Signal peptide (1); Site (1)
Keywords Calcium;Carbohydrate metabolism;Chloride;Disulfide bond;Glycosidase;Hydrolase;Metal-binding;Pyrrolidone carboxylic acid;Reference proteome;Secreted;Signal
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
Modified Residue MOD_RES 20; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000250
Post Translational Modification
Signal Peptide SIGNAL 1..19; /evidence=ECO:0000250
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10723747; 10925206; 11040291; 11070058; 11139506; 11139510; 11298976; 11442633; 11606707; 14704170; 15008418; 15166145; 19196346; 19761854; 20433773; 21036383; 21343364; 22296880; 22888286; 23071443; 23603562; 24762206; 24864304; 25133712; 25284780; 25294943; 25312911; 26298685; 27172210; 27312592; 30372516; 30633769; 31398343; 31722958; 31799578; 33773104; 33978737; 34120097; 34343293; 9872956;
Motif
Gene Encoded By
Mass 55,451
Kinetics
Metal Binding METAL 117; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P56634; METAL 168; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P56634; METAL 177; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P56634; METAL 211; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P56634
Rhea ID
Cross Reference Brenda