| IED ID | IndEnz0001000009 |
| Enzyme Type ID | amylase000009 |
| Protein Name |
Alpha-amylase EC 3.2.1.1 1,4-alpha-D-glucan glucanohydrolase Alpha-amylase isozyme 1B |
| Gene Name | AMY1.1 AMY1A Os02g0765600 LOC_Os02g52710 OJ1004_A11.13 P0539D10.32 |
| 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 | MQVLNTMVNKHFLSLSVLIVLLGLSSNLTAGQVLFQGFNWESWKENGGWYNFLMGKVDDIAAAGITHVWLPPPSHSVGEQGYMPGRLYDLDASKYGNEAQLKSLIEAFHGKGVQVIADIVINHRTAEHKDGRGIYCLFEGGTPDSRLDWGPHMICRDDPYGDGTGNPDTGADFAAAPDIDHLNKRVQRELIGWLDWLKMDIGFDAWRLDFAKGYSADMAKIYIDATEPSFAVAEIWTSMANGGDGKPNYDQNAHRQELVNWVDRVGGANSNATAFDFTTKGILNVAVEGELWRLRGEDGKAPGMIGWWPAKATTFVDNHDTGSTQHLWPFPSDKVMQGYAYILTHPGNPCIFYDHFFDWGLKEEIERLVSIRNRQGIHPASELRIMEADSDLYLAEIDGKVITKIGPRYDVEHLIPEGFQVVAHGDGYAIWEKI |
| Enzyme Length | 434 |
| Uniprot Accession Number | P17654 |
| Absorption | |
| Active Site | ACT_SITE 209; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P00693; ACT_SITE 234; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:P00693 |
| Activity Regulation | |
| Binding Site | BINDING 236; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00693; BINDING 238; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P04063; BINDING 256; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00693; BINDING 263; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00693; BINDING 300; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00693; BINDING 319; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00693; BINDING 325; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00693; BINDING 404; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00693; BINDING 431; /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); Beta strand (19); Binding site (9); Chain (1); Erroneous initiation (1); Glycosylation (1); Helix (20); Metal binding (14); Region (6); Sequence conflict (2); Signal peptide (1); Site (1); Turn (4) |
| Keywords | 3D-structure;Calcium;Carbohydrate metabolism;Glycoprotein;Glycosidase;Hydrolase;Metal-binding;Reference proteome;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | PTM: Only cereal amylase known to be glycosylated. |
| Signal Peptide | SIGNAL 1..31; /evidence=ECO:0000305 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 3WN6; |
| Mapped Pubmed ID | 10527416; 11950975; 12228339; 12554717; 12787245; 14500792; 1502164; 18268540; 1859866; 19767453; 2263460; 22967050; 23550921; 24046061; 24865690; 25036124; 25581614; 26545757; 26643956; 26850838; 27038670; 27478151; 7957256; 8028999; 8590656; 8934629; 9163949; 9640660; |
| Motif | |
| Gene Encoded By | |
| Mass | 48,457 |
| Kinetics | |
| Metal Binding | METAL 122; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P00693; METAL 139; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:P00693; METAL 142; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P00693; METAL 144; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P00693; METAL 148; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:P00693; METAL 158; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:P00693; METAL 168; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P00693; METAL 171; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P00693; METAL 172; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:P00693; METAL 173; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P00693; METAL 176; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P00693; METAL 178; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P00693; METAL 178; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:P00693; METAL 213; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P00693 |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.1; |