SODM_STRA3
ID SODM_STRA3 Reviewed; 202 AA.
AC P0A4J3; O33604; O54086; O54091; Q59799;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Superoxide dismutase [Mn/Fe];
DE EC=1.15.1.1 {ECO:0000250|UniProtKB:P80293};
GN Name=sodA; Synonyms=sod; OrderedLocusNames=gbs0808;
OS Streptococcus agalactiae serotype III (strain NEM316).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=211110;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NEM318 / Serotype III;
RA Gaillot I., Poyart C., Berche P., Trieu-Cuot P.;
RT "Molecular characterization and expression analysis of the superoxide
RT dismutase gene from Streptococcus agalacitiae.";
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEM316;
RX PubMed=12354221; DOI=10.1046/j.1365-2958.2002.03126.x;
RA Glaser P., Rusniok C., Buchrieser C., Chevalier F., Frangeul L., Msadek T.,
RA Zouine M., Couve E., Lalioui L., Poyart C., Trieu-Cuot P., Kunst F.;
RT "Genome sequence of Streptococcus agalactiae, a pathogen causing invasive
RT neonatal disease.";
RL Mol. Microbiol. 45:1499-1513(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 18-162.
RC STRAIN=ATCC 12403 / CIP 82.45 / D136C / Serotype III;
RX PubMed=7557308; DOI=10.1016/0378-1097(95)00232-t;
RA Poyart C., Berche P., Trieu-Cuot P.;
RT "Characterization of superoxide dismutase genes from Gram-positive bacteria
RT by polymerase chain reaction using degenerate primers.";
RL FEMS Microbiol. Lett. 131:41-45(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 18-162.
RC STRAIN=ATCC 12403 / CIP 82.45 / D136C / Serotype III, and
RC NEM318 / Serotype III;
RX PubMed=9431917; DOI=10.1128/jcm.36.1.41-47.1998;
RA Poyart C., Quesne G., Coulon S., Berche P., Trieu-Cuot P.;
RT "Identification of streptococci to species level by sequencing the gene
RT encoding the manganese-dependent superoxide dismutase.";
RL J. Clin. Microbiol. 36:41-47(1998).
CC -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC produced within the cells and which are toxic to biological systems.
CC Catalyzes the dismutation of superoxide anion radicals into O2 and H2O2
CC by successive reduction and oxidation of the transition metal ion at
CC the active site. {ECO:0000250|UniProtKB:P80293}.
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 Evidence={ECO:0000250|UniProtKB:P80293};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20697;
CC Evidence={ECO:0000250|UniProtKB:P80293};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P80293};
CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC Evidence={ECO:0000250|UniProtKB:P80293};
CC Note=Binds 1 Mn(2+) or Fe(3+) ion per subunit.
CC {ECO:0000250|UniProtKB:P80293};
CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; Y12224; CAA72899.1; -; Genomic_DNA.
DR EMBL; AL766847; CAD46452.1; -; Genomic_DNA.
DR EMBL; Z49249; CAA89216.1; -; Genomic_DNA.
DR EMBL; Z99178; CAB16322.1; -; Genomic_DNA.
DR EMBL; Z99179; CAB16323.1; -; Genomic_DNA.
DR RefSeq; WP_000974719.1; NC_004368.1.
DR AlphaFoldDB; P0A4J3; -.
DR SMR; P0A4J3; -.
DR STRING; 211110.gbs0808; -.
DR EnsemblBacteria; CAD46452; CAD46452; CAD46452.
DR KEGG; san:sod; -.
DR eggNOG; COG0605; Bacteria.
DR HOGENOM; CLU_031625_0_1_9; -.
DR OMA; YEGWKGE; -.
DR Proteomes; UP000000823; Chromosome.
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; 3.55.40.20; -; 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 Iron; Manganese; Metal-binding; Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..202
FT /note="Superoxide dismutase [Mn/Fe]"
FT /id="PRO_0000160086"
FT BINDING 27
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000250|UniProtKB:P80293"
FT BINDING 27
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P80293"
FT BINDING 81
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000250|UniProtKB:P80293"
FT BINDING 81
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P80293"
FT BINDING 163
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000250|UniProtKB:P80293"
FT BINDING 163
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P80293"
FT BINDING 167
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000250|UniProtKB:P80293"
FT BINDING 167
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P80293"
FT VARIANT 68
FT /note="R -> A (in strain: NEM318)"
FT VARIANT 104
FT /note="N -> D (in strain: ATCC 12403)"
SQ SEQUENCE 202 AA; 22621 MW; BA9A6878BB6F2E83 CRC64;
MAIILPDLPY AYDALEPHID AETMTLHHDK HHATYVANAN AALEKHPEIG EDLEALLADV
SQIPEDIRQA VINNGGGHLN HALFWELMSP EETQISQELS EDINATFGSF EDFKAAFTAA
ATGRFGSGWA WLVVNAEGKL EVLSTANQDT PIMEGKKPIL GLDVWEHAYY LNYRNVRPNY
IKAFFEIINW NKVNELYQAA KA
