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Database: UniProt
Entry: B5KMU8_9ENTE
LinkDB: B5KMU8_9ENTE
Original site: B5KMU8_9ENTE 
ID   B5KMU8_9ENTE            Unreviewed;       100 AA.
AC   B5KMU8;
DT   14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2008, sequence version 1.
DT   24-JAN-2024, entry version 30.
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};
DE   Flags: Fragment;
GN   Name=sodA {ECO:0000313|EMBL:ABW77426.1};
OS   Enterococcus haemoperoxidus.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=155618 {ECO:0000313|EMBL:ABW77426.1};
RN   [1] {ECO:0000313|EMBL:ABW77426.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=LMG 19487 {ECO:0000313|EMBL:ABW77426.1};
RX   PubMed=18558446; DOI=10.1016/j.mimet.2008.05.005;
RA   Martin B., Garriga M., Aymerich T.;
RT   "Identification of Enterococcus species by melting curve analysis of
RT   restriction fragments.";
RL   J. Microbiol. Methods 75:145-147(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   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC       {ECO:0000256|ARBA:ARBA00008714, ECO:0000256|RuleBase:RU000414}.
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DR   EMBL; EU089799; ABW77426.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5KMU8; -.
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; 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   SUPFAM; SSF54719; Fe,Mn superoxide dismutase (SOD), C-terminal domain; 1.
DR   SUPFAM; SSF46609; Fe,Mn superoxide dismutase (SOD), N-terminal domain; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000414}.
FT   DOMAIN          1..63
FT                   /note="Manganese/iron superoxide dismutase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00081"
FT   DOMAIN          70..100
FT                   /note="Manganese/iron superoxide dismutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02777"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ABW77426.1"
FT   NON_TER         100
FT                   /evidence="ECO:0000313|EMBL:ABW77426.1"
SQ   SEQUENCE   100 AA;  10850 MW;  5829C2268711D688 CRC64;
     HDKHHNTYVT NLNAAIDKHP ELGTKSVEDL IADMDSIPED IRTAVRNNGG GHANHSFFWE
     IMAPNAGGAP TGDIKDAIDA TFGSFDKLKE EFKAAATGRF
//
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