ID   SODM_YEREN              Reviewed;         207 AA.
AC   P53655;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Superoxide dismutase [Mn];
DE            EC=1.15.1.1;
GN   Name=sodA;
OS   Yersinia enterocolitica.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=630;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 51871 / WA-314 / Serotype O:8;
RX   PubMed=9353054; DOI=10.1128/iai.65.11.4705-4710.1997;
RA   Roggenkamp A., Bittner T., Leitritz L., Sing A., Heesemann J.;
RT   "Contribution of the Mn-cofactored superoxide dismutase (SodA) to the
RT   virulence of Yersinia enterocolitica serotype O8.";
RL   Infect. Immun. 65:4705-4710(1997).
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   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC       {ECO:0000305}.
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DR   EMBL; X96852; CAA65596.1; -; Genomic_DNA.
DR   RefSeq; WP_005175051.1; NZ_NWMR01000012.1.
DR   AlphaFoldDB; P53655; -.
DR   SMR; P53655; -.
DR   STRING; 1443113.LC20_00043; -.
DR   eggNOG; COG0605; Bacteria.
DR   OrthoDB; 1440645at2; -.
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.
FT   CHAIN           1..207
FT                   /note="Superoxide dismutase [Mn]"
FT                   /id="PRO_0000160111"
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         169
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         173
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   207 AA;  23229 MW;  DA040FF68D068F8F CRC64;
     MSYSLPSLPY AYDALEPHFD KQTMEIHHTK HHQTYVNNAN TVLESFPELA KFSVEDLIKD
     LDKVPAEKRT FMRNNAGGHA NHSLFWKGLK LGTTLTGDLK AAIERDFGSV DSFKEKFEAA
     AATRFGSGWA WLVLKDDGKL AVVSTANQDS PLMGEAVSGA SGFPIVGLDV WEHAYYLKFQ
     NRRPDYIKAF WNVVNWDEAA ARFAQAK