ID   SODF_LEGPH              Reviewed;         192 AA.
AC   P31108; Q5ZRB5;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Superoxide dismutase [Fe];
DE            EC=1.15.1.1;
GN   Name=sodB; OrderedLocusNames=lpg2967;
OS   Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC
OS   33152 / DSM 7513).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=272624;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9086394; DOI=10.7883/yoken1952.49.167;
RA   Amemura-Maekawa J., Kura F., Watanabe H.;
RT   "Cloning and nucleotide sequences of iron and copper-zinc superoxide
RT   dismutase genes of Legionella pneumophila and their distribution among
RT   Legionella species.";
RL   Jpn. J. Med. Sci. Biol. 49:167-186(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
RX   PubMed=15448271; DOI=10.1126/science.1099776;
RA   Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G.,
RA   Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V.,
RA   Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S., Georghiou A.,
RA   Chou I.-C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A.,
RA   Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A.,
RA   Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A.,
RA   Russo J.J.;
RT   "The genomic sequence of the accidental pathogen Legionella pneumophila.";
RL   Science 305:1966-1968(2004).
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=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC       Note=Binds 1 Fe cation per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAU29013.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; D12922; BAA02306.1; -; Genomic_DNA.
DR   EMBL; AE017354; AAU29013.1; ALT_INIT; Genomic_DNA.
DR   PIR; JS0749; JS0749.
DR   RefSeq; WP_016357051.1; NC_002942.5.
DR   RefSeq; YP_096960.1; NC_002942.5.
DR   AlphaFoldDB; P31108; -.
DR   SMR; P31108; -.
DR   STRING; 272624.lpg2967; -.
DR   PaxDb; P31108; -.
DR   PRIDE; P31108; -.
DR   EnsemblBacteria; AAU29013; AAU29013; lpg2967.
DR   GeneID; 66492135; -.
DR   KEGG; lpn:lpg2967; -.
DR   PATRIC; fig|272624.6.peg.3172; -.
DR   eggNOG; COG0605; Bacteria.
DR   HOGENOM; CLU_031625_0_0_6; -.
DR   Proteomes; UP000000609; 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; Metal-binding; Oxidoreductase; Reference proteome.
FT   CHAIN           1..192
FT                   /note="Superoxide dismutase [Fe]"
FT                   /id="PRO_0000159987"
FT   BINDING         27
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         74
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         157
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         161
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   192 AA;  21639 MW;  CA30F5459C0B4E9E CRC64;
     MTFTLPQLPY ALDALAPHVS KETLEYHYGK HHNTYVTNLN KLIPGTEFES MTLEEIIMKA
     KGGIFNNAAQ VWNHTFYWHS MSPNGGGEPK GRLAEAINKS FGSFAAFKEQ FSQTAATTFG
     SGWAWLVQDQ SGALKIINTS NAGTPMTEGL NALLTCDVWE HAYYIDYRNR RPDYIEAFWS
     LVNWDFASSN LK