| IED ID | IndEnz0001000260 |
| Enzyme Type ID | amylase000260 |
| Protein Name |
Maltogenic alpha-amylase EC 3.2.1.133 Glucan 1,4-alpha-maltohydrolase |
| Gene Name | amyM |
| Organism | Geobacillus stearothermophilus (Bacillus stearothermophilus) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Geobacillus Geobacillus stearothermophilus (Bacillus stearothermophilus) |
| Enzyme Sequence | MKKKTLSLFVGLMLLIGLLFSGSLPYNPNAAEASSSASVKGDVIYQIIIDRFYDGDTTNNNPAKSYGLYDPTKSKWKMYWGGDLEGVRQKLPYLKQLGVTTIWLSPVLDNLDTLAGTDNTGYHGYWTRDFKQIEEHFGNWTTFDTLVNDAHQNGIKVIVDFVPNHSTPFKANDSTFAEGGALYNNGTYMGNYFDDATKGYFHHNGDISNWDDRYEAQWKNFTDPAGFSLADLSQENGTIAQYLTDAAVQLVAHGADGLRIDAVKHFNSGFSKSLADKLYQKKDIFLVGEWYGDDPGTANHLEKVRYANNSGVNVLDFDLNTVIRNVFGTFTQTMYDLNNMVNQTGNEYKYKENLITFIDNHDMSRFLSVNSNKANLHQALAFILTSRGTPSIYYGTEQYMAGGNDPYNRGMMPAFDTTTTAFKEVSTLAGLRRNNAAIQYGTTTQRWINNDVYIYERKFFNDVVLVAINRNTQSSYSISGLQTALPNGSYADYLSGLLGGNGISVSNGSVASFTLAPGAVSVWQYSTSASAPQIGSVAPNMGIPGNVVTIDGKGFGTTQGTVTFGGVTATVKSWTSNRIEVYVPNMAAGLTDVKVTAGGVSSNLYSYNILSGTQTSVVFTVKSAPPTNLGDKIYLTGNIPELGNWSTDTSGAVNNAQGPLLAPNYPDWFYVFSVPAGKTIQFKFFIKRADGTIQWENGSNHVATTPTGATGNITVTWQN |
| Enzyme Length | 719 |
| Uniprot Accession Number | P19531 |
| Absorption | |
| Active Site | ACT_SITE 261; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P13507; ACT_SITE 289; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:P13507 |
| Activity Regulation | |
| Binding Site | BINDING 126; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P0C1B3; BINDING 165; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P0C1B3; BINDING 259; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P0C1B3; BINDING 292; /note=Substrate; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:P0C1B3; BINDING 362; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P0C1B3; BINDING 409; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P0C1B3 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive alpha-maltose residues from the non-reducing ends of the chains.; EC=3.2.1.133; |
| DNA Binding | |
| EC Number | 3.2.1.133 |
| Enzyme Function | FUNCTION: Converts starch into maltose. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (36); Binding site (6); Chain (1); Domain (2); Helix (21); Metal binding (15); Region (1); Sequence conflict (4); Signal peptide (1); Site (1); Turn (8) |
| Keywords | 3D-structure;Calcium;Carbohydrate metabolism;Direct protein sequencing;Glycosidase;Hydrolase;Metal-binding;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..33; /evidence=ECO:0000269|Ref.1 |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 1QHO; 1QHP; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 78,676 |
| Kinetics | |
| Metal Binding | METAL 54; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:10387084, ECO:0007744|PDB:1QHO"; METAL 56; /note="Calcium 1; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:10387084, ECO:0007744|PDB:1QHO"; METAL 59; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:10387084, ECO:0007744|PDB:1QHO"; METAL 60; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:10387084, ECO:0007744|PDB:1QHO"; METAL 81; /note="Calcium 1; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:10387084, ECO:0007744|PDB:1QHO"; METAL 83; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:10387084, ECO:0007744|PDB:1QHO"; METAL 109; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:10387084, ECO:0007744|PDB:1QHO"; METAL 110; /note="Calcium 2; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:10387084, ECO:0007744|PDB:1QHO"; METAL 112; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:10387084, ECO:0007744|PDB:1QHO"; METAL 134; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:10387084, ECO:0007744|PDB:1QHO"; METAL 135; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:10387084, ECO:0007744|PDB:1QHO"; METAL 164; /note="Calcium 3"; /evidence="ECO:0000269|PubMed:10387084, ECO:0007744|PDB:1QHO"; METAL 217; /note="Calcium 3; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:10387084, ECO:0007744|PDB:1QHO"; METAL 231; /note="Calcium 3"; /evidence="ECO:0000269|PubMed:10387084, ECO:0007744|PDB:1QHO"; METAL 265; /note="Calcium 3; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:10387084, ECO:0007744|PDB:1QHO" |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.133; |