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; |