IED Industry Enzyme Database

Detail Information for IndEnz0001000004
IED ID IndEnz0001000004
Enzyme Type ID amylase000004
Protein Name Alpha-amylase type A isozyme
EC 3.2.1.1
1,4-alpha-D-glucan glucanohydrolase
HvAMY1
Low pI alpha-amylase
Gene Name AMY1.1
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 MGKNGSLCCFSLLLLLLLAGLASGHQVLFQGFNWESWKQSGGWYNMMMGKVDDIAAAGVTHVWLPPPSHSVSNEGYMPGRLYDIDASKYGNAAELKSLIGALHGKGVQAIADIVINHRCADYKDSRGIYCIFEGGTSDGRLDWGPHMICRDDTKYSDGTANLDTGADFAAAPDIDHLNDRVQRELKEWLLWLKSDLGFDAWRLDFARGYSPEMAKVYIDGTSPSLAVAEVWDNMATGGDGKPNYDQDAHRQNLVNWVDKVGGAASAGMVFDFTTKGILNAAVEGELWRLIDPQGKAPGVMGWWPAKAATFVDNHDTGSTQAMWPFPSDKVMQGYAYILTHPGIPCIFYDHFFNWGFKDQIAALVAIRKRNGITATSALKILMHEGDAYVAEIDGKVVVKIGSRYDVGAVIPAGFVTSAHGNDYAVWEKNGAAATLQRS
Enzyme Length 438
Uniprot Accession Number P00693
Absorption
Active Site ACT_SITE 204; /note="Nucleophile"; /evidence="ECO:0000305|PubMed:16030022, ECO:0000305|PubMed:7901200"; ACT_SITE 229; /note="Proton donor"; /evidence="ECO:0000305|PubMed:7901200"
Activity Regulation ACTIVITY REGULATION: Redox-insensitive. {ECO:0000269|PubMed:24089528}.
Binding Site BINDING 231; /note="Substrate"; /evidence="ECO:0000305|PubMed:16030022"; BINDING 233; /note="Substrate"; /evidence="ECO:0000305|PubMed:16030022"; BINDING 251; /note="Substrate"; /evidence="ECO:0000305|PubMed:12906828, ECO:0000305|PubMed:16030022"; BINDING 258; /note="Substrate"; /evidence="ECO:0000305|PubMed:16030022, ECO:0000305|PubMed:17803687"; BINDING 295; /note="Substrate"; /evidence="ECO:0000305|PubMed:16030022"; BINDING 314; /note="Substrate"; /evidence="ECO:0000305|PubMed:16030022"; BINDING 320; /note="Substrate"; /evidence="ECO:0000305|PubMed:16030022"; BINDING 399; /note="Substrate"; /evidence="ECO:0000305|PubMed:12906828, ECO:0000305|PubMed:16030022"; BINDING 426; /note="Substrate"; /evidence="ECO:0000305|PubMed:16030022"
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:0000269|PubMed:16030022, ECO:0000269|PubMed:18588886, ECO:0000269|PubMed:24089528, ECO:0000269|PubMed:7901200};
DNA Binding
EC Number 3.2.1.1
Enzyme Function FUNCTION: Alpha-amylase displaying a robust amylolytic activity toward p-nitrophenyl maltoheptaoside (BPNP-G7), amylopectin and beta-limit dextrin (PubMed:24089528). {ECO:0000269|PubMed:24089528}.
Temperature Dependency
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5 with p-nitrophenyl maltoheptaoside or amylopectin as substrate. {ECO:0000269|PubMed:24089528};
Pathway
nucleotide Binding
Features Active site (2); Beta strand (20); Binding site (9); Chain (1); Helix (20); Metal binding (14); Mutagenesis (11); Region (6); Signal peptide (1); Site (1); Turn (5)
Keywords 3D-structure;Calcium;Carbohydrate metabolism;Germination;Glycosidase;Hydrolase;Metal-binding;Secreted;Signal
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted, extracellular space.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..24
Structure 3D X-ray crystallography (9)
Cross Reference PDB 1HT6; 1P6W; 1RP8; 1RP9; 1RPK; 2QPS; 2QPU; 3BSG; 3BSH;
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 47,796
Kinetics
Metal Binding METAL 116; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:12906828, ECO:0000269|PubMed:16030022, ECO:0000269|PubMed:17803687, ECO:0000269|PubMed:18588886"; METAL 133; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:12906828, ECO:0000269|PubMed:16030022, ECO:0000269|PubMed:17803687, ECO:0000269|PubMed:18588886"; METAL 136; /note="Calcium 2; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:12906828, ECO:0000269|PubMed:16030022, ECO:0000269|PubMed:17803687, ECO:0000269|PubMed:18588886"; METAL 138; /note="Calcium 2; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:12906828, ECO:0000269|PubMed:16030022, ECO:0000269|PubMed:17803687, ECO:0000269|PubMed:18588886"; METAL 142; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:12906828, ECO:0000269|PubMed:16030022, ECO:0000269|PubMed:17803687, ECO:0000269|PubMed:18588886"; METAL 152; /note="Calcium 3"; /evidence="ECO:0000269|PubMed:12906828, ECO:0000269|PubMed:16030022, ECO:0000269|PubMed:17803687, ECO:0000269|PubMed:18588886"; METAL 163; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:12906828, ECO:0000269|PubMed:16030022, ECO:0000269|PubMed:17803687, ECO:0000269|PubMed:18588886"; METAL 166; /note="Calcium 1; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:12906828, ECO:0000269|PubMed:16030022, ECO:0000269|PubMed:17803687, ECO:0000269|PubMed:18588886"; METAL 167; /note="Calcium 3"; /evidence="ECO:0000269|PubMed:12906828, ECO:0000269|PubMed:16030022, ECO:0000269|PubMed:17803687, ECO:0000269|PubMed:18588886"; METAL 168; /note="Calcium 3; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:12906828, ECO:0000269|PubMed:16030022, ECO:0000269|PubMed:17803687, ECO:0000269|PubMed:18588886"; METAL 171; /note="Calcium 3; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:12906828, ECO:0000269|PubMed:16030022, ECO:0000269|PubMed:17803687, ECO:0000269|PubMed:18588886"; METAL 173; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:12906828, ECO:0000269|PubMed:16030022, ECO:0000269|PubMed:17803687, ECO:0000269|PubMed:18588886"; METAL 173; /note="Calcium 3"; /evidence="ECO:0000269|PubMed:12906828, ECO:0000269|PubMed:16030022, ECO:0000269|PubMed:17803687, ECO:0000269|PubMed:18588886"; METAL 208; /note="Calcium 1; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:12906828, ECO:0000269|PubMed:16030022, ECO:0000269|PubMed:17803687, ECO:0000269|PubMed:18588886"
Rhea ID
Cross Reference Brenda 3.2.1.1;