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Search term: Rv1908c

General annotation | Coordinates | Sequence | Structural information | Orthologs/Cross-references | Interacting Drugs/Compounds | Bibliography
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General annotation
Gene namekatG
Rv numberRv1908c
FunctionMultifunctional enzyme, exhibiting both a catalase, a broad-spectrum peroxidase, and a peroxynitritase activities. May play a role in the intracellular survival of mycobacteria within macrophages; protection against reactive oxygen and nitrogen intermediates produced by phagocytic cells. Seems regulated by SIGB|Rv2710 [catalytic activity: 2 H(2)O(2) = O(2) + 2 H(2)O].
ProductCatalase-peroxidase-peroxynitritase T KatG
CommentsRv1908c, (MTCY180.10), len: 740 aa. KatG, catalase-peroxidase-peroxynitritase T (see citations below), HPI. FASTA results: Q57215 catalase-peroxidase from Mycobacterium tuberculosis (740 aa) opt: 5081, E(): 0, (100% identity in 740 aa overlap). Contains peroxidases active site signature (PS00436) and ATP/GTP-binding site motif A (P-loop; PS00017). Cosmid sequence was corrected to agree with a sequencing read from the H37Rv genome. Deletions or defects in KATG gene cause isoniazid (INH) resistance. Belongs to the peroxidase family. Bacterial peroxidase/catalase subfamily. KATG transcription seems to be regulated by FURA|Rv1909c product. The catalase-peroxidase activity is associated with the amino-terminal domain but no definite function has been assigned to the carboxy-terminal domain. Predicted possible vaccine candidate (See Zvi et al., 2008).
Molecular mass (Da)80572.8
Isoelectric point4.87
Gene length (bp)2223
Protein length740
Location (kb)2153.89

Functional categoryvirulence, detoxification, adaptation

ProteomicsThe product of this CDS corresponds to spot katG identified in cell wall by proteomics at the Statens Serum Institute (Denmark) (see Rosenkrands et al., 2000a; 2000b). Also identified in two-dimensional gel electrophoresis and by mass spectrometry, particularly in standing cultures (see Florczyk et al., 2001). Identified in the membrane fraction of M. tuberculosis H37Rv using 1D-SDS-PAGE and uLC-MS/MS (See Gu et al., 2003). Identified in the cytosol and cell membrane fraction of M. tuberculosis H37Rv using 2DLC/MS (See Mawuenyega et al., 2005). Identified in the membrane fraction of M. tuberculosis H37Rv using nanoLC-MS/MS (See Xiong et al., 2005). Identified in culture filtrates of M. tuberculosis H37Rv (See Malen et al., 2007). Identified by mass spectrometry in Triton X-114 extracts of M. tuberculosis H37Rv (See Malen et al., 2010). Identified by mass spectrometry in the culture filtrate, membrane protein fraction, and whole cell lysates of M. tuberculosis H37Rv (See de Souza et al., 2011). Translational start site supported by proteomics data (See de Souza et al., 2011) (See Kelkar et al., 2011).
Mutationnon essential gene by Himar1-based transposon mutagenesis in H37Rv and CDC1551 strains (see Sassetti et al., 2003 and Lamichhane et al., 2003). Essential gene for in vitro growth of H37Rv, by sequencing of Himar1-based transposon mutagenesis (See Griffin et al., 2011). Found to be deleted (partially or completely) in one or more clinical isolates (See Tsolaki et al., 2004). Check for mutants available at TARGET website
RegulonChIP-chip indicates SigF|Rv3286c binds to the intergenic upstream region (See Rodrigue et al., 2007).


Protein sequence in FASTA format
>M. tuberculosis H37Rv|Rv1908c|katG
Blastp: Pre-computed results
TransMembrane prediction using Hidden Markov Models: TMHMM
Genomic sequence

Add extra bases upstream (5') and downstream (3')

Structural information
Protein Data Bank1SFZ 1SJ2 2CCA 2CCD

Enzyme Classification1.11.1.6
Gene Ontologycatalase activity
heme binding
hydrogen peroxide catabolic process
response to antibiotic
oxidation reduction
M. bovisMb1943c
M. lepraeML2009
M. smegmatisMSMEG_6384
Multiple Sequences Alignment: between orthologs

Interacting Drugs/Compounds
TDR TargetsRv1908c
Drug Resistance MutationsIsoniazid

