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Database: UniProt
Entry: Q838I4
LinkDB: Q838I4
Original site: Q838I4 
ID   SODM_ENTFA              Reviewed;         202 AA.
AC   Q838I4;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   05-DEC-2018, entry version 84.
DE   RecName: Full=Superoxide dismutase [Fe];
DE            EC=1.15.1.1;
GN   Name=sodA; OrderedLocusNames=EF_0463;
OS   Enterococcus faecalis (strain ATCC 700802 / V583).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=226185;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700802 / V583;
RX   PubMed=12663927; DOI=10.1126/science.1080613;
RA   Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA   Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F.,
RA   Tettelin H., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA   Daugherty S.C., DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R.,
RA   Nelson W.C., Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J.,
RA   Khouri H.M., Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A.,
RA   Fraser C.M.;
RT   "Role of mobile DNA in the evolution of vancomycin-resistant
RT   Enterococcus faecalis.";
RL   Science 299:2071-2074(2003).
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=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC       Note=Binds 1 Fe cation per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
DR   EMBL; AE016830; AAO80318.1; -; Genomic_DNA.
DR   RefSeq; NP_814247.1; NC_004668.1.
DR   RefSeq; WP_002387688.1; NZ_KE136524.1.
DR   ProteinModelPortal; Q838I4; -.
DR   SMR; Q838I4; -.
DR   STRING; 226185.EF0463; -.
DR   PRIDE; Q838I4; -.
DR   EnsemblBacteria; AAO80318; AAO80318; EF_0463.
DR   GeneID; 1199378; -.
DR   KEGG; efa:EF0463; -.
DR   PATRIC; fig|226185.45.peg.2872; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   KO; K04564; -.
DR   OMA; YEGWKGE; -.
DR   BioCyc; EFAE226185:G1G0C-466-MONOMER; -.
DR   Proteomes; UP000001415; 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; Iron; Metal-binding; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN         1    202       Superoxide dismutase [Fe].
FT                                /FTId=PRO_0000160037.
FT   METAL        27     27       Iron. {ECO:0000250}.
FT   METAL        82     82       Iron. {ECO:0000250}.
FT   METAL       164    164       Iron. {ECO:0000250}.
FT   METAL       168    168       Iron. {ECO:0000250}.
SQ   SEQUENCE   202 AA;  22697 MW;  E5B16774BD086A3F CRC64;
     MTYTLPELPY AYDALEPYID VETMHLHHDK HHNTYVTNLN AAIEKHPELG EKSVENLISD
     MNAIPEDIRT AVRNNGGGHA NHTFFWEIMA PNAGGQPTGA IKEAIDETFG SFDEMKAAFK
     TAATGRFGSG WAWLVVNNGK LEITSTPNQD SPLMDGQTPV LGLDVWEHAY YLKYKNVRPD
     YIEAFWNVVN WDKVNELFAA AK
//
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