| IED ID | IndEnz0001000555 |
| Enzyme Type ID | amylase000555 |
| Protein Name |
Alpha-amylase type B isozyme EC 3.2.1.1 1,4-alpha-D-glucan glucanohydrolase AMY2-2 High pI alpha-amylase |
| Gene Name | AMY1.2 |
| Organism | Hordeum vulgare (Barley) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae Liliopsida Petrosaviidae commelinids Poales Poaceae BOP clade Pooideae Triticodae Triticeae Hordeinae Hordeum Hordeum vulgare (Barley) |
| Enzyme Sequence | MANKHLSLSLFLVLLGLSASLASGQVLFQGFNWESWKHNGGWYNFLMGKVDDIAAAGITHVWLPPASQSVAEQGYMPGRLYDLDASKYGNKAQLKSLIGALHGKGVKAIADIVINHRTAEHKDGRGIYCIFEGGTPDARLDWGPHMICRDDRPYADGTGNPDTGADFGAAPDIDHLNLRVQKELVEWLNWLKADIGFDGWRFDFAKGYSADVAKIYIDRSEPSFAVAEIWTSLAYGGDGKPNLNQDQHRQELVNWVDKVGGKGPATTFDFTTKGILNVAVEGELWRLRGTDGKAPGMIGWWPAKAVTFVDNHDTGSTQHMWPFPSDRVMQGYAYILTHPGTPCIFYDHFFDWGLKEEIDRLVSVRTRHGIHNESKLQIIEADADLYLAEIDGKVIVKLGPRYDVGNLIPGGFKVAAHGNDYAVWEKI |
| Enzyme Length | 427 |
| Uniprot Accession Number | P04063 |
| Absorption | |
| Active Site | ACT_SITE 203; /note=Nucleophile; /evidence=ECO:0000305|PubMed:9571044; ACT_SITE 228; /note=Proton donor; /evidence=ECO:0000305|PubMed:9571044 |
| Activity Regulation | |
| Binding Site | BINDING 230; /note=Substrate; /evidence=ECO:0000305|PubMed:9571044; BINDING 232; /note=Substrate; /evidence=ECO:0000305|PubMed:9571044; BINDING 250; /note=Substrate; /evidence=ECO:0000305|PubMed:9571044; BINDING 257; /note=Substrate; /evidence=ECO:0000305|PubMed:9571044; BINDING 293; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00693; BINDING 312; /note=Substrate; /evidence=ECO:0000305|PubMed:9571044; BINDING 318; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00693; BINDING 397; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00693; BINDING 424; /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 | |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (21); Binding site (9); Chain (1); Helix (19); Metal binding (14); Region (4); Sequence conflict (2); Signal peptide (1); Site (1); Turn (5) |
| Keywords | 3D-structure;Calcium;Carbohydrate metabolism;Germination;Glycosidase;Hydrolase;Metal-binding;Signal |
| Interact With | |
| Induction | INDUCTION: Type B isozyme mRNA is undetectable in unstimulated cells and increases a hundred-fold after stimulation with gibberellic acid. |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..24 |
| Structure 3D | X-ray crystallography (3) |
| Cross Reference PDB | 1AMY; 1AVA; 1BG9; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 47,356 |
| Kinetics | |
| Metal Binding | METAL 115; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:8196040, ECO:0000269|PubMed:9571044, ECO:0000269|PubMed:9634702, ECO:0007744|PDB:1AVA"; METAL 132; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:8196040, ECO:0000269|PubMed:9571044, ECO:0000269|PubMed:9634702, ECO:0007744|PDB:1AVA"; METAL 135; /note="Calcium 2; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:8196040, ECO:0000269|PubMed:9571044, ECO:0000269|PubMed:9634702, ECO:0007744|PDB:1AVA"; METAL 137; /note="Calcium 2; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:8196040, ECO:0000269|PubMed:9571044, ECO:0000269|PubMed:9634702, ECO:0007744|PDB:1AVA"; METAL 141; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:8196040, ECO:0000269|PubMed:9571044, ECO:0000269|PubMed:9634702, ECO:0007744|PDB:1AVA"; METAL 151; /note="Calcium 3"; /evidence="ECO:0000269|PubMed:8196040, ECO:0000269|PubMed:9571044, ECO:0000269|PubMed:9634702, ECO:0007744|PDB:1AVA"; METAL 162; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:8196040, ECO:0000269|PubMed:9571044, ECO:0000269|PubMed:9634702, ECO:0007744|PDB:1AVA"; METAL 165; /note="Calcium 1; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:8196040, ECO:0000269|PubMed:9571044, ECO:0000269|PubMed:9634702, ECO:0007744|PDB:1AVA"; METAL 166; /note="Calcium 3"; /evidence="ECO:0000269|PubMed:8196040, ECO:0000269|PubMed:9571044, ECO:0000269|PubMed:9634702, ECO:0007744|PDB:1AVA"; METAL 167; /note="Calcium 3; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:8196040, ECO:0000269|PubMed:9571044, ECO:0000269|PubMed:9634702, ECO:0007744|PDB:1AVA"; METAL 170; /note="Calcium 3; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:8196040, ECO:0000269|PubMed:9571044, ECO:0000269|PubMed:9634702, ECO:0007744|PDB:1AVA"; METAL 172; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:8196040, ECO:0000269|PubMed:9571044, ECO:0000269|PubMed:9634702, ECO:0007744|PDB:1AVA"; METAL 172; /note="Calcium 3"; /evidence="ECO:0000269|PubMed:8196040, ECO:0000269|PubMed:9571044, ECO:0000269|PubMed:9634702, ECO:0007744|PDB:1AVA"; METAL 207; /note="Calcium 1; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:8196040, ECO:0000269|PubMed:9571044, ECO:0000269|PubMed:9634702, ECO:0007744|PDB:1AVA" |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.1; |