ID   SODC_MYCLE              Reviewed;         240 AA.
AC   Q9CBI6;
DT   30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Superoxide dismutase [Cu-Zn];
DE            EC=1.15.1.1;
DE   Flags: Precursor;
GN   Name=sodC; OrderedLocusNames=ML1925;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems. May play a role in
CC       favoring mycobacterial survival in phagocytes (By similarity).
CC       {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:0000305};
CC       Note=Binds 1 copper ion per subunit. {ECO:0000305};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000305};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Lacks three conserved histidine residues and one conserved
CC       aspartate residue that bind copper and zinc. {ECO:0000305}.
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DR   EMBL; AL583923; CAC30880.1; -; Genomic_DNA.
DR   PIR; H87149; H87149.
DR   RefSeq; NP_302298.1; NC_002677.1.
DR   RefSeq; WP_010908619.1; NC_002677.1.
DR   AlphaFoldDB; Q9CBI6; -.
DR   SMR; Q9CBI6; -.
DR   STRING; 272631.ML1925; -.
DR   EnsemblBacteria; CAC30880; CAC30880; CAC30880.
DR   KEGG; mle:ML1925; -.
DR   PATRIC; fig|272631.5.peg.3645; -.
DR   Leproma; ML1925; -.
DR   eggNOG; COG2032; Bacteria.
DR   HOGENOM; CLU_056632_8_0_11; -.
DR   OMA; HADADNF; -.
DR   Proteomes; UP000000806; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; 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   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; PS51257; PROKAR_LIPOPROTEIN; 1.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE   3: Inferred from homology;
KW   Antioxidant; Cell membrane; Copper; Disulfide bond; Lipoprotein; Membrane;
KW   Metal-binding; Oxidoreductase; Palmitate; Reference proteome; Signal; Zinc.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           33..240
FT                   /note="Superoxide dismutase [Cu-Zn]"
FT                   /id="PRO_0000032838"
FT   BINDING         116
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         118
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         195
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   LIPID           33
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           33
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   DISULFID        123..234
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   240 AA;  24087 MW;  F042C680D80799DD CRC64;
     MSKLAGHRNV AAVTRSALSL SFVAACVALL SACIQNQPPA TLPGTTPTVW TGSPAPSGML
     GAEAESMGPP NIITRLNAPD GTQVATAKFE FNNGFATITI ATTGVGHLAP GFHGVHIHKV
     GKCEPSSAGP TGGAPGDFLS AGGHFQVPGH TVEPASGNLT SLQVRKDGIG TLVTTTDAFT
     MNDLLAGQKT AIIIHAGADN FGNIPPERYS QVNGTPGPDA TTISTGDAGK RVACGVIGAD