Detail Information for IndEnz0001000417
IED ID IndEnz0001000417
Enzyme Type ID amylase000417
Protein Name Alpha-amylase isozyme 2A
EC 3.2.1.1
1,4-alpha-D-glucan glucanohydrolase
Alpha-amylase isozyme C2
Gene Name AMY2A AMY1.5 AMYC2 Os06g0713800 LOC_Os06g49970 OJ1136_F03.12 OsJ_22644
Organism Oryza sativa subsp. japonica (Rice)
Taxonomic Lineage cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae Liliopsida Petrosaviidae commelinids Poales Poaceae BOP clade Oryzoideae Oryzeae Oryzinae Oryza Oryza sativa (Rice) Oryza sativa subsp. japonica (Rice)
Enzyme Sequence MATGRRLSMILLLLLLGLASGDKILFQGFNWESWRQSGGWYNLLMGKVDDIVAAGVTHVWLPPPSHSVSTQGYMPGRLYDLDASRYGTSMELKSLISALHGKGIQAIADVVINHRCADYKDSRGIYCIFEGGTPDGRLDWGPHMICRDDTQFSDGTGNLDTGADFAAAPDIDHLNGVVQRELTDWLLWLKSDEVGFDAWRLDFARGYSPEVAKVYIEGTTPVGLAVAELWDSMAYGGDGKPEYNQDAHRQALVDWVDRVGGTASAGMVFDFTTKGIMNTAVEGELWRLIDQQGKAPGVIGWWPAKAVTFVDNHDTGSTQQMWPFPSDKVMQGYAYILTHPGNPCIFYDHFFDWGLKEQIAALVAVRQRNGVTATSSLKIMLHDADAYVAEIDGKVVMKIGSRYDVSSLIPPGFHLAAHGNGYAVWEKIAAAAAAADHRTSSSASL
Enzyme Length 445
Uniprot Accession Number Q0D9J1
Absorption
Active Site ACT_SITE 202; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P00693; ACT_SITE 228; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:P00693
Activity Regulation
Binding Site BINDING 230; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00693; BINDING 232; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P04063; BINDING 250; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00693; BINDING 257; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00693; BINDING 294; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00693; BINDING 313; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00693; BINDING 319; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00693; BINDING 398; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00693; BINDING 425; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00693
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:P00693};
DNA Binding
EC Number 3.2.1.1
Enzyme Function FUNCTION: Important for breakdown of endosperm starch during germination.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Binding site (9); Chain (1); Metal binding (14); Region (6); Sequence conflict (1); Signal peptide (1); Site (1)
Keywords Calcium;Carbohydrate metabolism;Glycosidase;Hydrolase;Metal-binding;Reference proteome;Signal
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..21; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 1859866; 27438877;
Motif
Gene Encoded By
Mass 48,696
Kinetics
Metal Binding METAL 113; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P00693; METAL 130; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:P00693; METAL 133; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P00693; METAL 135; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P00693; METAL 139; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:P00693; METAL 149; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:P00693; METAL 160; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P00693; METAL 163; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P00693; METAL 164; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:P00693; METAL 165; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P00693; METAL 168; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P00693; METAL 170; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P00693; METAL 170; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:P00693; METAL 206; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P00693
Rhea ID
Cross Reference Brenda