| IED ID | IndEnz0001000590 |
| Enzyme Type ID | amylase000590 |
| Protein Name |
Alpha-amylase EC 3.2.1.1 1,4-alpha-D-glucan glucanohydrolase allergen Aca s 4 |
| Gene Name | |
| Organism | Acarus siro (Flour mite) (Tyroglyphus farinae) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Chelicerata Arachnida Acari Acariformes Sarcoptiformes Astigmata Acaroidea Acaridae Acarinae Acarus Acarus siro (Flour mite) (Tyroglyphus farinae) |
| Enzyme Sequence | MAHLLLAVVAITLALSQSVFGGSPYSNPHFTGSRSVITHLMQWKFDDIAAECERFLGPKGYGGIQLSPVNEHAVLGNRPWYELYQPVGYKIQSRSGNEEQFKGMVQRCNKVGVRIYVDIVMNHMSGAQEGHGNCWFKLQWHHDVSRCSLLVPNDFHGRESCHTDNMDIKNYDNPEEARNCRLSGLRDLKQSSEYVRQKQADFLNHLIDLGVAGSRSDASKHMWPGDLEAIYGKLHNLNTAYFPANSRPFIYHEVIYYGGDGIKSSDYTKLGRAIEFHFYRDIANVVRRHNQLKTVKNFGQPWGMVPSDDALVMVDSHDLQRFHTGQVGVNINYFESRLLKVATAFMLAWPYGVPRVMSSYHWDQKIEDGKDKNDWIGPPSDGSGNILSVTPQPDDTCNKEWICEHRWRQIYNMVHFRNVAGNEAVSHWWDNGDYQIAFGRGSKAFIAINLQDGQGLNRKLATGLPQGTYCDLVTGNLAGGKCTGGTVTVDGSGNADINIAKTAEDPFVAIHVEAKLH |
| Enzyme Length | 517 |
| Uniprot Accession Number | B0KZK1 |
| Absorption | |
| Active Site | ACT_SITE 217; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P56634; ACT_SITE 253; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:P56634 |
| Activity Regulation | ACTIVITY REGULATION: Activated by chloride ions. Inhibited by acarbose. Not inhibited by wheat alpha-amylase inhibitors 1 (WI-1, the tetrameric form) or 3 (WI-3, the monomeric form) and bean alpha-amylase inhibitor 1 (alphaAI-1). {ECO:0000269|PubMed:22292590}. |
| Binding Site | BINDING 215; /note=Chloride; /evidence=ECO:0000250|UniProtKB:P56634; BINDING 355; /note=Chloride; /evidence=ECO:0000250|UniProtKB:P56634 |
| 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:0000255|RuleBase:RU361134, ECO:0000269|PubMed:22292590}; |
| DNA Binding | |
| EC Number | 3.2.1.1 |
| Enzyme Function | |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5. Active in slightly acidic to neutral pH range. {ECO:0000269|PubMed:22292590}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Binding site (2); Chain (1); Disulfide bond (3); Metal binding (4); Signal peptide (1); Site (1) |
| Keywords | Allergen;Calcium;Carbohydrate metabolism;Chloride;Direct protein sequencing;Disulfide bond;Glycosidase;Hydrolase;Metal-binding;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:22292590}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..21; /evidence="ECO:0000255, ECO:0000269|PubMed:22292590" |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 58,092 |
| Kinetics | |
| Metal Binding | METAL 122; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P56634; METAL 178; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P56634; METAL 187; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P56634; METAL 221; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P56634 |
| Rhea ID | |
| Cross Reference Brenda |