Detail Information for IndEnz0001000555
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;