SODM_STAEP
ID SODM_STAEP Reviewed; 199 AA.
AC Q8VQ15; Q54103; Q8VLL5;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Superoxide dismutase [Mn/Fe];
DE EC=1.15.1.1 {ECO:0000305|PubMed:11724835, ECO:0000305|PubMed:11948161};
GN Name=sodA;
OS Staphylococcus epidermidis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1282;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Chiou J., Yang C.-W., Chiou J.-F.;
RT "Cloning, sequencing, and characterization of sodA gene from Staphylococcus
RT epidermidis.";
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-68.
RC STRAIN=BN 280;
RX PubMed=8764488; DOI=10.1111/j.1574-6968.1996.tb08345.x;
RA Heidrich C., Hantke K., Bierbaum G., Sahl H.-G.;
RT "Identification and analysis of a gene encoding a Fur-like protein of
RT Staphylococcus epidermidis.";
RL FEMS Microbiol. Lett. 140:253-259(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 18-160, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 14990 / DSM 20044 / CIP 81.55 / NCTC 11047, NEM2008, NEM2009,
RC and NEM2010;
RX PubMed=11724835; DOI=10.1128/jcm.39.12.4296-4301.2001;
RA Poyart C., Quesne G., Boumaila C., Trieu-Cuot P.;
RT "Rapid and accurate species-level identification of coagulase-negative
RT staphylococci by using the sodA gene as a target.";
RL J. Clin. Microbiol. 39:4296-4301(2001).
RN [4]
RP CATALYTIC ACTIVITY.
RC STRAIN=HAC111, HAC112, HAC113, HAC114, HAC115, HAC33, HAC36, and HAC94;
RX PubMed=11948161; DOI=10.1128/jb.184.9.2465-2472.2002;
RA Wright Valderas M., Gatson J.W., Wreyford N., Hart M.E.;
RT "The superoxide dismutase gene sodM is unique to Staphylococcus aureus:
RT absence of sodM in coagulase-negative staphylococci.";
RL J. Bacteriol. 184:2465-2472(2002).
CC -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC produced within the cells and which are toxic to biological systems.
CC Catalyzes the dismutation of superoxide anion radicals into O2 and H2O2
CC by successive reduction and oxidation of the transition metal ion at
CC the active site. {ECO:0000250|UniProtKB:P80293}.
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:0000305|PubMed:11724835, ECO:0000305|PubMed:11948161};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20697;
CC Evidence={ECO:0000305|PubMed:11724835, ECO:0000305|PubMed:11948161};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P80293};
CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC Evidence={ECO:0000250|UniProtKB:P80293};
CC Note=Binds 1 Mn(2+) or Fe(3+) ion per subunit.
CC {ECO:0000250|UniProtKB:P80293};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; AF462457; AAL68691.1; -; Genomic_DNA.
DR EMBL; X97011; CAA65734.1; -; Genomic_DNA.
DR EMBL; AJ343906; CAC86481.1; -; Genomic_DNA.
DR EMBL; AJ343946; CAC86528.1; -; Genomic_DNA.
DR EMBL; AJ343947; CAC86529.1; -; Genomic_DNA.
DR EMBL; AJ343948; CAC86530.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8VQ15; -.
DR SMR; Q8VQ15; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR Gene3D; 1.10.287.990; -; 1.
DR Gene3D; 3.55.40.20; -; 1.
DR InterPro; IPR001189; Mn/Fe_SOD.
DR InterPro; IPR019833; Mn/Fe_SOD_BS.
DR InterPro; IPR019832; Mn/Fe_SOD_C.
DR InterPro; IPR019831; Mn/Fe_SOD_N.
DR InterPro; IPR036324; Mn/Fe_SOD_N_sf.
DR InterPro; IPR036314; SOD_C_sf.
DR Pfam; PF02777; Sod_Fe_C; 1.
DR Pfam; PF00081; Sod_Fe_N; 1.
DR PIRSF; PIRSF000349; SODismutase; 1.
DR PRINTS; PR01703; MNSODISMTASE.
DR SUPFAM; SSF46609; SSF46609; 1.
DR SUPFAM; SSF54719; SSF54719; 1.
DR PROSITE; PS00088; SOD_MN; 1.
PE 1: Evidence at protein level;
KW Iron; Manganese; Metal-binding; Oxidoreductase; Stress response.
FT CHAIN 1..199
FT /note="Superoxide dismutase [Mn/Fe]"
FT /id="PRO_0000223465"
FT BINDING 27
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000250|UniProtKB:P80293"
FT BINDING 27
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P80293"
FT BINDING 81
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000250|UniProtKB:P80293"
FT BINDING 81
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P80293"
FT BINDING 161
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000250|UniProtKB:P80293"
FT BINDING 161
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P80293"
FT BINDING 165
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000250|UniProtKB:P80293"
FT BINDING 165
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P80293"
FT CONFLICT 12
FT /note="F -> Y (in Ref. 2; CAA65734)"
FT /evidence="ECO:0000305"
FT CONFLICT 22
FT /note="E -> Q (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 41..42
FT /note="AV -> SA (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 66
FT /note="D -> N (in Ref. 3; CAC86481/CAC86528/CAC86529/
FT CAC86530)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="T -> S (in Ref. 3; CAC86481/CAC86528/CAC86529/
FT CAC86530)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="E -> D (in Ref. 3; CAC86481/CAC86528/CAC86529/
FT CAC86530)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="L -> I (in Ref. 3; CAC86481/CAC86528/CAC86529/
FT CAC86530)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 199 AA; 22706 MW; 36B438907574560F CRC64;
MAFELPKLPY AFDALEPHID KETMEIHHDK HHNTYVTKLN AVVEGTDLEA KSIEEIVANL
DSVPSDIQTA VRNNGGGHLN HSLFWELLTP NSEEKGEVVE KIKEQWGSLD EFKKEFADKA
AARFGSGWAW LVVNNGQLEI VTTPNQDNPL TEGKTPILGL DVWEHAYYLK YQNKRPDYIS
AFWNVVNWEK VDELYNAAK
