Detail Information for IndEnz0018001051
IED ID IndEnz0018001051
Enzyme Type ID peroxidase001051
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;