H8F3Q9 · KATG_MYCTE
- ProteinCatalase-peroxidase
- GenekatG
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids740 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
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).
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).
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.
Catalytic activity
- 2 H2O2 = O2 + 2 H2O
Cofactor
Note: Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.
Features
Showing features for site, active site, binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Site | 104 | Transition state stabilizer | |||
Active site | 108 | Proton acceptor | |||
Binding site | 270 | Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); axial binding residue | |||
Active site | 321 | Tryptophan radical intermediate | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | catalase activity | |
Molecular Function | heme binding | |
Molecular Function | metal ion binding | |
Biological Process | cellular response to hydrogen peroxide | |
Biological Process | hydrogen peroxide catabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCatalase-peroxidase
- EC number
- Short namesCP
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Mycobacteriaceae > Mycobacterium > Mycobacterium tuberculosis complex
Accessions
- Primary accessionH8F3Q9
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Phenotypes & Variants
Disruption phenotype
Cells lacking this gene are devoid of catalase activity, supersensitive to H2O2 exposure and highly resistant to the antitubercular drug isoniazid (INH) in vitro. This mutant strain is markedly attenuated for virulence in mice and displays impaired growth in infected macrophages, but its growth and survival is indistinguishable from wild-type in macrophages lacking the ROS-generating NADPH oxidase (Phox).
PTM/Processing
Features
Showing features for chain, cross-link.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000422688 | 1-740 | Catalase-peroxidase | ||
Cross-link | 107↔229 | Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-255) | |||
Cross-link | 229↔255 | Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-107) | |||
Post-translational modification
Formation of the three residue Trp-Tyr-Met cross-link is important for the catalase, but not the peroxidase activity of the enzyme.
Keywords
- PTM
Expression
Induction
By the metal chelator phenanthroline via Rip1, RskA/SigK and RslA/SigL.
Interaction
Subunit
Homodimer.
Structure
Sequence
- Sequence statusComplete
- Length740
- Mass (Da)80,605
- Last updated2012-05-16 v1
- MD5 ChecksumD08E940EC2068562479EBDBDAD3F75BC
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AP012340 EMBL· GenBank· DDBJ | BAL65894.1 EMBL· GenBank· DDBJ | Genomic DNA |