| IED ID | IndEnz0018001457 |
| Enzyme Type ID | peroxidase001457 |
| Protein Name |
Catalase-3 EC 1.11.1.6 |
| Gene Name | cat-3 NCU00355 |
| Organism | Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Sordariomycetidae Sordariales Sordariaceae Neurospora Neurospora crassa Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) |
| Enzyme Sequence | MRVNALLPLSGLIGTALAACPFADPSALGRRAEGGEVDARQRLKEVEVDDNGQFMTTDFGGNIEEQFSLKAGGRGSTLLEDFIFRQKLQHFDHERIPERVVHARGAGAHGIFTSYGDWSNITAASFLGAKDKQTPVFVRFSTVAGSRGSADTARDVHGFATRFYTDEGNFDIVGNNIPVFFIQDAIRFPDLIHSVKPSPDNEVPQAATAHDSAWDFFSSQPSALHTLFWAMSGNGIPRSYRHMDGFGIHTFRLVTEDGKSKLVKWHWKTKQGKAALVWEEAQVLAGKNADFHRQDLWDAIESGNAPSWELAVQLIDEDKAQAYGFDLLDPTKFLPEEFAPLQVLGEMTLNRNPMNYFAETEQISFQPGHIVRGVDFTEDPLLQGRLYSYLDTQLNRHRGPNFEQLPINRPVSGVHNNHRDGQGQAWIHKNIHHYSPSYLNKGYPAQANQTVGRGFFTTPGRTASGVLNRELSATFDDHYTQPRLFFNSLTPVEQQFVINAIRFEASHVTNEQVKKNVLEQLNKISNDVAKRVAVALGLEAPQPDPTYYHNNVTRGVSIFNESLPTIATLRVGVLSTTKGGSLDKAKALKEQLEKDGLKVTVIAEYLASGVDQTYSAADATAFDAVVVAEGAERVFSGKGAMSPLFPAGRPSQILTDGYRWGKPVAAVGSAKKALQSIGVEEKEAGVYAGAQDEVIKGVEEGLKVFKFLERFAVDGDDEE |
| Enzyme Length | 719 |
| Uniprot Accession Number | Q9C169 |
| Absorption | |
| Active Site | ACT_SITE 102; /evidence=ECO:0000255|PROSITE-ProRule:PRU10013; ACT_SITE 175; /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:12160934}; |
| 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. {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (29); Chain (1); Helix (31); Metal binding (1); Propeptide (1); Signal peptide (1); Turn (9) |
| Keywords | 3D-structure;Direct protein sequencing;Heme;Hydrogen peroxide;Iron;Metal-binding;Oxidoreductase;Peroxidase;Reference proteome;Signal |
| Interact With | |
| Induction | INDUCTION: Induced under stress conditions, such as H(2)O(2), paraquat, cadmium, heat shock, uric acid and nitrate treatment. {ECO:0000269|PubMed:12160934}. |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (10) |
| Cross Reference PDB | 3EJ6; 3ZJ4; 3ZJ5; 4AJ9; 4BIM; 6NSW; 6NSY; 6NSZ; 6NT0; 6NT1; |
| Mapped Pubmed ID | 16697373; 19109972; 23832201; 30940570; |
| Motif | |
| Gene Encoded By | |
| Mass | 79,228 |
| Kinetics | |
| Metal Binding | METAL 389; /note=Iron (heme axial ligand); /evidence=ECO:0000250 |
| Rhea ID | RHEA:20309 |
| Cross Reference Brenda |