| IED ID | IndEnz0018000166 |
| Enzyme Type ID | peroxidase000166 |
| Protein Name |
Peroxisomal catalase A EC 1.11.1.6 |
| Gene Name | CTA1 YDR256C YD9320A.06C |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces Saccharomyces cerevisiae (Baker's yeast) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Enzyme Sequence | MSKLGQEKNEVNYSDVREDRVVTNSTGNPINEPFVTQRIGEHGPLLLQDYNLIDSLAHFNRENIPQRNPHAHGSGAFGYFEVTDDITDICGSAMFSKIGKRTKCLTRFSTVGGDKGSADTVRDPRGFATKFYTEEGNLDWVYNNTPVFFIRDPSKFPHFIHTQKRNPQTNLRDADMFWDFLTTPENQVAIHQVMILFSDRGTPANYRSMHGYSGHTYKWSNKNGDWHYVQVHIKTDQGIKNLTIEEATKIAGSNPDYCQQDLFEAIQNGNYPSWTVYIQTMTERDAKKLPFSVFDLTKVWPQGQFPLRRVGKIVLNENPLNFFAQVEQAAFAPSTTVPYQEASADPVLQARLFSYADAHRYRLGPNFHQIPVNCPYASKFFNPAIRDGPMNVNGNFGSEPTYLANDKSYTYIQQDRPIQQHQEVWNGPAIPYHWATSPGDVDFVQARNLYRVLGKQPGQQKNLAYNIGIHVEGACPQIQQRVYDMFARVDKGLSEAIKKVAEAKHASELSSNSKF |
| Enzyme Length | 515 |
| Uniprot Accession Number | P15202 |
| Absorption | |
| Active Site | ACT_SITE 70; /evidence=ECO:0000269|PubMed:9931255; ACT_SITE 143; /evidence=ECO:0000269|PubMed:9931255 |
| 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. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (18); Chain (1); Helix (19); Initiator methionine (1); Metal binding (1); Modified residue (1); Motif (1); Sequence conflict (1); Turn (6) |
| Keywords | 3D-structure;Acetylation;Heme;Hydrogen peroxide;Iron;Metal-binding;Oxidoreductase;Peroxidase;Peroxisome;Reference proteome |
| Interact With | P39940 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Peroxisome. |
| Modified Residue | MOD_RES 2; /note=N-acetylserine; /evidence=ECO:0007744|PubMed:22814378 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 1A4E; |
| Mapped Pubmed ID | 10926859; 10961694; 10978547; 11097021; 11145102; 11283351; 11679167; 12054464; 12697341; 14354151; 1444337; 14558145; 1474890; 14998369; 15456898; 15798189; 15864293; 15875812; 15893481; 16173060; 16606443; 17009956; 17100288; 17387467; 18021067; 18039473; 18178164; 18197247; 18452720; 18457571; 18621837; 18647484; 18671944; 18719252; 18728780; 1899286; 18997852; 19179331; 19536198; 19538506; 19722092; 19777209; 1986244; 19873875; 20124343; 20370606; 20696905; 20796282; 20952643; 20971184; 21076178; 21549177; 21605494; 21840858; 22094416; 22209905; 22659048; 22660740; 22662318; 22741594; 22970195; 23167605; 23275493; 23605494; 23793623; 23821148; 23993573; 24040173; 24223957; 24282812; 24401081; 24410772; 24563848; 25172136; 25280400; 25416226; 25422453; 25640729; 26618154; 27305947; 27667523; 27883213; 28828388; 30131444; 3889553; 3897793; 8406042; 8757790; 9041655; 9427398; 9885153; 9918826; |
| Motif | MOTIF 513..515; /note=Microbody targeting signal; /evidence=ECO:0000255 |
| Gene Encoded By | |
| Mass | 58,555 |
| Kinetics | |
| Metal Binding | METAL 355; /note=Iron (heme axial ligand); /evidence=ECO:0000269|PubMed:9931255 |
| Rhea ID | RHEA:20309 |
| Cross Reference Brenda |