| IED ID | IndEnz0007000008 |
| Enzyme Type ID | catalase000008 |
| Protein Name |
Catalase-peroxidase 2 CP 2 EC 1.11.1.21 Peroxidase/catalase 2 |
| Gene Name | KATG2 CPXB MagKatG2 MGG_09834 |
| 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 | MHASLSSWLLAASLLTQPISVSGQGCPFAKRDGTVDSSLPQKRADAPETTTFGRCAVKSNQAGGGTRSHDWWPCQLRLDVLRQFQPSQNPLGGDFDYAEAFQSLDYEAVKKDIAALMTESQDWWPADFGNYGGLFVRMAWHSAGTYRAMDGRGGGGMGQQRFAPLNSWPDNQNLDKARRLIWPIKQKYGNKISWADLMLLTGNVALENMGFKTLGFGGGRADTWQSDEAVYWGAETTFVPQGNDVRYNNSVDINARADKLEKPLAATHMGLIYVNPEGPNGTPDPAASAKDIREAFGRMGMNDTETVALIAGGHAFGKTHGAVKGSNIGPAPEAADLGMQGLGWHNSVGDGNGPNQMTSGLEVIWTKTPTKWSNGYLESLINNNWTLVESPAGAHQWEAVNGTVDYPDPFDKTKFRKATMLTSDLALINDPEYLKISQRWLEHPEELADAFAKAWFKLLHRDLGPTTRYLGPEVPKESFIWQDPLPAREGDLIDDADVDKLKAAILSTDGLDVSKLASTAMACATTYRNSDKRGGCNGARIALEPQRNWVSNNPTQLSAVLDALKKVQSDFNGSNGNKKVSLADLIVLGGTAAVEKAAKDAGVDIKVPFSAGRVDATQEQTDVTQFSYLEPQADGFRNYGRGTARARTEEIMVDKASQLTLTPPELTVLVGGMRALGANYDGSDVGVFTANKGKLTPDFFVNLVDMNIAWTASGADGESWVGTDRKSRSEKYKGSRADLVFGSHAELRAIAEVYAENGNQEKFVKDFVAAWTKVMNLDRFDLKVKK |
| Enzyme Length | 786 |
| Uniprot Accession Number | A4QUT2 |
| Absorption | |
| Active Site | ACT_SITE 141; /note=Proton acceptor |
| 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}; 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. Confers resistance to H(2)O(2) in hyphae. May play an antioxidative role in fungal defense against the host-produced H(2)O(2) (oxidative burst) at the early stage of plant infection. {ECO:0000255|HAMAP-Rule:MF_03108, ECO:0000269|PubMed:21043575, ECO:0000269|PubMed:21971530}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.25 for the catalase reaction. Stable from pH 5.5 to pH 11. {ECO:0000269|PubMed:21971530, ECO:0000269|PubMed:22822072}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (15); Chain (1); Cross-link (2); Disulfide bond (2); Glycosylation (5); Helix (43); Metal binding (1); Signal peptide (1); Site (1); Turn (9) |
| Keywords | 3D-structure;Direct protein sequencing;Disulfide bond;Glycoprotein;Heme;Hydrogen peroxide;Iron;Metal-binding;Oxidoreductase;Peroxidase;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000255|HAMAP-Rule:MF_03108, ECO:0000269|PubMed:21043575}. |
| 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 | SIGNAL 1..23; /evidence=ECO:0000255|HAMAP-Rule:MF_03108 |
| Structure 3D | X-ray crystallography (5) |
| Cross Reference PDB | 3UT2; 5CJH; 5JHX; 5JHY; 5JHZ; |
| Mapped Pubmed ID | 26290940; 27293030; |
| Motif | |
| Gene Encoded By | |
| Mass | 85,587 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.84 mM for H(2)O(2) for the catalase reaction (at pH 5.25) {ECO:0000269|PubMed:21971530, ECO:0000269|PubMed:22822072}; KM=2.77 mM for H(2)O(2) for the catalase reaction (at pH 7.0) {ECO:0000269|PubMed:21971530, ECO:0000269|PubMed:22822072}; Note=kcat is 6446 sec(-1) with H(2)O(2) as substrate at pH 5.25 and 3290 sec(-1) with H(2)O(2) as substrate at pH 7.0.; |
| Metal Binding | METAL 314; /note=Iron (heme b axial ligand) |
| Rhea ID | RHEA:30275; RHEA:20309 |
| Cross Reference Brenda | 1.11.1.21; |