ID   SODM_LISMO              Reviewed;         202 AA.
AC   P28764;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Superoxide dismutase [Mn];
DE            EC=1.15.1.1;
GN   Name=sodA; Synonyms=sod; OrderedLocusNames=lmo1439;
OS   Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=169963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=EGD / Serovar 1/2a;
RX   PubMed=1511873; DOI=10.1016/0378-1119(92)90258-q;
RA   Brehm K., Haas A., Goebel W., Kreft J.;
RT   "A gene encoding a superoxide dismutase of the facultative intracellular
RT   bacterium Listeria monocytogenes.";
RL   Gene 118:121-125(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-679 / EGD-e;
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA   Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA   Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA   Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA   Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA   Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA   Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA   Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA   Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA   Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
CC   -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC       produced within the cells and which are toxic to biological 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   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC       {ECO:0000305}.
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DR   EMBL; M80526; AAA25292.1; -; Genomic_DNA.
DR   EMBL; AL591979; CAC99517.1; -; Genomic_DNA.
DR   PIR; AG1254; AG1254.
DR   PIR; JC1272; JC1272.
DR   RefSeq; NP_464964.1; NC_003210.1.
DR   RefSeq; WP_003721944.1; NZ_CP023861.1.
DR   AlphaFoldDB; P28764; -.
DR   SMR; P28764; -.
DR   STRING; 169963.lmo1439; -.
DR   PaxDb; P28764; -.
DR   EnsemblBacteria; CAC99517; CAC99517; CAC99517.
DR   GeneID; 986791; -.
DR   KEGG; lmo:lmo1439; -.
DR   PATRIC; fig|169963.11.peg.1478; -.
DR   eggNOG; COG0605; Bacteria.
DR   HOGENOM; CLU_031625_0_1_9; -.
DR   OMA; YEGWKGE; -.
DR   PhylomeDB; P28764; -.
DR   BioCyc; LMON169963:LMO1439-MON; -.
DR   Proteomes; UP000000817; 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   Manganese; Metal-binding; Oxidoreductase; Reference proteome.
FT   CHAIN           1..202
FT                   /note="Superoxide dismutase [Mn]"
FT                   /id="PRO_0000160044"
FT   BINDING         27
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         82
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         164
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         168
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   202 AA;  22631 MW;  75D40A4C45A93450 CRC64;
     MTYELPKLPY TYDALEPNFD KETMEIHYTK HHNTYVTKLN EAVAGHPELA SKSAEELVTN
     LDSVPEDIRG AVRNHGGGHA NHTLFWSILS PNGGGAPTGN LKAAIESEFG TFDEFKEKFN
     AAAAARFGSG WAWLVVNDGK LEIVSTANQD SPLSDGKTPV LGLDVWEHAY YLKFQNRRPE
     YIETFWNVIN WDEANKRFDA AK