ID SODM_STRP8 Reviewed; 201 AA.
AC Q8P0D4;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 05-DEC-2018, entry version 96.
DE RecName: Full=Superoxide dismutase [Mn];
DE EC=1.15.1.1;
GN Name=sodA; OrderedLocusNames=spyM18_1414;
OS Streptococcus pyogenes serotype M18 (strain MGAS8232).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=186103;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGAS8232;
RX PubMed=11917108; DOI=10.1073/pnas.062526099;
RA Smoot J.C., Barbian K.D., Van Gompel J.J., Smoot L.M., Chaussee M.S.,
RA Sylva G.L., Sturdevant D.E., Ricklefs S.M., Porcella S.F.,
RA Parkins L.D., Beres S.B., Campbell D.S., Smith T.M., Zhang Q.,
RA Kapur V., Daly J.A., Veasy L.G., Musser J.M.;
RT "Genome sequence and comparative microarray analysis of serotype M18
RT group A Streptococcus strains associated with acute rheumatic fever
RT outbreaks.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4668-4673(2002).
CC -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC produced within the cells and which are toxic to biological
CC systems.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:18421; EC=1.15.1.1;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC family. {ECO:0000305}.
CC -!- CAUTION: Although found extracellularly, no signal sequence is
CC present. An alternative secretory pathway may be used.
CC {ECO:0000305}.
DR EMBL; AE009949; AAL98003.1; -; Genomic_DNA.
DR RefSeq; WP_011017948.1; NC_003485.1.
DR ProteinModelPortal; Q8P0D4; -.
DR SMR; Q8P0D4; -.
DR EnsemblBacteria; AAL98003; AAL98003; spyM18_1414.
DR KEGG; spm:spyM18_1414; -.
DR HOGENOM; HOG000013583; -.
DR KO; K04564; -.
DR OMA; YEGWKGE; -.
DR BioCyc; SPYO186103:G1FZQ-1260-MONOMER; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR Gene3D; 1.10.287.990; -; 1.
DR Gene3D; 2.40.500.20; -; 1.
DR InterPro; IPR001189; Mn/Fe_SOD.
DR InterPro; IPR019833; Mn/Fe_SOD_BS.
DR InterPro; IPR019832; Mn/Fe_SOD_C.
DR InterPro; IPR019831; Mn/Fe_SOD_N.
DR InterPro; IPR036324; Mn/Fe_SOD_N_sf.
DR InterPro; IPR036314; SOD_C_sf.
DR Pfam; PF02777; Sod_Fe_C; 1.
DR Pfam; PF00081; Sod_Fe_N; 1.
DR PIRSF; PIRSF000349; SODismutase; 1.
DR PRINTS; PR01703; MNSODISMTASE.
DR SUPFAM; SSF46609; SSF46609; 1.
DR SUPFAM; SSF54719; SSF54719; 1.
DR PROSITE; PS00088; SOD_MN; 1.
PE 3: Inferred from homology;
KW Manganese; Metal-binding; Oxidoreductase; Secreted.
FT INIT_MET 1 1 Removed. {ECO:0000250}.
FT CHAIN 2 201 Superoxide dismutase [Mn].
FT /FTId=PRO_0000160104.
FT METAL 27 27 Manganese. {ECO:0000250}.
FT METAL 81 81 Manganese. {ECO:0000250}.
FT METAL 163 163 Manganese. {ECO:0000250}.
FT METAL 167 167 Manganese. {ECO:0000250}.
SQ SEQUENCE 201 AA; 22653 MW; 7550586B0E7ED53F CRC64;
MAIILPELPY AYDALEPQFD AETMSLHHDK HHATYVANTN AALEKHPEIG ENLEELLADV
TKIPEDIRQA LINNGGGHLN HALFWELLSP EKQDVTPDVA QAIDDAFGSF DAFKEQFTAA
ATGRFGSGWA WLVVNKEGQL EITSTANQDT PISEGKKPIL ALDVWEHAYY LNYRNVRPNY
IKAFFEIINW KKVSELYQAA K
//
