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Database: UniProt
Entry: R4R7X5_ENTFL
LinkDB: R4R7X5_ENTFL
Original site: R4R7X5_ENTFL 
ID   R4R7X5_ENTFL            Unreviewed;       120 AA.
AC   R4R7X5;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 25.
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:AGL81769.1};
OS   Enterococcus faecalis (Streptococcus faecalis).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=1351 {ECO:0000313|EMBL:AGL81769.1};
RN   [1] {ECO:0000313|EMBL:AGL81769.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BEACHKN2 {ECO:0000313|EMBL:AGL81767.1}, BWKN1
RC   {ECO:0000313|EMBL:AGL81766.1}, and BWKTN8
RC   {ECO:0000313|EMBL:AGL81769.1};
RA   Dada A.C., Ahmad A., Usup G.;
RT   "Speciation of antibiotic resistant enterococci isolated from recreational
RT   beaches in Malaysia.";
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
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; KC603859; AGL81766.1; -; Genomic_DNA.
DR   EMBL; KC603860; AGL81767.1; -; Genomic_DNA.
DR   EMBL; KC603862; AGL81769.1; -; Genomic_DNA.
DR   AlphaFoldDB; R4R7X5; -.
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; 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   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.
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..57
FT                   /note="Manganese/iron superoxide dismutase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00081"
FT   DOMAIN          64..120
FT                   /note="Manganese/iron superoxide dismutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02777"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AGL81769.1"
FT   NON_TER         120
FT                   /evidence="ECO:0000313|EMBL:AGL81769.1"
SQ   SEQUENCE   120 AA;  12907 MW;  BE591716C00B09E7 CRC64;
     TYVTNLTAAI EKHPELGEKS VEDLISDMNA IPEDIRTAVR NNGGGHANHT FFWEIMAPNA
     GGQPTGAIKE AIDETFGSFD EMKAAFKTAA TGRFGSGWAW LVVNNGKLEI TSTPNQDSPL
//
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