| IED ID | IndEnz0001000551 |
| Enzyme Type ID | amylase000551 |
| Protein Name |
Alpha-amylase isozyme 2A EC 3.2.1.1 1,4-alpha-D-glucan glucanohydrolase Alpha-amylase isozyme C2 |
| Gene Name | AMYC2 AMY1.5 AMY2A OsI_023575 |
| Organism | Oryza sativa subsp. indica (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. indica (Rice) |
| Enzyme Sequence | MATGRRLSMILLLLLLGLASGDKILFQGFNWESWRQSGGWYNLLMGKVDDIVAAGVTHVWLPPPSHSVSTQGYMPGRLYDLDASRYGTSMELKSLISALHGKGIQAIADVVINHRCADYKDSRGIYCIFEGGTPDGRLDWGPHMICRDDTQFSDGTGNLDTGADFAAAPDIDHLNGVVQRELTDWLLWLKSDEVGFDAWRLDFARGYSPEVAKVYIEGTTPVGLAVAELWDSMAYGGDGKPEYNQDAHRQALVDWVDRVGGTASAGMVFDFTTKGIMNTAVEGELWRLIDQQGKAPGVIGWWPAKAVTFVDNHDTGSTQQMWPFPSDKVMQGYAYILTHPGNPCIFYDHFFDWGLKEQIAALVAVRQRNGVTATSSLKIMLHDADAYVAEIDGKVVMKIGSRYDVSSLIPPGFHLAAHGNGYAVWEKSAAAAAAAADHRTSSSASL |
| Enzyme Length | 446 |
| Uniprot Accession Number | A2YGY2 |
| 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); Frameshift (1); Metal binding (14); Region (6); Sequence conflict (2); 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 | - |
| Motif | |
| Gene Encoded By | |
| Mass | 48,741 |
| 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 |