SODM_LACLM
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 03-AUG-2022, entry version 79.
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; Lactococcus cremoris subsp. cremoris.
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, and
RT 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 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 family.
CC {ECO:0000305}.
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DR EMBL; U17388; AAA85266.1; -; Genomic_DNA.
DR EMBL; AM406671; CAL97033.1; -; Genomic_DNA.
DR RefSeq; WP_003131560.1; NZ_WJVF01000001.1.
DR AlphaFoldDB; P0A4J2; -.
DR SMR; P0A4J2; -.
DR STRING; 416870.llmg_0429; -.
DR EnsemblBacteria; CAL97033; CAL97033; llmg_0429.
DR GeneID; 61108730; -.
DR GeneID; 66441377; -.
DR KEGG; llm:llmg_0429; -.
DR eggNOG; COG0605; Bacteria.
DR HOGENOM; CLU_031625_0_1_9; -.
DR OMA; KWGSFDK; -.
DR PhylomeDB; P0A4J2; -.
DR BioCyc; LLAC416870:LLMG_RS02190-MON; -.
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; 3.55.40.20; -; 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 Manganese; Metal-binding; Oxidoreductase.
FT CHAIN 1..206
FT /note="Superoxide dismutase [Mn]"
FT /id="PRO_0000160041"
FT BINDING 27
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="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