| IED ID | IndEnz0007000004 |
| Enzyme Type ID | catalase000004 |
| Protein Name |
Peroxisomal catalase 1 EC 1.11.1.6 Catalase-2 |
| Gene Name | ctl-2 cat cat-1 Y54G11A.5 |
| Organism | Caenorhabditis elegans |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Nematoda (roundworms) Chromadorea Rhabditida Rhabditina Rhabditomorpha Rhabditoidea Rhabditidae Peloderinae Caenorhabditis Caenorhabditis elegans |
| Enzyme Sequence | MPNDPSDNQLKTYKETYPKPQVITTSNGAPIYSKTAVLTAGRRGPMLMQDVVYMDEMAHFDRERIPERVVHAKGAGAHGYFEVTHDISKYCKADIFNKVGKQTPLLIRFSTVGGESGSADTARDPRGFAIKFYTEEGNWDLVGNNTPIFFIRDPIHFPNFIHTQKRNPQTHLKDPNMIFDFWLHRPEALHQVMFLFSDRGLPDGYRHMNGYGSHTFKMVNKDGKAIYVKFHFKPTQGVKNLTVEKAGQLASSDPDYSIRDLFNAIEKGDFPVWKMFIQVMTFEQAEKWEFNPFDVTKVWPHGDYPLIEVGKMVLNRNPRNYFAEVEQSAFCPAHIVPGIEFSPDKMLQGRIFSYTDTHFHRLGPNYIQLPVNCPYRSRAHNTQRDGAMAYDNQQHAPNFFPNSFNYGKTRPDVKDTTFPATGDVDRYESGDDNNYDQPRQFWEKVLDTGARERMCQNFAGPLGECHDFIIKGMIDHFSKVHPDFGARVKALIQKQARSHI |
| Enzyme Length | 500 |
| Uniprot Accession Number | Q27487 |
| Absorption | |
| Active Site | ACT_SITE 71; /evidence=ECO:0000255|PROSITE-ProRule:PRU10013; ACT_SITE 144; /evidence=ECO:0000255|PROSITE-ProRule:PRU10013 |
| Activity Regulation | |
| 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; Evidence={ECO:0000255|PROSITE-ProRule:PRU10013, ECO:0000269|PubMed:10691967, ECO:0000269|PubMed:14996832}; |
| DNA Binding | |
| EC Number | 1.11.1.6 |
| Enzyme Function | FUNCTION: Peroxisomal catalase involved in the oxidative stress response serving to protect cells from toxicity (PubMed:25243607, PubMed:28456303). Plays a role in maintaining normal lifespan (PubMed:14996832). Plays a role in regulating the response to pathogens such as E.faecalis (PubMed:17483415). {ECO:0000269|PubMed:14996832, ECO:0000269|PubMed:17483415, ECO:0000269|PubMed:25243607, ECO:0000269|PubMed:28456303}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6. {ECO:0000269|PubMed:10691967}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Metal binding (1); Motif (1); Sequence conflict (1) |
| Keywords | Heme;Hydrogen peroxide;Iron;Metal-binding;Oxidoreductase;Peroxidase;Peroxisome;Reference proteome |
| Interact With | |
| Induction | INDUCTION: Up-regulated in response to Cu(2+) (PubMed:25243607). Up-regulated in response to phoxim (an organophosphorus insecticide) and carbaryl (a carbamate insecticide) (PubMed:28456303). {ECO:0000269|PubMed:25243607, ECO:0000269|PubMed:28456303}. |
| Subcellular Location | SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:10691967}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10778742; 12845331; 19627265; 21085631; 21177967; 21367940; 21849976; 22267497; 22369044; 22560298; 22921415; 23800452; 24884423; 25487147; 25635455; 27506200; 29348603; 30567997; 6593563; |
| Motif | MOTIF 498..500; /note=Microbody targeting signal |
| Gene Encoded By | |
| Mass | 57,467 |
| Kinetics | |
| Metal Binding | METAL 354; /note=Iron (heme axial ligand); /evidence=ECO:0000250 |
| Rhea ID | RHEA:20309 |
| Cross Reference Brenda |