| IED ID | IndEnz0018000478 |
| Enzyme Type ID | peroxidase000478 |
| Protein Name |
Catalase-peroxidase CP EC 1.11.1.21 Catalase-2 Peroxidase/catalase |
| Gene Name | katG cat-2 NCU05770 |
| 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 | MSECPVRKSNVGGGGTRNHDWWPAQLRLNILRQHTPVSNPLDKDFDYAAAFKSLDYEGLKKDLTKLMTDSQDWWPADFGHYGGLFIRMAWHSAGTYRVTDGRGGGGEGQQRFAPLNSWPDNVSLDKARRLLWPIKQKYGNKISWSDLLLLTGNVALESMGFKTFGFAGGRPDTWEADESVYWGAETTWLGNEDRYSEGQEGHEGHGVVQGDESKKQHTDIHNRDLQSPLASSHMGLIYVNPEGPDGIPDPVASAKDIRVTFGRMAMNDEETVALIAGGHSFGKTHGAGPTHHVGKEPEAAPIEHQGLGWANSFGQGKGPDTITSGLEVTWTPTPTKWGMGYLEYLYKFDWEPTKSPAGANQWVAKNAEPTIPDAYDPNKKKLPTMLTTDIALRMDPAYDKICRDYLANPDKFADAFARAWFKLLHRDMGPRTRWIGPEVPSEILPWEDYIPPVDYQIIDDNDIAALKKEILATGVAPKKLIFVAWSSASSFRGSDKRGGANGARIRLAPQNEWKVNDPSTLREVLAALESVQQKFNDSSSGKKVSLADLIVLGGVAALEQASGLVVPFTPGRNDATQEHTDVHSFTHLEPHADGFRSYGKGTKRVRTEQFLIDRASLLTLSAPELTALIGGLRVLEANYDGSSYGVLTKTPGKLTNDYFVNLLDTNTAWKAADNEGEVFIGYDRKTHDKKWTATRADLIFGAHAELRALAEVYAAVDGEEKFKRDFVAAWHKVMNLDRFDLKQEGRGQNAPKL |
| Enzyme Length | 753 |
| Uniprot Accession Number | Q8X182 |
| Absorption | |
| Active Site | ACT_SITE 91; /note=Proton acceptor; /evidence=ECO:0000255|HAMAP-Rule:MF_03108 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by KCN. {ECO:0000269|PubMed:12033445}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=AH2 + H2O2 = A + 2 H2O; Xref=Rhea:RHEA:30275, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:17499; EC=1.11.1.21; Evidence={ECO:0000255|HAMAP-Rule:MF_03108}; CATALYTIC ACTIVITY: Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.21; Evidence={ECO:0000255|HAMAP-Rule:MF_03108}; |
| DNA Binding | |
| EC Number | 1.11.1.21 |
| Enzyme Function | FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.75 for the peroxidase reaction and 6.25 for the catalase reaction. {ECO:0000269|PubMed:12033445}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (12); Chain (1); Cross-link (2); Helix (43); Metal binding (1); Region (1); Site (1); Turn (7) |
| Keywords | 3D-structure;Cytoplasm;Direct protein sequencing;Heme;Hydrogen peroxide;Iron;Metal-binding;Oxidoreductase;Peroxidase;Reference proteome |
| Interact With | |
| Induction | INDUCTION: Induced in late stationary growth phase. {ECO:0000269|PubMed:12033445}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03108}. |
| Modified Residue | |
| Post Translational Modification | PTM: Formation of the three residue Trp-Tyr-Met cross-link is important for the catalase, but not the peroxidase activity of the enzyme. {ECO:0000255|HAMAP-Rule:MF_03108}. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 5WHQ; 5WHS; |
| Mapped Pubmed ID | 29305053; |
| Motif | |
| Gene Encoded By | |
| Mass | 83,380 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=13.2 mM for H(2)O(2) for the catalase reaction {ECO:0000269|PubMed:12033445}; |
| Metal Binding | METAL 279; /note=Iron (heme b axial ligand); /evidence=ECO:0000255|HAMAP-Rule:MF_03108 |
| Rhea ID | RHEA:30275; RHEA:20309 |
| Cross Reference Brenda | 1.11.1.6; |