| IED ID | IndEnz0018001363 |
| Enzyme Type ID | peroxidase001363 |
| Protein Name |
Catalase-peroxidase CP EC 1.11.1.21 Peroxidase/catalase |
| Gene Name | katG cpeA |
| Organism | Talaromyces marneffei (Penicillium marneffei) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Trichocomaceae Talaromyces Talaromyces sect. Talaromyces Talaromyces marneffei (Penicillium marneffei) |
| Enzyme Sequence | MAESKCPAHQHVLKANVGGAGTSNQDWWPDRLKLNILRQNNPVSNPLGEEFDYAAAFNSLDYFALKKDIQDLMTDSQDWWPADFGHYGGLFIRMAWHSAGTYRVADGRGGGGGGQQRFAPLNSWPDNVGLDKARRLLWPIKQKYGNKISWADLLLLTGNVALESMGFKTFGFSGGRADTWEVDESANWGGETTWLGNDVRYSGGKADHKDIHNRDLDKPLAAAHMGLIYVNPEGPDGNPDPIAAAKDIRTTFGRMAMNDEETVALIAGGHTFGKTHGAGPADKLGPEPEAADMAQQGLGWTNSFKSGKGPDTTTSGLEVTWTKTPTKWSNQFLEYLFRYDWELTKSPAGAHQWVAKNAEAFIPDAFDPSKKRKPMMLTTDLSLRYDPIYEKISRRFLEHPDQFADAFARAWFKLLHRDLGPRALYIGPEVPAEVLPWQDPVPAVDHPLISNEDASALKQRILASGVKPSSLISTAWASASTFRGSDKRGGANGARIRLSPQREWAVNNQPWLRETLSVLEAIQKQFNTSQSGGKKVSIADLIVLAGVAAVEKAARDAGYAVTVPFTPGRTDASQEQTDVQSFSDMEPIADGFRNYGSSTSRVRAEEWLIDKAQLLTLSAPELAVLIGGLRVLNTNYDGSAHGVFTQRPGKLTNDFFVNLLDMNTAWKSIGGVDLYEGTDRKTGAKKWTATRNDLVFGSNAELRAIAEVYGSSDGQEKFVKDFVAAWDKVMNLDRFDLKKKQSTSSHRL |
| Enzyme Length | 748 |
| Uniprot Accession Number | Q8NJN2 |
| Absorption | |
| Active Site | ACT_SITE 97; /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}; 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 (By similarity). May be involved in protection from the host during host infection. {ECO:0000255|HAMAP-Rule:MF_03108}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Cross-link (2); Metal binding (1); Site (1) |
| Keywords | Cytoplasm;Heme;Hydrogen peroxide;Iron;Metal-binding;Oxidoreductase;Peroxidase |
| Interact With | |
| Induction | INDUCTION: Induced by temperature shift to 37 degrees Celsius, the condition whereby the pathogenic yeast phase is formed. {ECO:0000269|PubMed:16178368}. |
| 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 | 82,374 |
| Kinetics | |
| Metal Binding | METAL 270; /note=Iron (heme b axial ligand); /evidence=ECO:0000255|HAMAP-Rule:MF_03108 |
| Rhea ID | RHEA:30275; RHEA:20309 |
| Cross Reference Brenda |