| IED ID | IndEnz0007000414 |
| Enzyme Type ID | catalase000414 |
| Protein Name |
DNA protection during starvation protein EC 1.16.-.- |
| Gene Name | dps SF0763 S0805 |
| Organism | Shigella flexneri |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Shigella Shigella flexneri |
| Enzyme Sequence | MSTAKLVKSKATNLLYTRNDVSDSEKKATVELLNRQVIQFIDLSLITKQAHWNMRGANFIAVHEMLDGFRTALIDHLDTMAERAVQLGGVALGTTQVINSKTPLKSYPLDIHNVQDHLKELADRYAIVANDVRKAIGEAKDDDTADILTAASRDLDKFLWFIESNIE |
| Enzyme Length | 167 |
| Uniprot Accession Number | P0ABT4 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=2 Fe(2+) + 2 H(+) + H2O2 = 2 Fe(3+) + 2 H2O; Xref=Rhea:RHEA:48712, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; |
| DNA Binding | |
| EC Number | 1.16.-.- |
| Enzyme Function | FUNCTION: During stationary phase, binds the chromosome non-specifically, forming a highly ordered and stable dps-DNA co-crystal within which chromosomal DNA is condensed and protected from diverse damages. It protects DNA from oxidative damage by sequestering intracellular Fe(2+) ion and storing it in the form of Fe(3+) oxyhydroxide mineral, which can be released after reduction. One hydrogen peroxide oxidizes two Fe(2+) ions, which prevents hydroxyl radical production by the Fenton reaction. Dps also protects the cell from UV and gamma irradiation, iron and copper toxicity, thermal stress and acid and base shocks. Also shows a weak catalase activity (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Initiator methionine (1); Metal binding (4) |
| Keywords | Cytoplasm;DNA condensation;DNA-binding;Iron;Iron storage;Metal-binding;Oxidoreductase;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm, nucleoid {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 18,695 |
| Kinetics | |
| Metal Binding | METAL 51; /note=Iron 1; shared with dodecameric partner; /evidence=ECO:0000250; METAL 78; /note=Iron 1; /evidence=ECO:0000250; METAL 82; /note=Iron 1; /evidence=ECO:0000250; METAL 82; /note=Iron 2; /evidence=ECO:0000250 |
| Rhea ID | RHEA:48712 |
| Cross Reference Brenda |