IED ID | IndEnz0018000985 |
Enzyme Type ID | peroxidase000985 |
Protein Name |
Catalase EC 1.11.1.6 |
Gene Name | katA DR_1998 |
Organism | Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422) |
Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Deinococcus-Thermus Deinococci Deinococcales Deinococcaceae Deinococcus Deinococcus radiodurans Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422) |
Enzyme Sequence | MSDENNKGVGTAVQGVGGPRDGRTAPGEQGTTLTTRQGHPVHDNQNSRTVGSRGPMTLENYQFIEKLSHFDRERIPERVVHARGVGAHGVFRATGKVGDEPVSKYTRAKLFQEDGKETPVFVRFSTVGHGTHSPETLRDPRGFAVKFYTEDGNWDLVGNNLKIFFIRDALKFPDLIHSQKPSPTTNIQSQERIFDFFAGSPEATHMITLLYSPWGIPASYRFMQGSGVNTYKWVNDQGEGVLVKYHWEPVQGVRNLTQMQADEVQATNFNHATQDLHDAIERGDFPQWDLFVQIMEDGEHPELDFDPLDDTKIWPREQFPWRHVGQMTLNRNPENVFAETEQAAFGTGVLVDGLDFSDDKMLQGRTFSYSDTQRYRVGPNYLQLPINAPKKHVATNQRDGQMAYRVDTFEGQDQRVNYEPSLLSGPKEAPRRAPEHTPRVEGNLVRAAIERPNPFGQAGMQYRNFADWERDELVSNLSGALAGVDKRIQDKMLEYFTAADADYGQRVREGIQAKEAEMKGQKQEAPVYGTEASSLY |
Enzyme Length | 536 |
Uniprot Accession Number | Q59337 |
Absorption | |
Active Site | ACT_SITE 81; /evidence=ECO:0000250; ACT_SITE 159; /evidence=ECO:0000250 |
Activity Regulation | ACTIVITY REGULATION: Strongly inhibited by sodium azide and sodium cyanide, and slightly inhibited by 3-amino-1,2,4-triazole. {ECO:0000269|PubMed:16716939}. |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.6; |
DNA Binding | |
EC Number | 1.11.1.6 |
Enzyme Function | FUNCTION: Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide. {ECO:0000269|PubMed:16716939}. |
Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30 degrees Celsius. Active over a temperature range from 20 to 70 degrees Celsius. Retains 100% of its initial activity following incubation at 40 degrees Celsius, and 82% of its activity following incubation at 50 degrees Celsius. The activity decreases significantly to 30% of the initial activity following incubation at 60 degrees Celsius. {ECO:0000269|PubMed:16716939}; |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Beta strand (16); Chain (1); Compositional bias (1); Helix (18); Metal binding (1); Region (3); Sequence conflict (4); Turn (4) |
Keywords | 3D-structure;Cytoplasm;Heme;Hydrogen peroxide;Iron;Metal-binding;Oxidoreductase;Peroxidase;Reference proteome |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | X-ray crystallography (1) |
Cross Reference PDB | 4CAB; |
Mapped Pubmed ID | 24975828; |
Motif | |
Gene Encoded By | |
Mass | 60,513 |
Kinetics | |
Metal Binding | METAL 369; /note=Iron (heme axial ligand); /evidence=ECO:0000250 |
Rhea ID | RHEA:20309 |
Cross Reference Brenda |