Detail Information for IndEnz0018000278
IED ID IndEnz0018000278
Enzyme Type ID peroxidase000278
Protein Name Catalase
EC 1.11.1.6
Gene Name CAT
Organism Canis lupus familiaris (Dog) (Canis familiaris)
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 Laurasiatheria Carnivora Caniformia Canidae (dog coyote wolf fox) Canis Canis lupus (Gray wolf) Canis lupus familiaris (Dog) (Canis familiaris)
Enzyme Sequence MADSRDPASDQMKLWKEQRAAQKPDVLTTGGGNPIGDKLNVMTAGPRGPLLVQDVVFTDEMAHFDRERIPERVVHAKGAGAFGYFEVTHDITKYSKAKVFEHIGKRTPIAVRFSTVAGESGSADTVRDPRGFAVKFYTEDGNWDLVGNNTPIFFIRDAILFPSFIHSQKRNPQTHLKDPDMVWDFWSLRPESLHQVSFLFSDRGIPDGHRHMNGYGSHTFKLVNAAGEAVYCKFHYKTDQGIKNLSVEDAARLSHEDPDYGLRDLFNAIATGNYPSWTFYIQVMTFSQAETFPFNPFDLTKIWPHQDYPLIPVGKLVLNRNPVNYFAEVEQMAFDPSNMPPGIEPSPDKMLQGRLFAYPDTHRHRLGPNYLQIPVNCPFRARVANYQRDGPMCMLDNQGGAPNYYPNSFSAPEQQRCVLEHSSQCSPDVQRFNSANEDNVTQVRTFYLKVLGEEERKRLCENIAGHLKDAQLFIQKKAVKNFSDVHPDYGARIQALLDKYNAEKPKNAIHTFMQHGSHLAAREKANL
Enzyme Length 527
Uniprot Accession Number O97492
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 (14); Natural variant (1); Region (1)
Keywords Acetylation;Disease variant;Heme;Hydrogen peroxide;Iron;Metal-binding;Mitogen;NADP;Oxidoreductase;Peroxidase;Peroxisome;Phosphoprotein;Reference proteome
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}.
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 422; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P04040; MOD_RES 434; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P24270; 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 499; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:P24270; MOD_RES 511; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:P04040; MOD_RES 517; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P04040
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 59,797
Kinetics
Metal Binding METAL 358; /note=Iron (heme axial ligand); /evidence=ECO:0000250
Rhea ID RHEA:20309
Cross Reference Brenda