| IED ID | IndEnz0001000580 |
| Enzyme Type ID | amylase000580 |
| Protein Name |
Pancreatic alpha-amylase PA EC 3.2.1.1 1,4-alpha-D-glucan glucanohydrolase |
| Gene Name | |
| Organism | Struthio camelus (Common ostrich) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Sauropsida Sauria (diapsids) Archelosauria Archosauria Dinosauria Saurischia Theropoda Coelurosauria Aves Palaeognathae Struthioniformes (ostriches) Struthionidae Struthio Struthio camelus (Common ostrich) |
| Enzyme Sequence | QYNPNTQPGRTSIVHLFEWRWADIALECERYLAPYGFGGVQVSPPNENVIITNPYRPWWERYQPVSYKLCTRSGNENEFRDMVTRCNNVGVRIYVDAVKNHMCGSGAGSGTHSTCGAYFNAGNRDSPAVPYSGWDFNDGKCRTGSGEIENYGDASQVRDCRLVGLLDLALEKDYVRSTVAGYMNHLIDIGVAGFRLDAAKHMWPGDIKAFLDKLHNLNTNWFSSGSRPFIYQEVIDLGGEPITSSQYFGNHRVTEFKYGAKLGTVIRKWNGEKMAYLKNWGEGWGFVPSDRALVFVDNHDNQRGHGAGGASILTFWDARLYKMAVGFMLAHPYGFTRVMSSFRWPRHFENGKDVNDWYGPPSNSDGSTKEVTINADSTCGNDWVCEHRWRQIRNMVIFRNVVDGEPFSNWWDNNSNQVAFGRGSKGFIVFNNDDWHMNVDLYTGLPAGTYCDVISGQKEGSRCTGIQVYVSGNGKANFQISNNAEDPFIAIHVGAKL |
| Enzyme Length | 497 |
| Uniprot Accession Number | P83053 |
| Absorption | |
| Active Site | ACT_SITE 197; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P04746; ACT_SITE 233; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:P04746 |
| Activity Regulation | |
| Binding Site | BINDING 195; /note=Chloride; /evidence=ECO:0000250|UniProtKB:P04746; BINDING 298; /note=Chloride; /evidence=ECO:0000250|UniProtKB:P04746; BINDING 337; /note=Chloride; /evidence=ECO:0000250|UniProtKB:P04746 |
| 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|Ref.2}; |
| DNA Binding | |
| EC Number | 3.2.1.1 |
| Enzyme Function | |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Binding site (3); Chain (1); Disulfide bond (5); Metal binding (4); Modified residue (1); Sequence conflict (2); Site (1) |
| Keywords | Calcium;Carbohydrate metabolism;Chloride;Direct protein sequencing;Disulfide bond;Glycosidase;Hydrolase;Metal-binding;Pyrrolidone carboxylic acid;Secreted |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space. |
| Modified Residue | MOD_RES 1; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000269|PubMed:11281265 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 55,898 |
| Kinetics | |
| Metal Binding | METAL 100; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P04746; METAL 158; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P04746; METAL 167; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P04746; METAL 201; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P04746 |
| Rhea ID | |
| Cross Reference Brenda |