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Database: UniProt
Entry: P0A4J2
LinkDB: P0A4J2
Original site: P0A4J2 
ID   SODM_LACLM              Reviewed;         206 AA.
AC   P0A4J2; A2RID8; P50911;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   05-DEC-2018, entry version 66.
DE   RecName: Full=Superoxide dismutase [Mn];
DE            EC=1.15.1.1;
GN   Name=sodA; OrderedLocusNames=llmg_0429;
OS   Lactococcus lactis subsp. cremoris (strain MG1363).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=416870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7665513; DOI=10.1128/jb.177.18.5254-5260.1995;
RA   Sanders J.W., Leenhouts K.J., Haandrikman A.J., Venema G., Kok J.;
RT   "Stress response in Lactococcus lactis: cloning, expression analysis,
RT   and mutation of the lactococcal superoxide dismutase gene.";
RL   J. Bacteriol. 177:5254-5260(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MG1363;
RX   PubMed=17307855; DOI=10.1128/JB.01768-06;
RA   Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA   Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA   van Sinderen D., Kok J.;
RT   "The complete genome sequence of the lactic acid bacterial paradigm
RT   Lactococcus lactis subsp. cremoris MG1363.";
RL   J. Bacteriol. 189:3256-3270(2007).
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       Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
DR   EMBL; U17388; AAA85266.1; -; Genomic_DNA.
DR   EMBL; AM406671; CAL97033.1; -; Genomic_DNA.
DR   RefSeq; WP_003131560.1; NC_009004.1.
DR   ProteinModelPortal; P0A4J2; -.
DR   SMR; P0A4J2; -.
DR   STRING; 416870.llmg_0429; -.
DR   EnsemblBacteria; CAL97033; CAL97033; llmg_0429.
DR   KEGG; llm:llmg_0429; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013583; -.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   BioCyc; LLAC416870:LLMG_RS02190-MONOMER; -.
DR   Proteomes; UP000000364; 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   3: Inferred from homology;
KW   Complete proteome; Manganese; Metal-binding; Oxidoreductase.
FT   CHAIN         1    206       Superoxide dismutase [Mn].
FT                                /FTId=PRO_0000160041.
FT   METAL        27     27       Manganese. {ECO:0000250}.
FT   METAL        82     82       Manganese. {ECO:0000250}.
FT   METAL       168    168       Manganese. {ECO:0000250}.
FT   METAL       172    172       Manganese. {ECO:0000250}.
SQ   SEQUENCE   206 AA;  23254 MW;  2865BB33801DB644 CRC64;
     MAFTLPELPY APNALEPFFD EATMRLHHGK HHQTYVNNLN AAIEKHNELD DLSLEELLTD
     LSAIPEDIRT AVRNNGGGHL NHSQFWLWLR PNTDGSENHA DGEIGDAIAK EFGSFETFKT
     EFKAAATGRF GSGWAWLVVD EAGKLKVVST ANQDNPISEG LTPVLGLDVW EHAYYLKYHN
     VRPDYIEAFF NLVNWDKVNE LYAKAK
//
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