Expression Data

Saint-Joanis B, Saint -Joanis B, Souchon H, Wilming M, Johnsson K, Alzari PM, Cole ST,
Use of site-directed mutagenesis to probe the structure, function and isoniazid activation of the catalase/peroxidase, KatG, from Mycobacterium tuberculosis
Biochem J (1999) 338(Pt 3):753-60
Cited for: Secondary/Mutant
Mulder MA, Zappe H, Steyn LM,
Mycobacterial promoters
Tuber Lung Dis (1997) 78(5-6):211-23
Cited for: Review/Regulation
Mulder MA, Nair S, Abratt VR, Zappe H, Steyn LM,
Involvement of the N- and C-terminal domains of Mycobacterium tuberculosis KatG in the protection of mutant Escherichia coli against DNA -damaging agents
Microbiology (1999) 145(Pt 8):2011-21
Cited for: Product/Function
Mulder MA, Zappe H, Steyn LM,
The Mycobacterium tuberculosis katG promoter region contains a novel upstream activator
Microbiology (1999) 145(Pt 9):2507-18
Cited for: Regulation
Rosenkrands I, Weldingh K, Jacobsen S, Hansen CV, Florio W, Gianetri I, Andersen P,
Mapping and identification of Mycobacterium tuberculosis proteins by two-dimensional gel electrophoresis, microsequencing and immunodetection
Electrophoresis (2000) 21(5):935-48
Cited for: Proteomics
Rosenkrands I, King A, Weldingh K, Moniatte M, Moertz E, Andersen P,
Towards the proteome of Mycobacterium tuberculosis
Electrophoresis (2000) 21(17):3740-56
Cited for: Proteomics
Master S, Zahrt TC, Song J, Deretic V,
Mapping of Mycobacterium tuberculosis katG promoters and their differential expression in infected macrophages
J Bacteriol (2001) 183(13):4033-9
Cited for: Regulation
Pym AS, Domenech P, Honore N, Song J, Deretic V, Cole ST,
Regulation of catalase -peroxidase (KatG) expression, isoniazid sensitivity and virulence by furA of Mycobacterium tuberculosis
Mol Microbiol (2001) 40(4):879-89
Cited for: Regulation/Mutant
Florczyk MA, McCue LA, Stack RF, Hauer CR, McDonough KA,
Identification and characterization of mycobacterial proteins differentially expressed under standing and shaking culture conditions, including Rv2623 from a novel class of putative ATP-binding proteins
Infect Immun (2001) 69(9):5777-85
Cited for: Proteomics
Milano A, Forti F, Sala C, Riccardi G, Ghisotti D,
Transcriptional regulation of furA and katG upon oxidative stress in Mycobacterium smegmatis
J Bacteriol (2001) 183(23):6801-6
Cited for: Regulation
Wilming M, Johnsson K,
Inter- and intramolecular domain interactions of the catalase-peroxidase KatG from M. tuberculosis
FEBS Lett (2001) 509(2):272-6
Cited for: Product
Pym AS, Saint-Joanis B, Saint -Joanis B, Cole ST,
Effect of katG mutations on the virulence of Mycobacterium tuberculosis and the implication for transmission in humans
Infect Immun (2002) 70(9):4955-60
Cited for: Mutant/Function
Sassetti CM, Boyd DH, Rubin EJ,
Genes required for mycobacterial growth defined by high density mutagenesis.
Mol Microbiol (2003) 48(1):77-84
Cited for: Mutant
Lamichhane G, Zignol M, Blades NJ, Geiman DE, Dougherty A, Grosset J, Broman KW, Bishai WR,
A postgenomic method for predicting essential genes at subsaturation levels of mutagenesis: application to Mycobacterium tuberculosis.
Proc Natl Acad Sci U S A (2003) 100(12):7213-8
Cited for: Mutant
Gu S, Chen J, Dobos KM, Bradbury EM, Belisle JT, Chen X,
Comprehensive proteomic profiling of the membrane constituents of a Mycobacterium tuberculosis strain.
Mol Cell Proteomics (2003) 2(12):1284-96
Cited for: Proteomics
Tsolaki AG, Hirsh AE, DeRiemer K, Enciso JA, Wong MZ, Hannan M, Goguet de la Salmoniere YO, Aman K, Kato-Maeda M, Small PM,
Functional and evolutionary genomics of Mycobacterium tuberculosis: insights from genomic deletions in 100 strains.
