SODM_STRMT
ID SODM_STRMT Reviewed; 145 AA.
AC O33686; O54253; O54254;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 85.
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 mitis.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=28037;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 49456 / DSM 12643 / LMG 14557 / NCTC 12261, NEM1126, and
RC NEM1222;
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; Z95909; CAB09362.1; -; Genomic_DNA.
DR EMBL; Z99191; CAB16335.1; -; Genomic_DNA.
DR EMBL; Z99192; CAB16336.1; -; Genomic_DNA.
DR AlphaFoldDB; O33686; -.
DR SMR; O33686; -.
DR STRING; 585202.SMSK321_0264; -.
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_0000160093"
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 48
FT /note="A -> T (in strain: NEM1126)"
FT VARIANT 95
FT /note="E -> D (in strain: NEM1126)"
FT VARIANT 98
FT /note="A -> T (in strain: NEM1222)"
FT NON_TER 1
FT NON_TER 145
SQ SEQUENCE 145 AA; 15731 MW; 98F1AC896901A2A6 CRC64;
YIDAETMHLH HDKHHQTYVN NANAALEKHP EIGEDLEALL ADVESIPADI RQALINNGGG
HLNHALFWEL MTPEKTAPSA ELAAAIDATF GSFEEFQAAF TAAATTRFGS GWAWLVVNKE
GKLEVTSTAN QDTPISEGKK PILGL
