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Database: UniProt
Entry: O54263
LinkDB: O54263
Original site: O54263 
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   05-DEC-2018, entry version 80.
DE   RecName: Full=Superoxide dismutase [Mn/Fe];
DE            EC=1.15.1.1;
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,
RC   ATCC 35037 / CIP 102922 / DSM 20627 / LMG 14532 / NCTC 11427, and
RC   NEM1121;
RX   PubMed=9431917;
RA   Poyart C., Quesne G., Coulon S., Berche P., Trieu-Cuot P.;
RT   "Identification of streptococci to species level by sequencing the
RT   gene 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
CC       systems.
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   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC       Note=Binds 1 Mn(2+) or Fe(2+) ion per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
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   ProteinModelPortal; O54263; -.
DR   SMR; O54263; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
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; 2.40.500.20; -; 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       Superoxide dismutase [Mn/Fe].
FT                                /FTId=PRO_0000160095.
FT   METAL        10     10       Manganese or iron. {ECO:0000250}.
FT   METAL        64     64       Manganese or iron. {ECO:0000250}.
FT   VARIANT      17     17       A -> T (in strain: CIP 103216).
FT   VARIANT      32     32       I -> T (in strain: CIP 102922T).
FT   VARIANT      44     44       E -> D (in strain: CIP 102922T).
FT   VARIANT     113    113       A -> V (in strain: NEM1121).
FT   VARIANT     129    129       A -> T (in strain: CIP 103216).
FT   VARIANT     138    138       G -> S (in strain: NEM1121).
FT   NON_TER       1      1
FT   NON_TER     145    145
SQ   SEQUENCE   145 AA;  15700 MW;  9480B0F96901BED6 CRC64;
     YIDAETMHLH HDKHHQAYVN NANAALEKHP EIGEDLEALL ADVESIPADI RQALINNGGG
     HLNHALFWEL MTPEKTAPSA ELAAAIDATF GSFEEFQAAF TAAATTRFGS GWAWLVVNKE
     GKLEVTSTAN QDTPISEGKK PILGL
//
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