SODC_SALTY
ID SODC_SALTY Reviewed; 173 AA.
AC O68901;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Superoxide dismutase [Cu-Zn] 2;
DE EC=1.15.1.1;
DE AltName: Full=SodCII;
DE Flags: Precursor;
GN Name=sodC; Synonyms=sodC2; OrderedLocusNames=STM1440;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 14028s / SGSG 2262;
RX PubMed=10377444; DOI=10.1073/pnas.96.13.7502;
RA Fang F.C., DeGroote M.A., Foster J.W., Baumler A.J., Ochsner U.,
RA Testerman T., Bearson S., Giard J.-C., Xu Y., Campbell G., Laessig T.;
RT "Virulent Salmonella typhimurium has two periplasmic Cu,Zn-superoxide
RT dismutases.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:7502-7507(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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: Monomer. {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; AF056931; AAC13559.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20362.1; -; Genomic_DNA.
DR RefSeq; NP_460403.1; NC_003197.2.
DR RefSeq; WP_000826819.1; NC_003197.2.
DR AlphaFoldDB; O68901; -.
DR BMRB; O68901; -.
DR SMR; O68901; -.
DR STRING; 99287.STM1440; -.
DR PaxDb; O68901; -.
DR EnsemblBacteria; AAL20362; AAL20362; STM1440.
DR GeneID; 1252958; -.
DR KEGG; stm:STM1440; -.
DR PATRIC; fig|99287.12.peg.1523; -.
DR HOGENOM; CLU_056632_7_1_6; -.
DR OMA; EHGFNNP; -.
DR PhylomeDB; O68901; -.
DR BioCyc; SENT99287:STM1440-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IBA:GO_Central.
DR GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR GO; GO:0004784; F:superoxide dismutase activity; IBA:GO_Central.
DR GO; GO:0019430; P:removal of superoxide radicals; IBA:GO_Central.
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; 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..19
FT /evidence="ECO:0000250"
FT CHAIN 20..173
FT /note="Superoxide dismutase [Cu-Zn] 2"
FT /id="PRO_0000032825"
FT BINDING 67
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 147
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT DISULFID 74..169
FT /evidence="ECO:0000250"
SQ SEQUENCE 173 AA; 17737 MW; 5FDCF9F6EF64B3EF CRC64;
MKRLSLAMVT LLACAGAQAA SEKVEMNLVT AQGVGQSIGT VVIDETEGGL KFTPHLKALP
PGEHGFHIHA NGSCQPAIKD GKAVAAEAAG GHLDPQNTGK HEGPEGQGHL GDLPVLVVNN
DGIASEPVTA PRLKSLDEVK DKALMIHVGG DNMSDQPKPL GGGGMRYACG VIK
