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Database: UniProt/SWISS-PROT
Entry: SODF_SALTY
LinkDB: SODF_SALTY
Original site: SODF_SALTY 
ID   SODF_SALTY              Reviewed;         193 AA.
AC   P0A2F4; P40726;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   13-NOV-2013, entry version 57.
DE   RecName: Full=Superoxide dismutase [Fe];
DE            EC=1.15.1.1;
GN   Name=sodB; OrderedLocusNames=STM1431;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-56.
RC   STRAIN=LT2;
RA   Cheung M.W., Wong K.K., Kwan H.S.;
RT   "Cloning and sequence analysis of Salmonella typhimurium iron
RT   superoxide dismutase promoter.";
RL   Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases.
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: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC   -!- COFACTOR: Binds 1 iron ion per subunit (By similarity).
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family.
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DR   EMBL; AE006468; AAL20353.1; -; Genomic_DNA.
DR   EMBL; U09502; AAA56997.1; -; Unassigned_DNA.
DR   RefSeq; NP_460394.1; NC_003197.1.
DR   ProteinModelPortal; P0A2F4; -.
DR   SMR; P0A2F4; 2-193.
DR   STRING; 99287.STM1431; -.
DR   PaxDb; P0A2F4; -.
DR   PRIDE; P0A2F4; -.
DR   EnsemblBacteria; AAL20353; AAL20353; STM1431.
DR   GeneID; 1252949; -.
DR   KEGG; stm:STM1431; -.
DR   PATRIC; 32381347; VBISalEnt20916_1514.
DR   eggNOG; COG0605; -.
DR   HOGENOM; HOG000013584; -.
DR   KO; K04564; -.
DR   OMA; DYVLERY; -.
DR   OrthoDB; EOG63NMNT; -.
DR   ProtClustDB; PRK10543; -.
DR   BioCyc; SENT99287:GCTI-1441-MONOMER; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006801; P:superoxide metabolic process; IEA:InterPro.
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   PANTHER; PTHR11404; PTHR11404; 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; 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   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    193       Superoxide dismutase [Fe].
FT                                /FTId=PRO_0000159983.
FT   METAL        27     27       Iron (By similarity).
FT   METAL        74     74       Iron (By similarity).
FT   METAL       157    157       Iron (By similarity).
FT   METAL       161    161       Iron (By similarity).
FT   CONFLICT     51     51       K -> E (in Ref. 2; AAA56997).
SQ   SEQUENCE   193 AA;  21308 MW;  6CD35AC8BB3D5117 CRC64;
     MSFELPALPY AKDALAPHIS AETLEYHYGK HHQTYVTNLN NLIKGTAFEG KSLEEIVRTS
     EGGIFNNAAQ VWNHTFYWNC LAPNAGGEPT GKLADAIAAS FGSFAEFKAQ FTDAAIKNFG
     SGWTWLVKSA DGKLAIVSTS NAGTPLTTDA TPLLTVDVWE HAYYIDYRNA RPNYLEHFWA
     LVNWEFVAKN LAA
//
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