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Database: UniProt/SWISS-PROT
Entry: SODM_STRMU
LinkDB: SODM_STRMU
Original site: SODM_STRMU 
ID   SODM_STRMU              Reviewed;         203 AA.
AC   P09738; Q59791;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   28-MAR-2018, entry version 129.
DE   RecName: Full=Superoxide dismutase [Mn/Fe];
DE            EC=1.15.1.1;
GN   Name=sodA; Synonyms=sod; OrderedLocusNames=SMU_629;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=GS-5;
RX   PubMed=1321118; DOI=10.1128/jb.174.15.4928-4934.1992;
RA   Nakayama K.;
RT   "Nucleotide sequence of Streptococcus mutans superoxide dismutase gene
RT   and isolation of insertion mutants.";
RL   J. Bacteriol. 174:4928-4934(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J.,
RA   Carson M.B., Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P.,
RA   Qian Y., Li S., Zhu H., Najar F.Z., Lai H., White J., Roe B.A.,
RA   Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-23.
RX   PubMed=3722201;
RA   Martin M.E., Byers B.R., Olson M.O.J., Salin M.L., Arceneaux J.E.L.,
RA   Tolbert C.;
RT   "A Streptococcus mutans superoxide dismutase that is active with
RT   either manganese or iron as a cofactor.";
RL   J. Biol. Chem. 261:9361-9367(1986).
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: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
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; D01037; BAB86870.1; -; Genomic_DNA.
DR   EMBL; AE014133; AAN58363.1; -; Genomic_DNA.
DR   PIR; A42710; A42710.
DR   RefSeq; NP_721057.1; NC_004350.2.
DR   RefSeq; WP_002261912.1; NC_004350.2.
DR   PDB; 4YIP; X-ray; 2.15 A; A/B/C/D=1-202.
DR   PDBsum; 4YIP; -.
DR   ProteinModelPortal; P09738; -.
DR   SMR; P09738; -.
DR   STRING; 210007.SMU_629; -.
DR   EnsemblBacteria; AAN58363; AAN58363; SMU_629.
DR   GeneID; 1029605; -.
DR   KEGG; smu:SMU_629; -.
DR   PATRIC; fig|210007.7.peg.555; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   PhylomeDB; P09738; -.
DR   BioCyc; SMUT210007:G1FZX-613-MONOMER; -.
DR   Proteomes; UP000002512; Chromosome.
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; 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   3D-structure; Complete proteome; Direct protein sequencing; Iron;
KW   Manganese; Metal-binding; Oxidoreductase; Reference proteome.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:3722201}.
FT   CHAIN         2    203       Superoxide dismutase [Mn/Fe].
FT                                /FTId=PRO_0000160094.
FT   METAL        27     27       Manganese or iron. {ECO:0000250}.
FT   METAL        81     81       Manganese or iron. {ECO:0000250}.
FT   METAL       163    163       Manganese or iron. {ECO:0000250}.
FT   METAL       167    167       Manganese or iron. {ECO:0000250}.
FT   CONFLICT      4      4       L -> T (in Ref. 3; AA sequence).
FT                                {ECO:0000305}.
FT   TURN         12     18       {ECO:0000244|PDB:4YIP}.
FT   HELIX        21     29       {ECO:0000244|PDB:4YIP}.
FT   HELIX        31     45       {ECO:0000244|PDB:4YIP}.
FT   HELIX        47     49       {ECO:0000244|PDB:4YIP}.
FT   HELIX        53     58       {ECO:0000244|PDB:4YIP}.
FT   HELIX        59     62       {ECO:0000244|PDB:4YIP}.
FT   HELIX        65     87       {ECO:0000244|PDB:4YIP}.
FT   HELIX        97    107       {ECO:0000244|PDB:4YIP}.
FT   HELIX       110    123       {ECO:0000244|PDB:4YIP}.
FT   STRAND      126    134       {ECO:0000244|PDB:4YIP}.
FT   STRAND      140    146       {ECO:0000244|PDB:4YIP}.
FT   HELIX       151    154       {ECO:0000244|PDB:4YIP}.
FT   STRAND      157    163       {ECO:0000244|PDB:4YIP}.
FT   HELIX       166    168       {ECO:0000244|PDB:4YIP}.
FT   HELIX       170    173       {ECO:0000244|PDB:4YIP}.
FT   HELIX       177    184       {ECO:0000244|PDB:4YIP}.
FT   HELIX       185    187       {ECO:0000244|PDB:4YIP}.
FT   HELIX       190    202       {ECO:0000244|PDB:4YIP}.
SQ   SEQUENCE   203 AA;  22626 MW;  CC86C35928C415A6 CRC64;
     MAILLPDLPY AYDALEPYID AETMTLHHDK HHATYVANAN AALEKHPEIG ENLEVLLADV
     EQIPADIRQS LINNGGGHLN HALFWELLSP EKTKVTAEVA AAINEAFGSF DDFKAAFTAA
     ATTRFGSGWA WLVVDKEGKL EVTSTANQDT PISQGLKPIL ALDVWEHAYY LNYRNVRPNY
     IKAFFEVINW NTVARLYAEA LTK
//
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