SODM_CUPMC
ID SODM_CUPMC Reviewed; 197 AA.
AC P17550; Q5NUZ9; Q93JN0;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2002, sequence version 3.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Superoxide dismutase [Fe];
DE EC=1.15.1.1 {ECO:0000269|PubMed:12471500};
GN Name=chrC {ECO:0000303|PubMed:12471500}; OrderedLocusNames=Rmet_6201;
GN ORFNames=RMe0091;
OS Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS CH34) (Ralstonia metallidurans).
OG Plasmid pMOL28.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=266264;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUGGESTION
RP OF METAL-BINDING, SUBUNIT, AND INDUCTION.
RC STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34;
RX PubMed=12471500; DOI=10.1007/s00203-002-0492-5;
RA Juhnke S., Peitzsch N., Huebener N., Grosse C., Nies D.H.;
RT "New genes involved in chromate resistance in Ralstonia metallidurans
RT strain CH34.";
RL Arch. Microbiol. 179:15-25(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-69.
RX PubMed=2180932; DOI=10.1016/s0021-9258(19)39411-6;
RA Nies A., Nies D.H., Silver S.;
RT "Nucleotide sequence and expression of a plasmid-encoded chromate
RT resistance determinant from Alcaligenes eutrophus.";
RL J. Biol. Chem. 265:5648-5653(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA van der Lelie D., Monchy S., Taghavi S., McCorkle S., Dunn J.,
RA Benotmane M., Vallaeys T., Lapidus A., Mergeay M.;
RT "Sequence and features of the Ralstonia metallidurans CH34 heavy metal
RT plasmids pMOL28 and pMOL30.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34;
RX PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT master survivalist in harsh and anthropogenic environments.";
RL PLoS ONE 5:E10433-E10433(2010).
CC -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC produced within the cells and which are toxic to biological systems.
CC {ECO:0000305|PubMed:12471500}.
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 Evidence={ECO:0000269|PubMed:12471500};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000305|PubMed:12471500};
CC Note=Binds 1 Fe cation per subunit. {ECO:0000250|UniProtKB:Q9X6W9};
CC -!- SUBUNIT: Homotetramer. {ECO:0000305|PubMed:12471500}.
CC -!- INDUCTION: By chromate; induction increases when cells are grown in the
CC presence of high sulfate concentrations (3 mM NaSO4(2-)).
CC {ECO:0000269|PubMed:12471500}.
CC -!- MISCELLANEOUS: This protein is not essential for chromate resistance,
CC however it may contribute to resistance under certain environmental
CC conditions. {ECO:0000305|PubMed:12471500}.
CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; X90708; CAI30235.1; -; Genomic_DNA.
DR EMBL; CP000355; ABF13060.1; -; Genomic_DNA.
DR EMBL; AJ313327; CAC42412.1; -; Genomic_DNA.
DR PIR; C35177; C35177.
DR RefSeq; WP_011239974.1; NC_007972.2.
DR RefSeq; YP_161713.1; NC_006525.1.
DR AlphaFoldDB; P17550; -.
DR SMR; P17550; -.
DR EnsemblBacteria; ABF13060; ABF13060; Rmet_6201.
DR GeneID; 60825782; -.
DR KEGG; rme:Rmet_6201; -.
DR HOGENOM; CLU_031625_2_2_4; -.
DR OMA; DHHGNVG; -.
DR OrthoDB; 1440645at2; -.
DR Proteomes; UP000002429; Plasmid pMOL28.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004784; F:superoxide dismutase activity; IDA:CACAO.
DR GO; GO:0046687; P:response to chromate; IEA:UniProtKB-KW.
DR Gene3D; 3.55.40.20; -; 1.
DR InterPro; IPR001189; Mn/Fe_SOD.
DR InterPro; IPR019832; Mn/Fe_SOD_C.
DR InterPro; IPR036324; Mn/Fe_SOD_N_sf.
DR InterPro; IPR036314; SOD_C_sf.
DR Pfam; PF02777; Sod_Fe_C; 1.
DR PIRSF; PIRSF000349; SODismutase; 1.
DR SUPFAM; SSF46609; SSF46609; 1.
DR SUPFAM; SSF54719; SSF54719; 1.
PE 1: Evidence at protein level;
KW Chromate resistance; Iron; Metal-binding; Oxidoreductase; Plasmid;
KW Reference proteome.
FT CHAIN 1..197
FT /note="Superoxide dismutase [Fe]"
FT /id="PRO_0000160011"
FT BINDING 26
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q9X6W9"
FT BINDING 75
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q9X6W9"
FT BINDING 157
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q9X6W9"
FT BINDING 161
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q9X6W9"
SQ SEQUENCE 197 AA; 21565 MW; D0F101A425DA38BD CRC64;
MLYEMKPLGC EPAKLTGLSE KLIFSHYENN YGGAVKRLNA ITATLAELDM ATAPVFTLNG
LKREELIATN SMILHEVYFD SLGDGGSLDG ALKTAIERDF GSVERWQAEF TAMGKALGGG
SGWVLLTYSP RDGRLVNQWA SDHAHTLAGG TPVLALDMYE HSYHMDYGAK AAAYVDAFMQ
NIHWQRAATR FAAAVRD
