| IED ID | IndEnz0018000264 |
| Enzyme Type ID | peroxidase000264 |
| Protein Name |
Catalase-2 EC 1.11.1.6 |
| Gene Name | ctl-1 cat-2 Y54G11A.6 |
| 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 | MPNDPSDNQLKTYKETYPKPQVITTSNGAPIYSKTAVLTAGRRGPMLMQDVVYMDEMAHFDRERIPERVVHAKGAGAHGYFEVTHDITKYCKADMFNKVGKQTPLLVRFSTVAGESGSADTVRDPRGFSLKFYTEEGNWDLVGNNTPIFFIRDAIHFPNFIHALKRNPQTHMRDPNALFDFWMNRPESIHQVMFLYSDRGIPDGFRFMNGYGAHTFKMVNKEGNPIYCKFHFKPAQGSKNLDPTDAGKLASSDPDYAIRDLFNAIESRNFPEWKMFIQVMTFEQAEKWEFNPFDVTKVWPHGDYPLIEVGKMVLNRNVKNYFAEVEQAAFCPAHIVPGIEFSPDKMLQGRIFSYTDTHYHRLGPNYIQLPVNCPYRSRAHTTQRDGAMAYESQGDAPNYFPNSFRGYRTRDDVKESTFQTTGDVDRYETGDDHNYEQPRQFWEKVLKEEERDRLVGNLASDLGGCLEEIQNGMVKEFTKVHPDFGNALRHQLCQKKH |
| Enzyme Length | 497 |
| Uniprot Accession Number | O61235 |
| 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:14996832}; |
| DNA Binding | |
| EC Number | 1.11.1.6 |
| Enzyme Function | FUNCTION: Catalase involved in the oxidative stress response serving to protect cells from toxicity (Probable) (PubMed:25243607, PubMed:28456303). For instance plays a role in defending against oxidative damage induced by excessive copper stress (PubMed:25243607). Not required for maintaining normal lifespan (PubMed:14996832). {ECO:0000269|PubMed:14996832, ECO:0000269|PubMed:25243607, ECO:0000269|PubMed:28456303, ECO:0000305|PubMed:18077412}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Metal binding (1); Sequence caution (1); Sequence conflict (6) |
| Keywords | Heme;Hydrogen peroxide;Iron;Metal-binding;Oxidoreductase;Peroxidase;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 | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 12845331; 17164286; 17483415; 18587389; 19343510; 19503598; 20439776; 21177967; 22347378; 22921415; 23800452; 24324795; 24623772; 25487147; 28204614; 31216475; |
| Motif | |
| Gene Encoded By | |
| Mass | 57,305 |
| Kinetics | |
| Metal Binding | METAL 354; /note=Iron (heme axial ligand); /evidence=ECO:0000250 |
| Rhea ID | RHEA:20309 |
| Cross Reference Brenda |