Reviewed,
UniProtKB/Swiss-Prot P46817 (KATG_MYCBO)
Last modified
November 25, 2008.
Version 61.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Catalase-peroxidase Short name=CP EC=1.11.1.6 EC=1.11.1.7 Alternative name(s): Peroxidase/catalase | ||||
| Gene names |
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| Organism | Mycobacterium bovis [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 1765 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex |
Protein attributes
| Sequence length | 740 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. May play a role in the intracellular survival of mycobacteria. |
| Catalytic activity | 2 H(2)O(2) = O(2) + 2 H(2)O. Donor + H(2)O(2) = oxidized donor + 2 H(2)O. |
| Cofactor | Binds 1 heme B (iron-protoporphyrin IX) group per dimer By similarity. |
| Subunit structure | Homodimer. |
| Post-translational modification | The covalent Trp-Tyr-Met adduct is important for the catalase, but not the peroxidase activity of the enzyme By similarity. |
| Sequence similarities | Belongs to the peroxidase family. Peroxidase/catalase subfamily. |
Ontologies
Keywords | |
|---|---|
| Biological process | Hydrogen peroxide |
| Ligand | Heme Iron Metal-binding |
| Molecular function | Oxidoreductase Peroxidase |
| Technical term | Complete proteome |
Gene Ontology (GO) | |
| Biological process | hydrogen peroxide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | catalase activity Inferred from electronic annotation. Source: InterPro heme bindingInferred from electronic annotation. Source: InterPro iron ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 740 | 740 | Catalase-peroxidase | PRO_0000055571 | |||||||
Sites | |||||||||||
| Active site | 108 | 1 | Proton acceptor By similarity | ||||||||
| Metal binding | 270 | 1 | Iron (heme axial ligand) By similarity | ||||||||
| Site | 104 | 1 | Transition state stabilizer By similarity | ||||||||
Amino acid modifications | |||||||||||
| Cross-link | 107 ↔ 229 | Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-255) By similarity | |||||||||
| Cross-link | 229 ↔ 255 | Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-107) By similarity | |||||||||
Experimental info | |||||||||||
| Sequence conflict | 234 | 1 | G → A in CAA58266. Ref.1 | ||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Missense mutations in the catalase-peroxidase gene, katG, are associated with isoniazid resistance in Mycobacterium tuberculosis." Heym B., Alzari P.M., Honore N., Cole S.T. Mol. Microbiol. 15:235-245(1995) [PubMed: 7746145] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: BCG. |
| [2] | "The complete genome sequence of Mycobacterium bovis." Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M., Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B., Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J. Hewinson R.G.Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003) [PubMed: 12788972] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-935 / AF2122/97. |
| [3] | "Catalase-peroxidase of Mycobacterium bovis BCG converts isoniazid to isonicotinamide, but not to isonicotinic acid: differentiation parameter between enzymes of Mycobacterium bovis BCG and Mycobacterium tuberculosis." Kang S.-K., Lee J.-H., Lee Y.-C., Kim C.-H. Biochim. Biophys. Acta 1760:724-729(2006) [PubMed: 16563633] [Abstract] Cited for: FUNCTION, SUBUNIT. |
Cross-references
Sequence databases | |
|---|---|
| X83277 Genomic DNA. Translation: CAA58266.1. BX248340 Genomic DNA. Translation: CAD94645.1. | |
| RefSeq | NP_855594.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1MWV based on UniProtKB Q939D2. |
| SMR | P46817. Positions 26-740. |
| ModBase | Search... |
Protein family/group databases | |
| PeroxiBase | 2434. MboCP01_BCG. 4578. MboCP01_AF2122. |
Genome annotation databases | |
| GeneID | 1093267. |
| GenomeReviews | Gene locus Mb1943c in contig BX248333_GR. |
| KEGG | mbo:Mb1943c. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P46817. |
Family and domain databases | |
| HAMAP | MF_01961. [Tree] |
| InterPro | IPR000763. Catalase_proxase. IPR002016. Haem_peroxidase_pln/fun/bac. [Graphical view] |
| Pfam | PF00141. peroxidase. 2 hits. [Graphical view] |
| PRINTS | PR00460. BPEROXIDASE. PR00458. PEROXIDASE. |
| TIGRFAMs | TIGR00198. cat_per_HPI. 1 hit. |
| PROSITE | PS00435. PEROXIDASE_1. 1 hit. PS00436. PEROXIDASE_2. 1 hit. PS50873. PEROXIDASE_4. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | KATG_MYCBO | ||||||||
| Accession | Primary (citable) accession number: P46817 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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