SODC1_SALT4
ID SODC1_SALT4 Reviewed; 177 AA.
AC E8XDJ8; O33803; O50545; P53636;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Superoxide dismutase [Cu-Zn] 1;
DE EC=1.15.1.1;
DE AltName: Full=sodCI;
DE Flags: Precursor;
GN Name=sodC1; Synonyms=sodC; OrderedLocusNames=STM474_1035;
OS Salmonella typhimurium (strain 4/74).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=909946;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=4/74;
RX PubMed=9379906; DOI=10.1046/j.1365-2958.1997.5151877.x;
RA Farrant J.L., Sansone A., Canvin J.R., Pallen M.J., Langford P.R.,
RA Wallis T.S., Dougan G., Kroll J.S.;
RT "Bacterial copper- and zinc-cofactored superoxide dismutase contributes to
RT the pathogenesis of systemic salmonellosis.";
RL Mol. Microbiol. 25:785-796(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4/74;
RX PubMed=21478351; DOI=10.1128/jb.00394-11;
RA Richardson E.J., Limaye B., Inamdar H., Datta A., Manjari K.S.,
RA Pullinger G.D., Thomson N.R., Joshi R.R., Watson M., Stevens M.P.;
RT "Genome sequences of Salmonella enterica serovar typhimurium, Choleraesuis,
RT Dublin, and Gallinarum strains of well- defined virulence in food-producing
RT animals.";
RL J. Bacteriol. 193:3162-3163(2011).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 77-163.
RC STRAIN=4/74;
RX PubMed=8869506; DOI=10.1111/j.1574-6968.1996.tb08052.x;
RA Canvin J., Langford P.R., Wilks K.E., Kroll J.S.;
RT "Identification of sodC encoding periplasmic [Cu,Zn]-superoxide dismutase
RT in Salmonella.";
RL FEMS Microbiol. Lett. 136:215-220(1996).
CC -!- FUNCTION: Destroys radicals which are normally produced within the
CC 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=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Note=Binds 1 copper ion per subunit.;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 1 zinc ion per subunit.;
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- MISCELLANEOUS: Encoded by a cryptic bacteriophage.
CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Y13121; CAA73588.1; -; Genomic_DNA.
DR EMBL; CP002487; ADX16741.1; -; Genomic_DNA.
DR EMBL; X94327; CAA63988.1; -; Genomic_DNA.
DR RefSeq; WP_000877926.1; NC_016857.1.
DR PDB; 6D52; X-ray; 1.60 A; A/B/C/D=21-177.
DR PDBsum; 6D52; -.
DR AlphaFoldDB; E8XDJ8; -.
DR SMR; E8XDJ8; -.
DR EnsemblBacteria; ADX16741; ADX16741; STM474_1035.
DR KEGG; seb:STM474_1035; -.
DR PATRIC; fig|909946.3.peg.1066; -.
DR HOGENOM; CLU_056632_7_1_6; -.
DR OMA; SIGKIMI; -.
DR Proteomes; UP000008978; 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; PS00332; SOD_CU_ZN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antioxidant; Copper; Disulfide bond; Metal-binding;
KW Oxidoreductase; Periplasm; Signal; Zinc.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..177
FT /note="Superoxide dismutase [Cu-Zn] 1"
FT /id="PRO_0000408966"
FT BINDING 69
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 71
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 94
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 103
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 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 150
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT DISULFID 76..172
FT /evidence="ECO:0000250"
FT CONFLICT 148
FT /note="M -> T (in Ref. 3; CAA63988)"
FT /evidence="ECO:0000305"
FT STRAND 23..32
FT /evidence="ECO:0007829|PDB:6D52"
FT STRAND 35..48
FT /evidence="ECO:0007829|PDB:6D52"
FT STRAND 51..58
FT /evidence="ECO:0007829|PDB:6D52"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:6D52"
FT STRAND 68..74
FT /evidence="ECO:0007829|PDB:6D52"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:6D52"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:6D52"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:6D52"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:6D52"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:6D52"
FT HELIX 139..142
FT /evidence="ECO:0007829|PDB:6D52"
FT STRAND 145..152
FT /evidence="ECO:0007829|PDB:6D52"
FT STRAND 156..161
FT /evidence="ECO:0007829|PDB:6D52"
FT HELIX 162..165
FT /evidence="ECO:0007829|PDB:6D52"
FT STRAND 168..175
FT /evidence="ECO:0007829|PDB:6D52"
SQ SEQUENCE 177 AA; 18370 MW; 1EC743EE2AB38CAE CRC64;
MKYTILSLVA GALISCSAMA ENTLTVKMND ALSSGTGENI GEITVSETPY GLLFTPHLNG
LTPGIHGFHV HTNPSCMPGM KDGKEVPALM AGGHLDPEKT GKHLGPYNDK GHLGDLPGLV
VNADGTATYP LLAPRLKSLS ELKGHSLMIH KGGDNYSDKP APLGGGGARF ACGVIEK
