SODM_STRAY
ID SODM_STRAY Reviewed; 145 AA.
AC O33605;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 79.
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 alactolyticus.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=29389;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43077 / CIP 103244 / DSM 20728 / LMG 14808 / NCIMB 701091;
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; Z95894; CAB09347.1; -; Genomic_DNA.
DR AlphaFoldDB; O33605; -.
DR SMR; O33605; -.
DR PRIDE; O33605; -.
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_0000160089"
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 NON_TER 1
FT NON_TER 145
SQ SEQUENCE 145 AA; 16107 MW; 495EB5685AB3B815 CRC64;
YIDKETMILH HDKHHATYLA NANAALEKHP EIGEDLEFLL SDVTRIPEDI RQALINNGGG
HLNHALFWEL LTPEKQEPTA EVLAAIEDAF GSFEDFKTAF TQAATTRFGS GWAWLVVNQE
GKLEVMSTGN QDNPISQGKQ PILGL
