| IED ID | IndEnz0001000017 |
| Enzyme Type ID | amylase000017 |
| Protein Name |
Alpha-amylase EC 3.2.1.1 1,4-alpha-D-glucan glucanohydrolase |
| Gene Name | amy |
| Organism | Pseudoalteromonas haloplanktis (Alteromonas haloplanktis) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Alteromonadales Pseudoalteromonadaceae Pseudoalteromonas Pseudoalteromonas haloplanktis (Alteromonas haloplanktis) |
| Enzyme Sequence | MKLNKIITTAGLSLGLLLPSIATATPTTFVHLFEWNWQDVAQECEQYLGPKGYAAVQVSPPNEHITGSQWWTRYQPVSYELQSRGGNRAQFIDMVNRCSAAGVDIYVDTLINHMAAGSGTGTAGNSFGNKSFPIYSPQDFHESCTINNSDYGNDRYRVQNCELVGLADLDTASNYVQNTIAAYINDLQAIGVKGFRFDASKHVAASDIQSLMAKVNGSPVVFQEVIDQGGEAVGASEYLSTGLVTEFKYSTELGNTFRNGSLAWLSNFGEGWGFMPSSSAVVFVDNHDNQRGHGGAGNVITFEDGRLYDLANVFMLAYPYGYPKVMSSYDFHGDTDAGGPNVPVHNNGNLECFASNWKCEHRWSYIAGGVDFRNNTADNWAVTNWWDNTNNQISFGRGSSGHMAINKEDSTLTATVQTDMASGQYCNVLKGELSADAKSCSGEVITVNSDGTINLNIGAWDAMAIHKNAKLNTSSASSTESDWQRTVIFINAQTQSGQDMFIRGGIDHAYANANLGRNCQTSNFECAMPIRHNNLKNVTTSPWKANDNYLDWYGIENGQSSEAEGSATDWTTNVWPAGWGAEKTVNTDGFGVTPLNIWGEHYWMLDVDMDCSKAVNGWFELKAFIKNGQGWETAIAQDNAPYTSTNHMAQCGKINKFEFNNSGVVIRSF |
| Enzyme Length | 669 |
| Uniprot Accession Number | P29957 |
| Absorption | |
| Active Site | ACT_SITE 198; /note=Nucleophile; /evidence=ECO:0000269|PubMed:11914073; ACT_SITE 224; /note=Proton donor; /evidence=ECO:0000269|PubMed:11914073 |
| Activity Regulation | ACTIVITY REGULATION: Requires chloride ions for optimal activity. {ECO:0000269|PubMed:12021442}. |
| Binding Site | BINDING 113; /note="Substrate"; /evidence="ECO:0000305|PubMed:11914073"; BINDING 196; /note="Chloride"; /evidence="ECO:0000269|PubMed:11914073, ECO:0000269|PubMed:9541387, ECO:0007744|PDB:1AQH"; BINDING 196; /note="Substrate"; /evidence="ECO:0000250"; BINDING 231; /note="Substrate"; /evidence="ECO:0000305|PubMed:11914073"; BINDING 286; /note="Chloride"; /evidence="ECO:0000269|PubMed:9541387, ECO:0007744|PDB:1AQH"; BINDING 288; /note="Substrate"; /evidence="ECO:0000305|PubMed:11914073"; BINDING 293; /note="Substrate"; /evidence="ECO:0000305|PubMed:11914073"; BINDING 324; /note="Chloride"; /evidence="ECO:0000269|PubMed:11914073, ECO:0000269|PubMed:9541387, ECO:0007744|PDB:1AQH" |
| 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:1544904}; |
| DNA Binding | |
| EC Number | 3.2.1.1 |
| Enzyme Function | |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Thermolabile. {ECO:0000269|PubMed:1544904}; |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (29); Binding site (8); Chain (1); Disulfide bond (4); Helix (21); Metal binding (4); Mutagenesis (1); Propeptide (1); Region (2); Signal peptide (1); Site (1); Turn (3) |
| Keywords | 3D-structure;Calcium;Carbohydrate metabolism;Chloride;Direct protein sequencing;Disulfide bond;Glycosidase;Hydrolase;Metal-binding;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1544904}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..24; /evidence=ECO:0000269|PubMed:1544904 |
| Structure 3D | X-ray crystallography (9) |
| Cross Reference PDB | 1AQH; 1AQM; 1B0I; 1G94; 1G9H; 1JD7; 1JD9; 1KXH; 1L0P; |
| Mapped Pubmed ID | 9862804; |
| Motif | |
| Gene Encoded By | |
| Mass | 73,268 |
| Kinetics | |
| Metal Binding | METAL 112; /note="Calcium"; /evidence="ECO:0000269|PubMed:11914073, ECO:0000269|PubMed:12021442, ECO:0000269|PubMed:9541387, ECO:0007744|PDB:1AQH"; METAL 159; /note="Calcium; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:11914073, ECO:0000269|PubMed:12021442, ECO:0000269|PubMed:9541387, ECO:0007744|PDB:1AQH"; METAL 168; /note="Calcium"; /evidence="ECO:0000269|PubMed:11914073, ECO:0000269|PubMed:12021442, ECO:0000269|PubMed:9541387, ECO:0007744|PDB:1AQH"; METAL 202; /note="Calcium; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:11914073, ECO:0000269|PubMed:12021442, ECO:0000269|PubMed:9541387, ECO:0007744|PDB:1AQH" |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.1; |