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 01-MAY-2013, entry version 54.
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; NCMAPNG; -.
DR ProtClustDB; PRK10543; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004784; F:superoxide dismutase activity; IEA: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; SODismutase; 1.
DR SUPFAM; SSF54719; SODismutase; 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
//