ID D2BNT9_LACLK Unreviewed; 206 AA.
AC D2BNT9;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Superoxide dismutase {ECO:0000256|ARBA:ARBA00012682, ECO:0000256|RuleBase:RU000414};
DE EC=1.15.1.1 {ECO:0000256|ARBA:ARBA00012682, ECO:0000256|RuleBase:RU000414};
GN Name=sodA {ECO:0000313|EMBL:ADA64228.1};
GN OrderedLocusNames=LLKF_0460 {ECO:0000313|EMBL:ADA64228.1};
OS Lactococcus lactis subsp. lactis (strain KF147).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=684738 {ECO:0000313|EMBL:ADA64228.1, ECO:0000313|Proteomes:UP000001886};
RN [1] {ECO:0000313|EMBL:ADA64228.1, ECO:0000313|Proteomes:UP000001886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KF147 {ECO:0000313|EMBL:ADA64228.1,
RC ECO:0000313|Proteomes:UP000001886};
RX PubMed=18039825; DOI=10.1128/AEM.01850-07;
RA Siezen R.J., Starrenburg M.J., Boekhorst J., Renckens B., Molenaar D.,
RA van Hylckama Vlieg J.E.;
RT "Genome-scale genotype-phenotype matching of two Lactococcus lactis
RT isolates from plants identifies mechanisms of adaptation to the plant
RT niche.";
RL Appl. Environ. Microbiol. 74:424-436(2008).
CC -!- FUNCTION: Destroys radicals which are normally produced within the
CC cells and which are toxic to biological systems.
CC {ECO:0000256|RuleBase:RU000414}.
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:0000256|RuleBase:RU000414};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC {ECO:0000256|ARBA:ARBA00008714, ECO:0000256|RuleBase:RU000414}.
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DR EMBL; CP001834; ADA64228.1; -; Genomic_DNA.
DR RefSeq; WP_003131560.1; NC_013656.1.
DR AlphaFoldDB; D2BNT9; -.
DR SMR; D2BNT9; -.
DR GeneID; 69712452; -.
DR KEGG; llk:LLKF_0460; -.
DR HOGENOM; CLU_031625_0_1_9; -.
DR Proteomes; UP000001886; 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; Fe,Mn superoxide dismutase (SOD) domain; 1.
DR Gene3D; 3.55.40.20; Iron/manganese superoxide dismutase, C-terminal domain; 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 PANTHER; PTHR43595; 37S RIBOSOMAL PROTEIN S26, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43595:SF2; 37S RIBOSOMAL PROTEIN S26, MITOCHONDRIAL; 1.
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; SSF54719; Fe,Mn superoxide dismutase (SOD), C-terminal domain; 1.
DR SUPFAM; SSF46609; Fe,Mn superoxide dismutase (SOD), N-terminal domain; 1.
DR PROSITE; PS00088; SOD_MN; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000349-1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000414}.
FT DOMAIN 3..88
FT /note="Manganese/iron superoxide dismutase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00081"
FT DOMAIN 101..200
FT /note="Manganese/iron superoxide dismutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02777"
FT BINDING 27
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT BINDING 82
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT BINDING 168
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT BINDING 172
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
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
//
