| IED ID | IndEnz0018000311 |
| Enzyme Type ID | peroxidase000311 |
| Protein Name |
Catalase-peroxidase 1 CP 1 EC 1.11.1.21 Peroxidase/catalase 1 |
| Gene Name | katG1 MagKatG1 MGG_04337 |
| Organism | Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Pyricularia oryzae) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Sordariomycetidae Magnaporthales Pyriculariaceae Pyricularia Magnaporthe oryzae (Rice blast fungus) (Pyricularia oryzae) Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Pyricularia oryzae) |
| Enzyme Sequence | MGECPLRTANVAGGGTRNRDWWPNTLKLNILRQHTEATNPYDPNFDYAEAFKSLDYEGLKKDLRALMTDSQEYWPADFGHYGGLFVRMAWHSAGTYRVMDGRGGGGQGQQRFAPLNSWPDNVSLDKARRLLWPIKQKYGNKISWADLMLLTGNVALEDMGFKTFGFAGGRPDTWEADESTYWGGETTWLGNEVRYSSGNEGHKESGVIDGSESKKGHKDIHTRDLEKPVSAAHMGLIYVNPEGPDGIPDPVAAARDIRTTFSRMAMNDEETVALIAGGHTVGKTHGAAPSDNVGPEPEAAPIENQGLGWSNKHGSGKGPDTITSGLEVIWTKEPAKFTMNYLEYLFKYEWELTKSPAGANQWVAKNAEEFIPDAFDPSKKHKPRMLTTDLSLRFDPEYEKISRRFLENPEQFKDAFARAWFKLLHRDMGPRSRWLGPEVPKETLLWEDPIPTPDHPIIDGSDVDSLKKAILATGVAPSKLIQTAWASASTFRGGDKRGGANGARIRLEPQNKWEVNNPQQLAEVLKALEGVKADFEKSGKKVSIADLIVLAGVAAVEQAAGVPVPFTPGRGDATQEQTDVESFTHLEPAADAFRNYGKGTSRVTTEQIMVDRAQQLTLTAPELTVLVGGLRVLGANYDGSSHGVWTDKPGKLTNDFFVTLLDPYTSWKSVDGEVFEGTNSKSGKKLTGTRADLVFGSHSELRALAEVYGSADGQQKFTKDFVAAWDKVMNLDRFDVRRGIYDETRLKSKL |
| Enzyme Length | 750 |
| Uniprot Accession Number | A4R5S9 |
| Absorption | |
| Active Site | ACT_SITE 91; /note=Proton acceptor; /evidence=ECO:0000255|HAMAP-Rule:MF_03108 |
| Activity Regulation | |
| 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, ECO:0000269|PubMed:19000033}; 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, ECO:0000269|PubMed:19000033}; |
| DNA Binding | |
| EC Number | 1.11.1.21 |
| Enzyme Function | FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. {ECO:0000255|HAMAP-Rule:MF_03108, ECO:0000269|PubMed:19000033}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0 for the catalase reaction. {ECO:0000269|PubMed:19000033}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Cross-link (2); Metal binding (1); Region (1); Site (1) |
| Keywords | Cytoplasm;Heme;Hydrogen peroxide;Iron;Metal-binding;Oxidoreductase;Peroxidase;Reference proteome |
| Interact With | |
| Induction | |
| 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 | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 82,859 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.8 mM for H(2)O(2) for the catalase reaction {ECO:0000269|PubMed:19000033}; Note=kcat is 7010 sec(-1) with H(2)O(2) as substrate.; |
| 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 | 1.11.1.21; |