| IED ID | IndEnz0001000240 |
| Enzyme Type ID | amylase000240 |
| Protein Name |
Alpha-amylase 1 EC 3.2.1.1 1,4-alpha-D-glucan glucanohydrolase 1 |
| Gene Name | LKA1 |
| Organism | Lipomyces kononenkoae (Yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Lipomycetaceae Lipomyces Lipomyces kononenkoae (Yeast) |
| Enzyme Sequence | MLLINFFIAVLGVISLSPIVVARYILRRDCTTVTVLSSPESVTGSNHVQLASYEMCGSTLSASLYVYNDDYDKIVTLYYLTSSGTTGSTLALILPVWSNNWELWTLSAIAAGAVEITGASYVDSDTSVTYTTSLDLPLTTTSASVPTGTAANWRGRSIYQVVTDRFARTDGSITYSCDVTDRVYCGGSYRGIINMLDYIQGMGFTAIWISPIVENIPDDTGYGYAYHGYWMKDIFALNTNFGGADDLIALATELHNRGMYLMVDIVVNHFAFSGNHADVDYSEYFPYSSQDYFHSFCWITDYSNQTNVEECWLGDDSVPLVDVNTQLDTVKSEYQSWVKQLIANYSIDGLRIDTVKHVQMDFWAPFQEAAGIYTVGEVFDGDPSYTCPYQENLDGVLNYPVYYPVVSAFQRVGGSISSLVDMIDTLKSECIDTTLLGSFLENQDNPRFPSYTSDESLIKNAIAFTILSDGIPIIYYGQEQGLNGGNDPYNREALWPTGYSTTSTFYEYIASLNQIRNHAIYIDDTYLTYQNWVIYSDSTTIAMRKGFTGNQIITVLSNLGSSGSSYTLTLSNTGYTASSVVYEILTCTAVTVDLSGNLAVPMSGGLPRVFYPESQLVGSGICSM |
| Enzyme Length | 624 |
| Uniprot Accession Number | Q01117 |
| Absorption | |
| Active Site | ACT_SITE 353; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P56271; ACT_SITE 377; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:P56271 |
| Activity Regulation | |
| Binding Site | BINDING 230; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P0C1B3; BINDING 269; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P0C1B3; BINDING 351; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P0C1B3; BINDING 381; /note=Substrate; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:P0C1B3; BINDING 444; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P0C1B3; BINDING 491; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P0C1B3 |
| 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:8529895, ECO:0000269|PubMed:8593683}; |
| DNA Binding | |
| EC Number | 3.2.1.1 |
| Enzyme Function | |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Binding site (6); Chain (1); Disulfide bond (4); Domain (1); Erroneous initiation (1); Glycosylation (2); Metal binding (6); Region (1); Signal peptide (1); Site (1) |
| Keywords | Calcium;Carbohydrate metabolism;Direct protein sequencing;Disulfide bond;Glycoprotein;Glycosidase;Hydrolase;Metal-binding;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8529895, ECO:0000269|PubMed:8593683}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..28; /evidence=ECO:0000269|PubMed:8593683 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 68,877 |
| Kinetics | |
| Metal Binding | METAL 268; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P0C1B3; METAL 309; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P56271; METAL 322; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P56271; METAL 353; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:P0C1B3; METAL 357; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P0C1B3; METAL 377; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:P0C1B3 |
| Rhea ID | |
| Cross Reference Brenda |