| IED ID | IndEnz0002013720 |
| Enzyme Type ID | protease013720 |
| Protein Name |
Catalase-peroxidase CP EC 1.11.1.21 Peroxidase/catalase |
| Gene Name | katG ERDMAN_2101 |
| Organism | Mycobacterium tuberculosis (strain ATCC 35801 / TMC 107 / Erdman) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Corynebacteriales Mycobacteriaceae Mycobacterium Mycobacterium tuberculosis complex Mycobacterium tuberculosis Mycobacterium tuberculosis (strain ATCC 35801 / TMC 107 / Erdman) |
| Enzyme Sequence | MPEQHPPITETTTGAASNGCPVVGHMKYPVEGGGNQDWWPNRLNLKVLHQNPAVADPMGAAFDYAAEVATIDVDALTRDIEEVMTTSQPWWPADYGHYGPLFIRMAWHAAGTYRIHDGRGGAGGGMQRFAPLNSWPDNASLDKARRLLWPVKKKYGKKLSWADLIVFAGNCALESMGFKTFGFGFGRVDQWEPDEVYWGKEATWLGDERYSGKRDLENPLAAVQMGLIYVNPEGPNGNPDPMAAAVDIRETFRRMAMNDVETAALIVGGHTFGKTHGAGPADLVGPEPEAAPLEQMGLGWKSSYGTGTGKDAITSGIEVVWTNTPTKWDNSFLEILYGYEWELTKSPAGAWQYTAKDGAGAGTIPDPFGGPGRSPTMLATDLSLRVDPIYERITRRWLEHPEELADEFAKAWYKLIHRDMGPVARYLGPLVPKQTLLWQDPVPAVSHDLVGEAEIASLKSQIRASGLTVSQLVSTAWAAASSFRGSDKRGGANGGRIRLQPQVGWEVNDPDGDLRKVIRTLEEIQESFNSAAPGNIKVSFADLVVLGGCAAIEKAAKAAGHNITVPFTPGRTDASQEQTDVESFAVLEPKADGFRNYLGKGNPLPAEYMLLDKANLLTLSAPEMTVLVGGLRVLGANYKRLPLGVFTEASESLTNDFFVNLLDMGITWEPSPADDGTYQGKDGSGKVKWTGSRVDLVFGSNSELRALVEVYGADDAQPKFVQDFVAAWDKVMNLDRFDVR |
| Enzyme Length | 740 |
| Uniprot Accession Number | H8F3Q9 |
| Absorption | |
| Active Site | ACT_SITE 108; /note=Proton acceptor; /evidence=ECO:0000255|HAMAP-Rule:MF_01961; ACT_SITE 321; /note=Tryptophan radical intermediate; /evidence=ECO:0000250|UniProtKB:P9WIE5 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | 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_01961}; 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_01961}; |
| DNA Binding | |
| EC Number | 1.11.1.21 |
| Enzyme Function | FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity, oxidizing various electron donors including NADP(H) (By similarity). Protects M.tuberculosis against toxic reactive oxygen species (ROS) including hydrogen peroxide as well as organic peroxides and thus contributes to its survival within host macrophages by countering the phagocyte oxidative burst (PubMed:15165233). Also displays efficient peroxynitritase activity, which may help the bacterium to persist in macrophages (By similarity). {ECO:0000250|UniProtKB:P9WIE5, ECO:0000255|HAMAP-Rule:MF_01961, ECO:0000269|PubMed:15165233}.; FUNCTION: Catalyzes the oxidative activation of the antitubercular pro-drug isoniazid (INH) to generate an isonicotinoyl radical that then reacts nonenzymatically with NAD to form an isonicotinoyl-NAD adduct which inhibits InhA. {ECO:0000250|UniProtKB:P9WIE5}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Cross-link (2); Metal binding (1); Site (1) |
| Keywords | Heme;Hydrogen peroxide;Iron;Metal-binding;Organic radical;Oxidoreductase;Peroxidase;Virulence |
| Interact With | |
| Induction | INDUCTION: By the metal chelator phenanthroline via Rip1, RskA/SigK and RslA/SigL. {ECO:0000269|PubMed:20545848}. |
| Subcellular Location | |
| 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_01961}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 80,605 |
| Kinetics | |
| Metal Binding | METAL 270; /note=Iron (heme axial ligand); /evidence=ECO:0000255|HAMAP-Rule:MF_01961 |
| Rhea ID | RHEA:20309; RHEA:30275 |
| Cross Reference Brenda |