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 24-JAN-2024, entry version 128.
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; Pseudomonadota; 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; 272624-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 OrthoDB; 9803125at2; -.
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; Fe,Mn superoxide dismutase (SOD) domain; 1.
DR Gene3D; 3.55.40.20; Iron/manganese superoxide dismutase, C-terminal domain; 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 PANTHER; PTHR42769; SUPEROXIDE DISMUTASE; 1.
DR PANTHER; PTHR42769:SF3; SUPEROXIDE DISMUTASE [FE] 2, CHLOROPLASTIC; 1.
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; SSF54719; Fe,Mn superoxide dismutase (SOD), C-terminal domain; 1.
DR SUPFAM; SSF46609; Fe,Mn superoxide dismutase (SOD), N-terminal domain; 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
//
