| IED ID | IndEnz0018000101 |
| Enzyme Type ID | peroxidase000101 |
| Protein Name |
Catalase EC 1.11.1.6 |
| Gene Name | Cat Cas1 |
| Organism | Rattus norvegicus (Rat) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MADSRDPASDQMKQWKEQRAPQKPDVLTTGGGNPIGDKLNIMTAGPRGPLLVQDVVFTDEMAHFDRERIPERVVHAKGAGAFGYFEVTHDITRYSKAKVFEHIGKRTPIAVRFSTVAGESGSADTVRDPRGFAVKFYTEDGNWDLVGNNTPIFFIRDAMLFPSFIHSQKRNPQTHLKDPDMVWDFWSLCPESLHQVTFLFSDRGIPDGHRHMNGYGSHTFKLVNANGEAVYCKFHYKTDQGIKNLPVEEAGRLAQEDPDYGLRDLFNAIASGNYPSWTFYIQVMTFKEAETFPFNPFDLTKVWPHKDYPLIPVGKLVLNRNPANYFAEVEQMAFDPSNMPPGIEPSPDKMLQGRLFAYPDTHRHRLGPNYLQIPVNCPYRARVANYQRDGPMCMHDNQGGAPNYYPNSFSAPEQQGSALEHHSQCSADVKRFNSANEDNVTQVRTFYTKVLNEEERKRLCENIANHLKDAQLFIQRKAVKNFTDVHPDYGARVQALLDQYNSQKPKNAIHTYVQAGSHIAAKGKANL |
| Enzyme Length | 527 |
| Uniprot Accession Number | P04762 |
| Absorption | |
| Active Site | ACT_SITE 75; /evidence=ECO:0000255|PROSITE-ProRule:PRU10013; ACT_SITE 148; /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}; |
| DNA Binding | |
| EC Number | 1.11.1.6 |
| Enzyme Function | FUNCTION: Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide. Promotes growth of cells. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Compositional bias (1); Initiator methionine (1); Metal binding (1); Modified residue (16); Region (1); Sequence conflict (1) |
| Keywords | Acetylation;Direct protein sequencing;Heme;Hydrogen peroxide;Iron;Metal-binding;Mitogen;NADP;Oxidoreductase;Peroxidase;Peroxisome;Phosphoprotein;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Peroxisome. |
| Modified Residue | MOD_RES 2; /note=N-acetylalanine; /evidence=ECO:0000250|UniProtKB:P04040; MOD_RES 9; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P04040; MOD_RES 13; /note=N6-succinyllysine; /evidence=ECO:0000250|UniProtKB:P24270; MOD_RES 221; /note=N6-succinyllysine; /evidence=ECO:0000250|UniProtKB:P24270; MOD_RES 233; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:P24270; MOD_RES 306; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P24270; MOD_RES 306; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P24270; MOD_RES 417; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P24270; MOD_RES 434; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 449; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P24270; MOD_RES 449; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P24270; MOD_RES 480; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P24270; MOD_RES 480; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P24270; MOD_RES 511; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:P04040; MOD_RES 517; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 522; /note=N6-succinyllysine; /evidence=ECO:0000250|UniProtKB:P24270 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10220857; 10569634; 11510883; 12225545; 12456800; 12592055; 14561759; 14575298; 14624470; 14713308; 15109710; 15287906; 15372991; 15638087; 15721881; 15734284; 15773229; 15777843; 15836852; 15869839; 16131024; 16223488; 16238459; 16396496; 16716903; 16770742; 16938375; 17215005; 17320761; 17514533; 17524832; 17564305; 17576767; 17597213; 17895592; 18008141; 18049893; 18171680; 18270324; 18430061; 18547798; 18655190; 18793622; 19196076; 19298531; 19302986; 19445928; 19641679; 19675389; 19693467; 19842849; 19891630; 19895324; 19914224; 19966046; 20007347; 20063054; 20299359; 20376213; 20387083; 20465785; 20534640; 20698742; 20830981; 20888583; 21138988; 21213399; 21276205; 21295034; 21305585; 21314438; 21339256; 21452373; 21463646; 21525431; 21635889; 21660462; 21686137; 21942371; 22173336; 22206666; 22237725; 22509733; 22683338; 22733796; 22905402; 23096233; 23232760; 23485553; 23527889; 23658840; 23808586; 23911387; 23952340; 24669281; 24740756; 25038876; 25639505; 26071777; 26109091; 26208597; 26459835; 26503970; 27221506; 28290603; 29229353; 29847079; 29896255; 9250541; |
| Motif | |
| Gene Encoded By | |
| Mass | 59,757 |
| Kinetics | |
| Metal Binding | METAL 358; /note=Iron (heme axial ligand); /evidence=ECO:0000250 |
| Rhea ID | RHEA:20309 |
| Cross Reference Brenda | 1.11.1.6; |