Gene Rv3846 (sodB, sod)
in Mycobacterium tuberculosis H37Rv
General annotation
| Type | CDS |
| Function | Destroys radicals which are normally produced within the cells and are toxic to biological systems [catalytic activity: 2 peroxide radical + 2 H(+) = O(2) + H(2)O(2)]. |
| Product | Superoxide dismutase [FE] SodA |
| Comments | Rv3846, (MTCY01A6.22c), len: 207 aa. SodA (alternate gene names: sodB, sod), superoxide dismutase (see citations below), equivalent to many e.g. P47201|SODM_MYCAV|soda|sod from Mycobacterium avium (206 aa), FASTA scores: opt: 1210, E(): 1.8e-73, (82.5% identity in 206 aa overlap); Q9F9R1|sod from Mycobacterium paratuberculosis (207 aa), FASTA scores: opt: 1207, E(): 2.9e-73, (81.65% identity in 207 aa overlap); O86165|SODM_MYCLP|soda|sod from Mycobacterium lepraemurium (206 aa), FASTA scores: opt: 1204, E(): 4.5e-73, (82.05% identity in 206 aa overlap); P13367|SODM_MYCLE|soda|ML0072 from Mycobacterium leprae (206 aa), FASTA scores: opt: 1169, E(): 9.6e-71, (80.5% identity in 205 aa overlap); etc. Contains PS00088 Manganese and iron superoxide dismutases signature. Belongs to the iron/manganese superoxide dismutase family. Although found extracellularly, no signal sequence is present. An alternative secretory pathway may be used. |
| Functional category | Virulence, detoxification, adaptation |
| Proteomics | Corresponds to spots SodA identified in short term culture filtrate and cytosol by proteomics at the Statens Serum Institute (Denmark) (see proteomics citations). 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 culture supernatant of M. tuberculosis H37Rv using mass spectrometry and Edman degradation (See Mattow 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). |
| Transcriptomics | mRNA identified by DNA microarray analysis: possibly down-regulated by hrcA|Rv2374c (see Stewart et al., 2002), and up-regulated after 4h, 24h and 96h of starvation (see Betts et al., 2002). |
| Mutant | Essential gene for in vitro growth of H37Rv in a MtbYM rich medium, by Himar1 transposon mutagenesis (see Minato et al. 2019). Essential gene for in vitro growth of H37Rv, by analysis of saturated Himar1 transposon libraries (see DeJesus et al. 2017). Essential gene for in vitro growth of H37Rv, by Himar1 transposon mutagenesis (See Griffin et al., 2011). Check for mutants available at TARGET website |
Coordinates
| Type | Start | End | Orientation |
|---|---|---|---|
| CDS | 4320704 | 4321327 | + |
Genomic sequence
Feature type
Upstream flanking region (bp)
Downstream flanking region (bp)
Update
Protein sequence
>Mycobacterium tuberculosis H37Rv|Rv3846|sodA
VAEYTLPDLDWDYGALEPHISGQINELHHSKHHATYVKGANDAVAKLEEARAKEDHSAILLNEKNLAFNLAGHVNHTIWWKNLSPNGGDKPTGELAAAIADAFGSFDKFRAQFHAAATTVQGSGWAALGWDTLGNKLLIFQVYDHQTNFPLGIVPLLLLDMWEHAFYLQYKNVKVDFAKAFWNVVNWADVQSRYAAATSQTKGLIFG
Bibliography
- Zhang Y et al. [1991]. Genetic analysis of superoxide dismutase, the 23 kilodalton antigen of Mycobacterium tuberculosis. Product
- Cooper JB et al. [1995]. X-ray structure analysis of the iron-dependent superoxide dismutase from Mycobacterium tuberculosis at 2.0 Angstroms resolution reveals novel dimer-dimer interactions. Structure
- Cooper JB et al. [1996]. X-ray structure analysis of an engineered Fe-superoxide dismutase Gly-Ala mutant with significantly reduced stability to denaturant. Structure
- Bunting K et al. [1998]. Engineering a change in metal-ion specificity of the iron-dependent superoxide dismutase from Mycobacterium tuberculosis-- X-ray structure analysis of site-directed mutants. Structure
- Harth G et al. [1999]. Export of recombinant Mycobacterium tuberculosis superoxide dismutase is dependent upon both information in the protein and mycobacterial export machinery. A model for studying export of leaderless proteins by pathogenic mycobacteria. Product
- Rosenkrands I, Weldingh K, Jacobsen S, Hansen CV, Florio W, Gianetri I and Andersen P [2000]. Mapping and identification of Mycobacterium tuberculosis proteins by two-dimensional gel electrophoresis, microsequencing and immunodetection. Proteomics
- Rosenkrands I et al. [2000]. Towards the proteome of Mycobacterium tuberculosis. Proteomics
- Pym AS et al. [2001]. Regulation of catalase-peroxidase (KatG) expression, isoniazid sensitivity and virulence by furA of Mycobacterium tuberculosis. Secondary Regulation
- Stewart GR et al. [2002]. Dissection of the heat-shock response in Mycobacterium tuberculosis using mutants and microarrays. Transcriptome Regulation
- Betts JC et al. [2002]. Evaluation of a nutrient starvation model of Mycobacterium tuberculosis persistence by gene and protein expression profiling. Transcriptome
- Bunting KA et al. [2002]. Engineering of an intersubunit disulfide bridge in the iron-superoxide dismutase of Mycobacterium tuberculosis. Structure
- Braunstein M et al. [2003]. SecA2 functions in the secretion of superoxide dismutase A and in the virulence of Mycobacterium tuberculosis. Secondary Function
- Gu S et al. [2003]. Comprehensive proteomic profiling of the membrane constituents of a Mycobacterium tuberculosis strain. Proteomics
- Mattow J, Schaible UE, Schmidt F, Hagens K, Siejak F, Brestrich G, Haeselbarth G, Muller EC, Jungblut PR and Kaufmann SH [2003]. Comparative proteome analysis of culture supernatant proteins from virulent Mycobacterium tuberculosis H37Rv and attenuated M. bovis BCG Copenhagen. Proteomics
- Xiong Y, Chalmers MJ, Gao FP, Cross TA and Marshall AG [2005]. Identification of Mycobacterium tuberculosis H37Rv integral membrane proteins by one-dimensional gel electrophoresis and liquid chromatography electrospray ionization tandem mass spectrometry. Proteomics
- Mawuenyega KG et al. [2005]. Mycobacterium tuberculosis functional network analysis by global subcellular protein profiling. Proteomics
- Målen H et al. [2007]. Comprehensive analysis of exported proteins from Mycobacterium tuberculosis H37Rv. Proteomics
- Målen H et al. [2010]. Definition of novel cell envelope associated proteins in Triton X-114 extracts of Mycobacterium tuberculosis H37Rv. Proteomics
- de Souza GA et al. [2011]. Bacterial proteins with cleaved or uncleaved signal peptides of the general secretory pathway. Proteomics
- Kelkar DS et al. [2011]. Proteogenomic analysis of Mycobacterium tuberculosis by high resolution mass spectrometry. Proteomics Sequence
- Griffin JE et al. [2011]. High-resolution phenotypic profiling defines genes essential for mycobacterial growth and cholesterol catabolism. Mutant
- de Souza GA et al. [2011]. Proteogenomic analysis of polymorphisms and gene annotation divergences in prokaryotes using a clustered mass spectrometry-friendly database. Proteomics Sequence
- DeJesus MA et al. [2017]. Comprehensive Essentiality Analysis of the Mycobacterium tuberculosis Genome via Saturating Transposon Mutagenesis. Mutant
- Minato Y et al. [2019]. Genomewide Assessment of Mycobacterium tuberculosis Conditionally Essential Metabolic Pathways. Mutant
