ID   SODC_PASMU              Reviewed;         186 AA.
AC   Q59689;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 2.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Superoxide dismutase [Cu-Zn];
DE            EC=1.15.1.1;
DE   Flags: Precursor;
GN   Name=sodC; OrderedLocusNames=PM1952;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 87-173.
RC   STRAIN=T5;
RX   PubMed=7496539; DOI=10.1099/13500872-141-9-2271;
RA   Kroll J.S., Langford P.R., Wilks K.E., Keil A.D.;
RT   "Bacterial [Cu,Zn]-superoxide dismutase: phylogenetically distinct from the
RT   eukaryotic enzyme, and not so rare after all!";
RL   Microbiology 141:2271-2279(1995).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems. {ECO:0000250}.
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=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
CC       Note=Binds 1 copper ion per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000305}.
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DR   EMBL; AE004439; AAK04036.1; -; Genomic_DNA.
DR   EMBL; X83124; CAA58205.1; -; Genomic_DNA.
DR   RefSeq; WP_010907421.1; NC_002663.1.
DR   AlphaFoldDB; Q59689; -.
DR   SMR; Q59689; -.
DR   STRING; 747.DR93_2146; -.
DR   EnsemblBacteria; AAK04036; AAK04036; PM1952.
DR   KEGG; pmu:PM1952; -.
DR   PATRIC; fig|272843.6.peg.1976; -.
DR   HOGENOM; CLU_056632_7_1_6; -.
DR   OMA; AQRGFHI; -.
DR   Proteomes; UP000000809; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR   Gene3D; 2.60.40.200; -; 1.
DR   InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR   InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
DR   InterPro; IPR018152; SOD_Cu/Zn_BS.
DR   InterPro; IPR001424; SOD_Cu_Zn_dom.
DR   PANTHER; PTHR10003; PTHR10003; 1.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   SUPFAM; SSF49329; SSF49329; 1.
DR   PROSITE; PS00087; SOD_CU_ZN_1; 1.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE   3: Inferred from homology;
KW   Antioxidant; Copper; Disulfide bond; Metal-binding; Oxidoreductase;
KW   Periplasm; Reference proteome; Signal; Zinc.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..186
FT                   /note="Superoxide dismutase [Cu-Zn]"
FT                   /id="PRO_0000032835"
FT   BINDING         79
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         81
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         104
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         104
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250"
FT   BINDING         113
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250"
FT   BINDING         122
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250"
FT   BINDING         125
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250"
FT   BINDING         160
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   DISULFID        86..182
FT                   /evidence="ECO:0000250"
FT   CONFLICT        130
FT                   /note="A -> V (in Ref. 2; CAA58205)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   186 AA;  19718 MW;  34D702070EE00DDC CRC64;
     MKKTVLALMF SCGMVASAFA HNHAVEHKHT GEMLEVKVEL LDPAKGNQEI GKVVITESAY
     GLVFTPELKN LTAGLHGFHI HQNPSCDAKE KDGKLVAGLA AGGHWDPKNA GKHGYPWSDD
     AHLGDLPALA VNQDGTANNP VLAPRLKHLD DVKGRSLMIH EGGDNHDDHP APLGGGGPRM
     ACGVIK