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Database: UniProt
Entry: P43019
LinkDB: P43019
Original site: P43019 
ID   SODM_SALTY              Reviewed;         206 AA.
AC   P43019;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   05-DEC-2018, entry version 120.
DE   RecName: Full=Superoxide dismutase [Mn];
DE            EC=1.15.1.1;
GN   Name=sodA; OrderedLocusNames=STM4055;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 14028 / SGSG 2980 / CDC 6516-60 / NCTC 12023;
RX   PubMed=7729880;
RA   Tsolis R.M., Baumler A.J., Heffron F.;
RT   "Role of Salmonella typhimurium Mn-superoxide dismutase (SodA) in
RT   protection against early killing by J774 macrophages.";
RL   Infect. Immun. 63:1739-1744(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M.,
RA   Waterston R., Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium
RT   LT2.";
RL   Nature 413:852-856(2001).
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=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
DR   EMBL; U20645; AAC43331.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL22895.1; -; Genomic_DNA.
DR   RefSeq; NP_462936.1; NC_003197.2.
DR   RefSeq; WP_000122635.1; NC_003197.2.
DR   ProteinModelPortal; P43019; -.
DR   SMR; P43019; -.
DR   STRING; 99287.STM4055; -.
DR   PaxDb; P43019; -.
DR   PRIDE; P43019; -.
DR   EnsemblBacteria; AAL22895; AAL22895; STM4055.
DR   GeneID; 1255582; -.
DR   KEGG; stm:STM4055; -.
DR   PATRIC; fig|99287.12.peg.4275; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013583; -.
DR   KO; K04564; -.
DR   OMA; YEGWKGE; -.
DR   PhylomeDB; P43019; -.
DR   BioCyc; SENT99287:STM4055-MONOMER; -.
DR   Proteomes; UP000001014; 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; Manganese; Metal-binding; Oxidoreductase;
KW   Reference proteome.
FT   INIT_MET      1      1       Removed. {ECO:0000250}.
FT   CHAIN         2    206       Superoxide dismutase [Mn].
FT                                /FTId=PRO_0000160033.
FT   METAL        27     27       Manganese. {ECO:0000250}.
FT   METAL        82     82       Manganese. {ECO:0000250}.
FT   METAL       168    168       Manganese. {ECO:0000250}.
FT   METAL       172    172       Manganese. {ECO:0000250}.
FT   CONFLICT     91     91       K -> T (in Ref. 1; AAC43331).
FT                                {ECO:0000305}.
FT   CONFLICT    204    205       AK -> L (in Ref. 1). {ECO:0000305}.
SQ   SEQUENCE   206 AA;  23079 MW;  BFB2AD228267FD3C CRC64;
     MSYTLPSLPY AYDALEPHFD KQTMEIHHTK HHQTYVNNAN AALENLPEFA SLPVEELITK
     LDQVPADKKT VLRNNAGGHA NHSLFWKGLK KGTTLQGDLK AAIERDFGSV DNFKAEFEKA
     AATRFGSGWA WLVLKGDKLA VVSTANQDSP LMGEAISGAS GFPILGLDVW EHAYYLKFQN
     RRPDYIKEFW NVVNWDEAAA RFAAKK
//
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