ID   SODF_BORPE              Reviewed;         192 AA.
AC   P37369;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2003, sequence version 2.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Superoxide dismutase [Fe];
DE            EC=1.15.1.1;
GN   Name=sodB; OrderedLocusNames=BP2761;
OS   Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257313;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BP504;
RX   PubMed=8181762; DOI=10.1016/0378-1119(94)90359-x;
RA   Deshazer D., Bannan J.D., Moran M.J., Friedman R.L.;
RT   "Characterization of the gene encoding superoxide dismutase of Bordetella
RT   pertussis and construction of a SOD-deficient mutant.";
RL   Gene 142:85-89(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA   Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA   Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA   Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA   Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA   Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
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; X63055; CAA44779.1; -; Genomic_DNA.
DR   EMBL; M83095; AAC36882.1; -; Unassigned_DNA.
DR   EMBL; BX640419; CAE43036.1; -; Genomic_DNA.
DR   PIR; I40319; I40319.
DR   RefSeq; NP_881365.1; NC_002929.2.
DR   RefSeq; WP_010931119.1; NZ_CP039022.1.
DR   AlphaFoldDB; P37369; -.
DR   SMR; P37369; -.
DR   STRING; 257313.BP2761; -.
DR   GeneID; 45387996; -.
DR   GeneID; 66438258; -.
DR   KEGG; bpe:BP2761; -.
DR   PATRIC; fig|257313.5.peg.2977; -.
DR   eggNOG; COG0605; Bacteria.
DR   HOGENOM; CLU_031625_0_0_4; -.
DR   OMA; KWGSFDK; -.
DR   Proteomes; UP000002676; 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_0000159974"
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"
FT   CONFLICT        43
FT                   /note="I -> V (in Ref. 1; CAA44779/AAC36882)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   192 AA;  21287 MW;  592781D1E384BA5F CRC64;
     MAHTLPPLPY ALDALAPRIS KETLEFHYGK HHQTYVTNLN NLIPGTEFEN LSLEEIVKKS
     SGGVFNNAAQ VWNHTFYWNS LSPNGGGEPS GALADAIKAK WGSVDAFKEA FNKSAAGNFG
     SGWTWLVKKA DGTLDIVNTS NAATPLTTAD KALLTCDVWE HAYYIDYRNA RPKYLENFWA
     LVNWEFAAKN FA