SODM_STROR
ID SODM_STROR Reviewed; 145 AA.
AC O54263; O33693; O33694;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Superoxide dismutase [Mn/Fe];
DE EC=1.15.1.1 {ECO:0000250|UniProtKB:P80293};
DE Flags: Fragment;
GN Name=sodA;
OS Streptococcus oralis.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 10557 / CIP 103216 / LMG 14533 / NCTC 7864 / SK 2,
RC ATCC 35037 / CIP 102922 / DSM 20627 / KCTC 13048 / LMG 14532 / NCTC 11427 /
RC PB182, and NEM1121;
RX PubMed=9431917; DOI=10.1128/jcm.36.1.41-47.1998;
RA Poyart C., Quesne G., Coulon S., Berche P., Trieu-Cuot P.;
RT "Identification of streptococci to species level by sequencing the gene
RT encoding the manganese-dependent superoxide dismutase.";
RL J. Clin. Microbiol. 36:41-47(1998).
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:0000250|UniProtKB:P80293};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20697;
CC Evidence={ECO:0000250|UniProtKB:P80293};
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 -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; Z99195; CAB16339.1; -; Genomic_DNA.
DR EMBL; Z95912; CAB09365.1; -; Genomic_DNA.
DR EMBL; Z99194; CAB16338.1; -; Genomic_DNA.
DR EMBL; Z95911; CAB09364.1; -; Genomic_DNA.
DR AlphaFoldDB; O54263; -.
DR SMR; O54263; -.
DR STRING; 1303.SORDD17_01437; -.
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; 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 PRINTS; PR01703; MNSODISMTASE.
DR SUPFAM; SSF46609; SSF46609; 1.
DR SUPFAM; SSF54719; SSF54719; 1.
PE 3: Inferred from homology;
KW Iron; Manganese; Metal-binding; Oxidoreductase.
FT CHAIN <1..>145
FT /note="Superoxide dismutase [Mn/Fe]"
FT /id="PRO_0000160095"
FT REGION 126..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 10
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000250|UniProtKB:P80293"
FT BINDING 10
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P80293"
FT BINDING 64
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000250|UniProtKB:P80293"
FT BINDING 64
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P80293"
FT VARIANT 17
FT /note="A -> T (in strain: CIP 103216)"
FT VARIANT 32
FT /note="I -> T (in strain: CIP 102922T)"
FT VARIANT 44
FT /note="E -> D (in strain: CIP 102922T)"
FT VARIANT 113
FT /note="A -> V (in strain: NEM1121)"
FT VARIANT 129
FT /note="A -> T (in strain: CIP 103216)"
FT VARIANT 138
FT /note="G -> S (in strain: NEM1121)"
FT NON_TER 1
FT NON_TER 145
SQ SEQUENCE 145 AA; 15700 MW; 9480B0F96901BED6 CRC64;
YIDAETMHLH HDKHHQAYVN NANAALEKHP EIGEDLEALL ADVESIPADI RQALINNGGG
HLNHALFWEL MTPEKTAPSA ELAAAIDATF GSFEEFQAAF TAAATTRFGS GWAWLVVNKE
GKLEVTSTAN QDTPISEGKK PILGL