Detail Information for IndEnz0001000592
IED ID IndEnz0001000592
Enzyme Type ID amylase000592
Protein Name Alpha-amylase
EC 3.2.1.1
1,4-alpha-D-glucan glucanohydrolase
Gene Name
Organism Bacillus amyloliquefaciens (Bacillus velezensis)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus subtilis group Bacillus amyloliquefaciens group Bacillus amyloliquefaciens (Bacillus velezensis)
Enzyme Sequence MIQKRKRTVSFRLVLMCTLLFVSLPITKTSAVNGTLMQYFEWYTPNDGQHWKRLQNDAEHLSDIGITAVWIPPAYKGLSQSDNGYGPYDLYDLGEFQQKGTVRTKYGTKSELQDAIGSLHSRNVQVYGDVVLNHKAGADATEDVTAVEVNPANRNQETSEEYQIKAWTDFRFPGRGNTYSDFKWHWYHFDGADWDESRKISRIFKFRGEGKAWDWEVSSENGNYDYLMYADVDYDHPDVVAETKKWGIWYANELSLDGFRIDAAKHIKFSFLRDWVQAVRQATGKEMFTVAEYWQNNAGKLENYLNKTSFNQSVFDVPLHFNLQAASSQGGGYDMRRLLDGTVVSRHPEKAVTFVENHDTQPGQSLESTVQTWFKPLAYAFILTRESGYPQVFYGDMYGTKGTSPKEIPSLKDNIEPILKARKEYAYGPQHDYIDHPDVIGWTREGDSSAAKSGLAALITDGPGGSKRMYAGLKNAGETWYDITGNRSDTVKIGSDGWGEFHVNDGSVSIYVQK
Enzyme Length 514
Uniprot Accession Number P00692
Absorption
Active Site ACT_SITE 262; /note=Nucleophile; ACT_SITE 292; /note=Proton donor
Activity Regulation
Binding Site
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:P29957};
DNA Binding
EC Number 3.2.1.1
Enzyme Function
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Beta strand (30); Chain (1); Helix (15); Metal binding (16); Sequence conflict (4); Signal peptide (1); Site (1); Turn (7)
Keywords 3D-structure;Calcium;Carbohydrate metabolism;Direct protein sequencing;Glycosidase;Hydrolase;Metal-binding;Secreted;Signal
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2830166}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..31; /evidence=ECO:0000269|PubMed:6156671
Structure 3D X-ray crystallography (5)
Cross Reference PDB 1E3X; 1E3Z; 1E40; 1E43; 3BH4;
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 58,403
Kinetics
Metal Binding METAL 133; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:10924103, ECO:0000269|PubMed:20124706, ECO:0007744|PDB:1E40"; METAL 190; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:10924103, ECO:0000269|PubMed:20124706, ECO:0007744|PDB:1E40"; METAL 190; /note="Sodium"; /evidence="ECO:0000269|PubMed:10924103, ECO:0007744|PDB:1E40"; METAL 212; /note="Calcium 2; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:10924103, ECO:0000269|PubMed:20124706, ECO:0007744|PDB:1E40"; METAL 214; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:10924103, ECO:0000269|PubMed:20124706, ECO:0007744|PDB:1E40"; METAL 214; /note="Sodium"; /evidence="ECO:0000269|PubMed:10924103, ECO:0007744|PDB:1E40"; METAL 225; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:10924103, ECO:0000269|PubMed:20124706, ECO:0007744|PDB:1E40"; METAL 225; /note="Sodium"; /evidence="ECO:0000269|PubMed:10924103, ECO:0007744|PDB:1E40"; METAL 231; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:10924103, ECO:0000269|PubMed:20124706, ECO:0007744|PDB:1E40"; METAL 231; /note="Sodium"; /evidence="ECO:0000269|PubMed:10924103, ECO:0007744|PDB:1E40"; METAL 233; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:10924103, ECO:0000269|PubMed:20124706, ECO:0007744|PDB:1E40"; METAL 235; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:10924103, ECO:0000269|PubMed:20124706, ECO:0007744|PDB:1E40"; METAL 266; /note="Calcium 1; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:10924103, ECO:0000269|PubMed:20124706, ECO:0007744|PDB:1E40"; METAL 331; /note="Calcium 3; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:20124706, ECO:0007744|PDB:3BH4"; METAL 438; /note="Calcium 3"; /evidence="ECO:0000269|PubMed:20124706, ECO:0007744|PDB:3BH4"; METAL 461; /note="Calcium 3"; /evidence="ECO:0000269|PubMed:20124706, ECO:0007744|PDB:3BH4"
Rhea ID
Cross Reference Brenda 3.2.1.1;