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SODM_STRA5
ID   SODM_STRA5              Reviewed;         202 AA.
AC   P0A4J4; 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 86.
DE   RecName: Full=Superoxide dismutase [Mn/Fe];
DE            EC=1.15.1.1 {ECO:0000250|UniProtKB:P80293};
GN   Name=sodA; Synonyms=sod; OrderedLocusNames=SAG0788;
OS   Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=208435;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-611 / 2603 V/R;
RX   PubMed=12200547; DOI=10.1073/pnas.182380799;
RA   Tettelin H., Masignani V., Cieslewicz M.J., Eisen J.A., Peterson S.N.,
RA   Wessels M.R., Paulsen I.T., Nelson K.E., Margarit I., Read T.D.,
RA   Madoff L.C., Wolf A.M., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA   DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Lewis M.R., Radune D.,
RA   Fedorova N.B., Scanlan D., Khouri H.M., Mulligan S., Carty H.A.,
RA   Cline R.T., Van Aken S.E., Gill J., Scarselli M., Mora M., Iacobini E.T.,
RA   Brettoni C., Galli G., Mariani M., Vegni F., Maione D., Rinaudo D.,
RA   Rappuoli R., Telford J.L., Kasper D.L., Grandi G., Fraser C.M.;
RT   "Complete genome sequence and comparative genomic analysis of an emerging
RT   human pathogen, serotype V Streptococcus agalactiae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:12391-12396(2002).
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; AE009948; AAM99675.1; -; Genomic_DNA.
DR   RefSeq; NP_687803.1; NC_004116.1.
DR   RefSeq; WP_000974719.1; NC_004116.1.
DR   AlphaFoldDB; P0A4J4; -.
DR   SMR; P0A4J4; -.
DR   STRING; 208435.SAG0788; -.
DR   EnsemblBacteria; AAM99675; AAM99675; SAG0788.
DR   KEGG; sag:SAG0788; -.
DR   PATRIC; fig|208435.3.peg.795; -.
DR   HOGENOM; CLU_031625_0_1_9; -.
DR   OMA; YEGWKGE; -.
DR   Proteomes; UP000000821; 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; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..202
FT                   /note="Superoxide dismutase [Mn/Fe]"
FT                   /id="PRO_0000160087"
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"
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
 
 
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