| IED ID | IndEnz0001000599 |
| Enzyme Type ID | amylase000599 |
| Protein Name |
Alpha-amylase EC 3.2.1.1 |
| Gene Name | |
| Organism | Oryzias latipes (Japanese rice fish) (Japanese killifish) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Actinopterygii Actinopteri Neopterygii Teleostei Osteoglossocephalai Clupeocephala Euteleosteomorpha Neoteleostei Eurypterygia Ctenosquamata Acanthomorphata Euacanthomorphacea Percomorphaceae Ovalentaria Atherinomorphae Beloniformes (medakas needlefish and others) Adrianichthyoidei Adrianichthyidae Oryziinae (medakas) Oryzias Oryzias latipes (Japanese rice fish) (Japanese killifish) |
| Enzyme Sequence | MKLFVLIALFGLGFAQHNPNTRDGRTAIVHLFEWRWADIAAECERFLGPKGFAGVQISPPNEHILVSSPWRPWWQRYQPISYNLCSRSGGENELRDMITRCNNVGVNVYVDAVINHMCGAGGGEGTHSSCGSWFNANNKDFPSVPYSNLDFNDGKCKTGSGNIENYGDPYQVRDCRLVGLLDLALEKDYVRGKVADFMNKLIDMGVAGFRVDACKHMWPGDLDNVYRRLNNLNTKWFPGGSRPFIFQEVIDLGGEPITTGEYVGLGRVTEFKYGARLGELFRKWNGQKLSYTKNWGEGWGFMADGNAVVFTDNHDNQRGHGAGGASILTFWDPRLYKMAVGYMLAHPYGFTRVMSSYSWDRNFVNGKDENDWIGPPSNGDGSTKPVPINPDQTCGDGWVCEHRWRQIMNMVQFRNVVNGQPHANWWDNGNNQVAFGRGNRGFIVFNNDDWALDVTLNTGLPGGTYCDVISGNKDGGSCTGKQITVGGDGRAHFYINNSEEDPFIAIHADSKL |
| Enzyme Length | 512 |
| Uniprot Accession Number | H2N0D4 |
| Absorption | |
| Active Site | ACT_SITE 212; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P04746; ACT_SITE 248; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:P04746 |
| Activity Regulation | |
| Binding Site | BINDING 210; /note="Chloride"; /evidence="ECO:0000269|PubMed:22613096, ECO:0007744|PDB:3VM5"; BINDING 352; /note="Chloride"; /evidence="ECO:0000269|PubMed:22613096, ECO:0007744|PDB:3VM5" |
| 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:22613096}; |
| DNA Binding | |
| EC Number | 3.2.1.1 |
| Enzyme Function | FUNCTION: Catalyzes the hydrolysis of alpha-1,4 glycosidic linkages in starch, glycogen and similar oligosaccharides. {ECO:0000269|PubMed:22613096}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. {ECO:0000269|PubMed:22613096}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.1. {ECO:0000269|PubMed:22613096}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (27); Binding site (2); Chain (1); Disulfide bond (5); Glycosylation (1); Helix (21); Metal binding (4); Signal peptide (1); Site (1); Turn (8) |
| Keywords | 3D-structure;Calcium;Carbohydrate metabolism;Chloride;Disulfide bond;Glycoprotein;Glycosidase;Hydrolase;Metal-binding;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..15; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 3VM5; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 57,167 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.18 mg/ml for potato amylopectin {ECO:0000269|PubMed:22613096}; Vmax=2560 umol/min/mg enzyme {ECO:0000269|PubMed:22613096}; |
| Metal Binding | METAL 115; /note="Calcium"; /evidence="ECO:0000269|PubMed:22613096, ECO:0007744|PDB:3VM5"; METAL 173; /note="Calcium; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:22613096, ECO:0007744|PDB:3VM5"; METAL 182; /note="Calcium"; /evidence="ECO:0000269|PubMed:22613096, ECO:0007744|PDB:3VM5"; METAL 216; /note="Calcium; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:22613096, ECO:0007744|PDB:3VM5" |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.1; |