| IED ID | IndEnz0001000322 |
| Enzyme Type ID | amylase000322 |
| Protein Name |
4-alpha-glucanotransferase EC 2.4.1.25 Amylomaltase Disproportionating enzyme D-enzyme Maltodextrin glycosyltransferase |
| Gene Name | mgtA |
| Organism | Thermotoga neapolitana |
| Taxonomic Lineage | cellular organisms Bacteria Thermotogae Thermotogae Thermotogales Thermotogaceae Thermotoga Thermotoga neapolitana |
| Enzyme Sequence | MIGYQIYVRSFRDGNFDGVGDFKGLKGAISYLKELGVDFVWLMPVFSSISFHGYDVVDFYSFKAEYGDEKDFREMIEAFHDNGIKVVLDLPIHHTGFLHTWFQKALKGDPHYRDYYVWASEKTDLDERREWDNERIWHPLEDGRFYRGLFGPLSPDLNYDNPQVFEEMKKVVYHLLEMGVDGFRFDAAKHMRDTLEQNVRFWRYFLSDIEGIFLAEIWAESKVVDEHGRIFGYMLNFDTSHCIKEAVWKENFKVLIESIERALVGKDYLPVNFTSNHDMSRLASFEGGLSEEKVKLSLSILFTLPGVPLIFYGDELGMKGIYRKPNTEVVLDPFPWSENISLEGQTFWKWPAYNSPFSGVSVEYQKKKRDSILLHIMKWTGFRKENHWLDRANIEFLCKEEKLLHVYRLVDEGRSLKVIHNLSNGEMVFEGVRVQPYSTEVI |
| Enzyme Length | 442 |
| Uniprot Accession Number | O86956 |
| Absorption | |
| Active Site | ACT_SITE 186; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 216; /note=Proton donor; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan.; EC=2.4.1.25; Evidence={ECO:0000269|Ref.1}; |
| DNA Binding | |
| EC Number | 2.4.1.25 |
| Enzyme Function | FUNCTION: Hydrolyzes the 1,4-alpha-glycoside bonds in oligomeric and polymeric 1,4-alpha-glucans and transfers oligosaccharides (maltotriose being the shortest one) to acceptor maltodextrins. {ECO:0000269|Ref.1}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 85 degrees Celsius. {ECO:0000269|Ref.1}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. {ECO:0000269|Ref.1}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Metal binding (5); Site (1) |
| Keywords | Calcium;Carbohydrate metabolism;Cytoplasm;Glycosyltransferase;Metal-binding;Transferase |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 51,935 |
| Kinetics | |
| Metal Binding | METAL 13; /note=Calcium; /evidence=ECO:0000250; METAL 15; /note=Calcium; /evidence=ECO:0000250; METAL 17; /note=Calcium; /evidence=ECO:0000250; METAL 19; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 21; /note=Calcium; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |