Nakayama,K. Nucleotide sequence of Streptococcus mutans superoxide dismutase gene and isolation of insertion mutants J. Bacteriol. 174 (15), 4928-4934 (1992) PubMed: 1321118
Martin,M.E., Byers,B.R., Olson,M.O., Salin,M.L., Arceneaux,J.E. and Tolbert,C. A Streptococcus mutans superoxide dismutase that is active with either manganese or iron as a cofactor J. Biol. Chem. 261 (20), 9361-9367 (1986) PubMed: 3722201
Poyart,C., Quesne,G., Coulon,S., Berche,P. and Trieu-Cuot,P. Identification of streptococci to species level by sequencing the gene encoding the manganese-dependent superoxide dismutase J. Clin. Microbiol. 36 (1), 41-47 (1998) PubMed: 9431917
Secondary Evidence: Gerlach,D., Reichardt,W. and Vettermann,S. Extracellular superoxide dismutase from Streptococcus pyogenes type 12 strain is manganese-dependent FEMS Microbiol. Lett. 160 (2), 217-224 (1998) PubMed: 9532741
Gibson,C.M. and Caparon,M.G. Insertional inactivation of Streptococcus pyogenes sod suggests that prtF is regulated in response to a superoxide signal J. Bacteriol. 178 (15), 4688-4695 (1996) PubMed: 8755901
Poyart,C., Berche,P. and Trieu-Cuot,P. Characterization of superoxide dismutase genes from gram-positive bacteria by polymerase chain reaction using degenerate primers FEMS Microbiol. Lett. 131 (1), 41-45 (1995) PubMed: 7557308
Inaoka,T., Matsumura,Y. and Tsuchido,T. Molecular cloning and nucleotide sequence of the superoxide dismutase gene and characterization of its product from Bacillus subtilis J. Bacteriol. 180 (14), 3697-3703 (1998) PubMed: 9658017
Sanders,J.W., Leenhouts,K.J., Haandrikman,A.J., Venema,G. and Kok,J. Stress response in Lactococcus lactis: cloning, expression analysis, and mutation of the lactococcal superoxide dismutase gene J. Bacteriol. 177 (18), 5254-5260 (1995) PubMed: 7665513
Bowler,C., Van Kaer,L., Van Camp,W., Van Montagu,M., Inze,D. and Dhaese,P. Characterization of the Bacillus stearothermophilus manganese superoxide dismutase gene and its ability to complement copper/zinc superoxide dismutase deficiency in Saccharomyces cerevisiae J. Bacteriol. 172 (3), 1539-1546 (1990) PubMed: 2407726
Comment: This enzyme destroys radicals which are normally produced within the cells and are toxic to biological systems [gi:2507403].
Blast Summary:PSI-Blast Search Matches in gapped BLAST to superoxide dismutase:residues 1-203 are 93% similar to the previously published enzyme in S.mutans (2507403|).
Residues 1-200 are 78% similar to the enzyme from S.pyogenes (15675326|) and are 76% similar to the enzyme from S.agalactiae (2765187|).
The best hit to the Streptococcus agalactiae 2603 V/R genome is to SAG0788 (1e-90).
Top Blast Hits:Updated monthly
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COGS Summary:COGS Search BeTs to 11 clades of COG0605
COG name: Superoxide dismutase
Functional Class: P
The phylogenetic pattern of COG0605 is --t-Yq-cEBrhuj--o-inx
Number of proteins in this genome belonging to this COG is 1 Blocks Summary:Blocks Search ***** IPB001189 (Manganese and iron superoxide dismutase (SODM)) with a combined E-value of 2.1e-92. IPB001189A 5-40 IPB001189B 74-90 IPB001189C 95-132 IPB001189D 158-190
ProDom Summary:Protein Domain Search Residues 5-200 are 92% similar to a (DISMUTASE SUPEROXIDE OXIDOREDUCTASE MANGANESE MN IRON) protein domain (PD000475 which is seen in SODM_STRMU.
Paralogs:Local Blast Search SMu0571 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.
Pfam Summary:Pfam Search Residues 2 to 89 (E-value = 3.2e-42) place SMu0571 in the Sod_Fe_N family which is described as Iron/manganese superoxide dismutases, alpha-hairpin domain (PF00081) Residues 96 to 197 (E-value = 5e-61) place SMu0571 in the Sod_Fe_C family which is described as Iron/manganese superoxide dismutases, C-terminal domain (PF02777)
Top PDB Hits: pdb|1MNG|A Chain A, Manganese Superoxide Dismutase (E.C.1.15.1.... 217 9e-058 pdb|1D5N|A Chain A, Crystal Structure Of E. Coli Mnsod At 100k ... 199 2e-052 pdb|1VAR|A Chain A, Mitochondrial Manganese Superoxide Dismutas... 166 2e-042
Gene Protein Sequence:
MAILLPDLPYAYDALEPYIDAETMTLHHDKHHATYVANANAALEKHPEIG ENLEVLLADVEQIPADIRQSLINNGGGHLNHALFWELLSPEKTKVTAEVA AAINEAFGSFDDFKAAFTAAATTRFGSGWAWLVVDKEGKLEVTSTANQDT PISQGLKPILALDVWEHAYYLNYRNVRPNYIKAFFEVINWNTVARLYAEA LTK