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Search term: Rv0432

General annotation | Coordinates | Sequence | Structural information | Orthologs/Cross-references | Interacting Drugs/Compounds | Bibliography
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General annotation
Gene namesodC
Rv numberRv0432
FunctionDestroys radicals which are normally produced within the cells and are toxic to biological systems [catalytic activity: 2 superoxide + 2 H+ = O2 + H2O2].
ProductPeriplasmic superoxide dismutase [Cu-Zn] SodC
CommentsRv0432, (MTCY22G10.29), len: 240 aa. sodC, periplasmic superoxide dismutase [Cu-Zn], equivalent to CAC30880.1|AL583923 superoxide dismutase precursor (Cu-Zn) from Mycobacterium leprae (240 aa); and AAK20038.1|AF326234_1 copper zinc superoxide dismutase from Mycobacterium avium subsp. paratuberculosis (226 aa). Also similar to others e.g. SODC_PHOLE|P00446 superoxide dismutase precursor (Cu-Zn) from Photobacterium leiognathi (173 aa), FASTA scores: opt: 214, E(): 5.2 e-06, (36.5% identity in 181 aa overlap). Contains PS00013 Prokaryotic membrane lipoprotein lipid attachment site. Belongs to the Cu-Zn superoxide dismutase family. Possibly localized in periplasm, membrane-bound.
Molecular mass (Da)23844.5
Isoelectric point6.4255
Gene length (bp)723
Protein length240
Location (kb)519.6

Functional categoryvirulence, detoxification, adaptation

ProteomicsIdentified in the membrane fraction of M. tuberculosis H37Rv using 1D-SDS-PAGE and uLC-MS/MS (See Gu et al., 2003). Identified in the membrane fraction of M. tuberculosis H37Rv using nanoLC-MS/MS (See Xiong et al., 2005). Identified in the detergent phase of Triton X-114 extracts of M. tuberculosis H37Rv membranes using 1-DGE and MALDI-TOF-MS (See Sinha et al., 2005). Putative glycoprotein identified by LC/ESI-MS/MS in the culture filtrate of M. tuberculosis H37Rv (See Gonzalez-Zamorano et al., 2009). Identified by mass spectrometry in Triton X-114 extracts of M. tuberculosis H37Rv (See Malen et al., 2010). Identified by mass spectrometry in the membrane protein fraction and whole cell lysates of M. tuberculosis H37Rv but not the culture filtrate (See de Souza et al., 2011).
Mutationnon essential gene by Himar1-based transposon mutagenesis in H37Rv strain (see Sassetti et al., 2003). Non-essential gene for in vitro growth of H37Rv, by sequencing of Himar1-based transposon mutagenesis (See Griffin et al., 2011). Check for mutants available at TARGET website


Protein sequence in FASTA format
>M. tuberculosis H37Rv|Rv0432|sodC
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 Bank1PZS

Enzyme Classification1.15.1.1
Gene Ontologysuperoxide dismutase activity
plasma membrane
superoxide metabolic process
metal ion binding
oxidation reduction
M. bovisMb0440
M. lepraeML1925
M. marinumMMAR_0747
M. smegmatisMSMEG_0835
Multiple Sequences Alignment: between orthologs

Interacting Drugs/Compounds
TDR TargetsRv0432

Expression Data

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
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
Spagnolo L, Toro I, D'Orazio M, O'Neill P, Pedersen JZ, Carugo O, Rotilio G, Battistoni A, Djinovic-Carugo K,
Unique features of the sodC-encoded superoxide dismutase from Mycobacterium tuberculosis, a fully functional copper-containing enzyme lacking zinc in the active site.
J Biol Chem (2004) 279(32):33447-55
Cited for: Structure
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
Sinha S, Kosalai K, Arora S, Namane A, Sharma P, Gaikwad AN, Brodin P, Cole ST,
Immunogenic membrane-associated proteins of Mycobacterium tuberculosis revealed by proteomics.
Microbiology (2005) 151(Pt 7):2411-9
Cited for: Proteomics
Gonzalez-Zamorano M, Mendoza-Hernandez G, Xolalpa W, Parada C, Vallecillo AJ, Bigi F, Espitia C,
Mycobacterium tuberculosis glycoproteomics based on ConA-lectin affinity capture of mannosylated proteins.
J Proteome Res (2009) 8(2):721-33
Cited for: Proteomics
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, 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
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