Detail Information for IndEnz0018000916
IED ID IndEnz0018000916
Enzyme Type ID peroxidase000916
Protein Name Catalase
EC 1.11.1.6
Gene Name CAT
Organism Bos taurus (Bovine)
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 Artiodactyla Ruminantia Pecora Bovidae Bovinae Bos (oxen cattle) Bos taurus (Bovine)
Enzyme Sequence MADNRDPASDQMKHWKEQRAAQKPDVLTTGGGNPVGDKLNSLTVGPRGPLLVQDVVFTDEMAHFDRERIPERVVHAKGAGAFGYFEVTHDITRYSKAKVFEHIGKRTPIAVRFSTVAGESGSADTVRDPRGFAVKFYTEDGNWDLVGNNTPIFFIRDALLFPSFIHSQKRNPQTHLKDPDMVWDFWSLRPESLHQVSFLFSDRGIPDGHRHMNGYGSHTFKLVNANGEAVYCKFHYKTDQGIKNLSVEDAARLAHEDPDYGLRDLFNAIATGNYPSWTLYIQVMTFSEAEIFPFNPFDLTKVWPHGDYPLIPVGKLVLNRNPVNYFAEVEQLAFDPSNMPPGIEPSPDKMLQGRLFAYPDTHRHRLGPNYLQIPVNCPYRARVANYQRDGPMCMMDNQGGAPNYYPNSFSAPEHQPSALEHRTHFSGDVQRFNSANDDNVTQVRTFYLKVLNEEQRKRLCENIAGHLKDAQLFIQKKAVKNFSDVHPEYGSRIQALLDKYNEEKPKNAVHTYVQHGSHLSAREKANL
Enzyme Length 527
Uniprot Accession Number P00432
Absorption
Active Site ACT_SITE 75; /evidence="ECO:0000255|PROSITE-ProRule:PRU10013, ECO:0000269|PubMed:7328661"; ACT_SITE 148
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};
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 BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7. {ECO:0000269|PubMed:10691967};
Pathway
nucleotide Binding
Features Active site (2); Beta strand (19); Chain (1); Compositional bias (1); Helix (21); Initiator methionine (1); Metal binding (1); Modified residue (15); Region (1); Sequence conflict (2); Turn (7)
Keywords 3D-structure;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=Blocked amino end (Ala); alternate; /evidence=ECO:0000269|PubMed:7082009; MOD_RES 2; /note=N-acetylalanine; alternate; /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 417; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P24270; 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 X-ray crystallography (13); Electron microscopy (5)
Cross Reference PDB 1TGU; 1TH2; 1TH3; 1TH4; 3J7B; 3NWL; 3RE8; 3RGP; 3RGS; 4BLC; 5GKN; 6JNT; 6JNU; 6PM7; 6PO0; 7CAT; 7DI8; 8CAT;
Mapped Pubmed ID 21524057; 25730881; 30928615; 33469549; 3856839;
Motif
Gene Encoded By
Mass 59,915
Kinetics
Metal Binding METAL 358; /note=Iron (heme axial ligand); /evidence=ECO:0000269|PubMed:7328661
Rhea ID RHEA:20309
Cross Reference Brenda 1.11.1.6;