SODC1_SALTY
ID SODC1_SALTY Reviewed; 177 AA.
AC P0CW86; O33803; O50545; P53636;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 65.
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=STM1044;
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].
RX PubMed=9391141; DOI=10.1073/pnas.94.25.13997;
RA De Groote M.A., Ochsner U.A., Shiloh M.U., Nathan C., McCord J.M.,
RA Dinauer M.C., Libby S.J., Vazquez-Torres A., Xu Y., Fang F.C.;
RT "Periplasmic superoxide dismutase protects Salmonella from products of
RT phagocyte NADPH-oxidase and nitric oxide synthase.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:13997-14001(1997).
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).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=10970746; DOI=10.1006/jmbi.2000.4074;
RA Pesce A., Battistoni A., Stroppolo M.E., Polizio F., Nardini M.,
RA Kroll J.S., Langford P.R., O'Neill P., Sette M., Desideri A., Bolognesi M.;
RT "Functional and crystallographic characterization of Salmonella typhimurium
RT Cu,Zn superoxide dismutase coded by the sodCI virulence gene.";
RL J. Mol. Biol. 302:465-478(2000).
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 -!- INTERACTION:
CC P0CW86; P0CW86: sodC1; NbExp=2; IntAct=EBI-6399836, EBI-6399836;
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- MISCELLANEOUS: Encoded by a cryptic bacteriophage.
CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; AF007380; AAB62385.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL19978.1; -; Genomic_DNA.
DR RefSeq; WP_000877926.1; NC_003197.2.
DR PDB; 1EQW; X-ray; 2.30 A; A/B/C/D=22-177.
DR PDB; 6VBS; X-ray; 1.70 A; A/B/C/D/E/F=21-177.
DR PDB; 6VBT; X-ray; 1.70 A; A/B=21-177.
DR PDBsum; 1EQW; -.
DR PDBsum; 6VBS; -.
DR PDBsum; 6VBT; -.
DR AlphaFoldDB; P0CW86; -.
DR SMR; P0CW86; -.
DR STRING; 99287.STM1044; -.
DR PaxDb; P0CW86; -.
DR EnsemblBacteria; AAL19978; AAL19978; STM1044.
DR PATRIC; fig|99287.12.peg.1105; -.
DR HOGENOM; CLU_056632_7_1_6; -.
DR OMA; SIGKIMI; -.
DR PhylomeDB; P0CW86; -.
DR BioCyc; SENT99287:STM1044-MON; -.
DR EvolutionaryTrace; P0CW86; -.
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:0042802; F:identical protein binding; IPI:IntAct.
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 1: Evidence at protein level;
KW 3D-structure; Antioxidant; Copper; Disulfide bond; Metal-binding;
KW Oxidoreductase; Periplasm; Reference proteome; Signal; Zinc.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..177
FT /note="Superoxide dismutase [Cu-Zn] 1"
FT /id="PRO_0000032826"
FT BINDING 69
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT BINDING 71
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT BINDING 94
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT BINDING 150
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT DISULFID 76..172
FT CONFLICT 49
FT /note="P -> T (in Ref. 2; AAB62385)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="M -> T (in Ref. 2; AAB62385)"
FT /evidence="ECO:0000305"
FT STRAND 23..31
FT /evidence="ECO:0007829|PDB:6VBS"
FT STRAND 33..48
FT /evidence="ECO:0007829|PDB:6VBS"
FT STRAND 51..58
FT /evidence="ECO:0007829|PDB:6VBS"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:6VBS"
FT STRAND 68..74
FT /evidence="ECO:0007829|PDB:6VBS"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:6VBS"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:6VBS"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:6VBS"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:6VBS"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:6VBS"
FT HELIX 139..142
FT /evidence="ECO:0007829|PDB:6VBS"
FT STRAND 146..152
FT /evidence="ECO:0007829|PDB:6VBS"
FT STRAND 156..161
FT /evidence="ECO:0007829|PDB:6VBS"
FT HELIX 162..165
FT /evidence="ECO:0007829|PDB:6VBS"
FT STRAND 168..174
FT /evidence="ECO:0007829|PDB:6VBS"
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