Proc Natl Acad Sci U S A (2004) 101(14):4865-70
Cited for: Mutant
Bertrand T, Eady NA, Jones JN, J esmin, Nagy JM, Jamart-Gregoire B, Raven EL, Brown KA,
Crystal structure of Mycobacterium tuberculosis catalase-peroxidase.
J Biol Chem (2004) 279(37):38991-9
Cited for: Structure
Mawuenyega KG, Forst CV, Dobos KM, Belisle JT, Chen J, Bradbury EM, Bradbury AR, Chen X,
Mycobacterium tuberculosis functional network analysis by global subcellular protein profiling.
Mol Biol Cell (2005) 16(1):396-404
Cited for: Proteomics
Xiong Y, Chalmers MJ, Gao FP, Cross TA, Marshall AG,
Identification of Mycobacterium tuberculosis H37Rv integral membrane proteins by one-dimensional gel electrophoresis and liquid chromatography electrospray ionization tandem mass spectrometry.
J Proteome Res (2005) 4(3):855-61
Cited for: Proteomics
Zhao X, Yu H, Yu S, Wang F, Sacchettini JC, Magliozzo RS,
Hydrogen peroxide-mediated isoniazid activation catalyzed by Mycobacterium tuberculosis catalase-peroxidase (KatG) and its S315T mutant.
Biochemistry (2006) 45(13):4131-40
Cited for: Structure
Rodrigue S, Brodeur J, Jacques PE, Gervais AL, Brzezinski R, Gaudreau L,
Identification of mycobacterial sigma factor binding sites by chromatin immunoprecipitation assays.
J Bacteriol (2007) 189(5):1505-13
Cited for: Regulon
Malen H, Berven FS, Fladmark KE, Wiker HG,
Comprehensive analysis of exported proteins from Mycobacterium tuberculosis H37Rv.
Proteomics (2007) 7(10):1702-18
Cited for: Proteomics
Zvi A, Ariel N, Fulkerson J, Sadoff JC, Shafferman A,
Whole genome identification of Mycobacterium tuberculosis vaccine candidates by comprehensive data mining and bioinformatic analyses.
BMC Med Genomics (2008) 1:18
Cited for: Immunology
Malen H, Pathak S, Softeland T, de Souza GA, Wiker HG,
Definition of novel cell envelope associated proteins in Triton X-114 extracts of Mycobacterium tuberculosis H37Rv.
BMC Microbiol (2010) 10:132
Cited for: Proteomics
de Souza GA, Arntzen MO, Fortuin S, Schurch AC, Malen H, McEvoy CR, van Soolingen D, Thiede B, Warren RM, Wiker HG,
Proteogenomic analysis of polymorphisms and gene annotation divergences in prokaryotes using a clustered mass spectrometry-friendly database.
Mol Cell Proteomics (2011) 10(1):M110.002527
Cited for: Proteomics/Sequence
de Souza GA, Leversen NA, Malen H, Wiker HG,
Bacterial proteins with cleaved or uncleaved signal peptides of the general secretory pathway.
J Proteomics (2011) 75(2):502-10
Cited for: Proteomics
Kelkar DS, Kumar D, Kumar P, Balakrishnan L, Muthusamy B, Yadav AK, Shrivastava P, Marimuthu A, Anand S, Sundaram H, Kingsbury R, Harsha HC, Nair B, Prasad TS, Chauhan DS, Katoch K, Katoch VM, Kumar P, Chaerkady R, Ramachandran S, Dash D, Pandey A,
Proteogenomic analysis of Mycobacterium tuberculosis by high resolution mass spectrometry.
Mol Cell Proteomics (2011) 10(12):M111.011627
Cited for: Proteomics/Sequence
Griffin JE, Gawronski JD, Dejesus MA, Ioerger TR, Akerley BJ, Sassetti CM,
High-resolution phenotypic profiling defines genes essential for mycobacterial growth and cholesterol catabolism.
PLoS Pathog (2011) 7(9):e1002251
Cited for: Mutant
Heym B, Alzari PM, Honore N, Cole ST,
Missense mutations in the catalase-peroxidase gene, katG, are associated with isoniazid resistance in Mycobacterium tuberculosis
Mol Microbiol (1995) 15(2):235-45
Cited for: Product/Mutant
Heym B, Stavropoulos E, Honore N, Domenech P, Saint-Joanis B, Saint -Joanis B, Wilson TM, Collins DM, Colston MJ, Cole ST,
Effects of overexpression of the alkyl hydroperoxide reductase AhpC on the virulence and isoniazid resistance of Mycobacterium tuberculosis
Infect Immun (1997) 65(4):1395-401
Cited for: Secondary/Mutant