| IED ID | IndEnz0001000589 |
| Enzyme Type ID | amylase000589 |
| Protein Name |
Amylosucrase EC 2.4.1.4 |
| Gene Name | ams |
| Organism | Neisseria meningitidis |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Betaproteobacteria Neisseriales Neisseriaceae Neisseria Neisseria meningitidis |
| Enzyme Sequence | MLTPTQQVGLILQYLKTRILDIYTPEQRAGIEKSEDWRQFSRRMDTHFPKLMNELDSVYGNNEALLPMLEMLLAQAWQSYSQRSASLKNIDIERENNPDWILSNKQVGGVCYVDLFAGDLKGLKDKIHYFQELGLTYLHLMPLFKCPEGKSDGGYAVSSYRDVNPALGTIGDLREVIAALHEAGISAVVDFIFNHTSNEHEWAQRCAAGDPLFDNFYYIFPDRRMPDQYDRTLREIFPDQHPGGFSQLEDGRWVWTTFNSFQWDLNYSNPWVFRAMAGEMMFLANLGVDILRMDAVAFIWKQMGTSCENLPQAHALIRAFNAVMRIAAPAVFFKSEAIVHPDQVVQYIGQDECQIGYNPLQMALLWNTLATREVNLLHQALTYRHNLPEHTAWVNYVRSHDDIGWTFADEDAAYLGISGYDHRQFLNRFFVNRFDGSFARGVPFQYNPNTGDCRVSGTSAALAGLAQNDPHAVSRIKLLYSIALSTGGLPLIYLGDEVGTPNDDGWVQDSNKSDDSRWAHRPRYNEALYAQRNDPSTAAGQIYQGLRHMIAVRQSNPRFDGGRLVTFNTNNKHIIGYIRNNALLAFGNFSEYPQTVTAHTLQAMPFKAHDLIGGKTVSLNQDLTLQPYQVMWLEIA |
| Enzyme Length | 636 |
| Uniprot Accession Number | Q84HD6 |
| Absorption | |
| Active Site | ACT_SITE 294; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:Q9ZEU2; ACT_SITE 336; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:Q9ZEU2 |
| Activity Regulation | |
| Binding Site | BINDING 152; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9ZEU2; BINDING 195; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9ZEU2; BINDING 262; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9ZEU2; BINDING 292; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9ZEU2; BINDING 400; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9ZEU2; BINDING 401; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9ZEU2; BINDING 517; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9ZEU2 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=[(1->4)-alpha-D-glucosyl](n) + sucrose = [(1->4)-alpha-D-glucosyl](n+1) + D-fructose; Xref=Rhea:RHEA:24572, Rhea:RHEA-COMP:9584, Rhea:RHEA-COMP:9587, ChEBI:CHEBI:15444, ChEBI:CHEBI:17992, ChEBI:CHEBI:37721; EC=2.4.1.4; Evidence={ECO:0000250|UniProtKB:Q9ZEU2}; |
| DNA Binding | |
| EC Number | 2.4.1.4 |
| Enzyme Function | FUNCTION: Catalyzes the synthesis of alpha-glucan from sucrose. Catalyzes, in addition, sucrose hydrolysis, maltose and maltotriose synthesis by successive transfers of the glucosyl moiety of sucrose onto the released glucose, and finally turanose and trehalulose synthesis, these two sucrose isomers being obtained by glucosyl transfer onto fructose (By similarity). {ECO:0000250|UniProtKB:Q9ZEU2}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Binding site (7); Chain (1); Site (1) |
| Keywords | Glycosyltransferase;Secreted;Transferase |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9ZEU2}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 72,340 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:24572 |
| Cross Reference Brenda |