ID   SODF_CAMJE              Reviewed;         220 AA.
AC   Q0PBW9; P53640;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Superoxide dismutase [Fe];
DE            EC=1.15.1.1;
GN   Name=sodB; OrderedLocusNames=Cj0169;
OS   Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS   11168).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=192222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 33560 / CIP 702 / DSM 4688 / NCTC 11351;
RX   PubMed=8025686; DOI=10.1099/13500872-140-5-1203;
RA   Purdy D., Park S.F.;
RT   "Cloning, nucleotide sequence and characterization of a gene encoding
RT   superoxide dismutase from Campylobacter jejuni and Campylobacter coli.";
RL   Microbiology 140:1203-1208(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700819 / NCTC 11168;
RX   PubMed=10688204; DOI=10.1038/35001088;
RA   Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA   Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA   Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA   Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA   Barrell B.G.;
RT   "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT   reveals hypervariable sequences.";
RL   Nature 403:665-668(2000).
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. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC       {ECO:0000305}.
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DR   EMBL; X76692; CAA54123.1; -; Genomic_DNA.
DR   EMBL; AL111168; CAL34339.1; -; Genomic_DNA.
DR   PIR; H81434; H81434.
DR   RefSeq; WP_002851662.1; NC_002163.1.
DR   RefSeq; YP_002343628.1; NC_002163.1.
DR   AlphaFoldDB; Q0PBW9; -.
DR   SMR; Q0PBW9; -.
DR   IntAct; Q0PBW9; 7.
DR   STRING; 192222.Cj0169; -.
DR   PaxDb; Q0PBW9; -.
DR   PRIDE; Q0PBW9; -.
DR   EnsemblBacteria; CAL34339; CAL34339; Cj0169.
DR   GeneID; 904414; -.
DR   KEGG; cje:Cj0169; -.
DR   PATRIC; fig|192222.6.peg.166; -.
DR   eggNOG; COG0605; Bacteria.
DR   HOGENOM; CLU_031625_0_0_7; -.
DR   OMA; KWGSFDK; -.
DR   Proteomes; UP000000799; 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..220
FT                   /note="Superoxide dismutase [Fe]"
FT                   /id="PRO_0000159976"
FT   BINDING         26
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         73
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         164
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         168
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        153
FT                   /note="I -> N (in Ref. 1; CAA54123)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        218
FT                   /note="P -> S (in Ref. 1; CAA54123)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   220 AA;  24813 MW;  1E0BE7150960D017 CRC64;
     MFELRKLPYD TNAFGDFLSA ETFSYHHGKH HNTYVTNLNN LIKDTEFAGK DLVSIIKTSN
     GGVFNNAAQV YNHDFYFDCI KPSTGCGCGG SCQSIDANLQ AALEKEFGSL ENFKAEFIKG
     ATGVFGSGWF WLVYNTKNQK LEFVGTSNAA TPITEDKVPL LVVDVWEHAY YVDHRNARPA
     YLEKFYAHIN WEFVAKAYEW ALKEGMGSVS FYANELHPVK