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Database: UniProt/SWISS-PROT
Entry: SODF_ECOLI
LinkDB: SODF_ECOLI
Original site: SODF_ECOLI 
ID   SODF_ECOLI              Reviewed;         193 AA.
AC   P0AGD3; P09157;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   28-MAR-2018, entry version 103.
DE   RecName: Full=Superoxide dismutase [Fe];
DE            EC=1.15.1.1;
GN   Name=sodB; OrderedLocusNames=b1656, JW1648;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=K12;
RX   PubMed=2447093;
RA   Carlioz A., Ludwig M.L., Stallings W.C., Fee J.A., Steinman H.M.,
RA   Touati D.;
RT   "Iron superoxide dismutase. Nucleotide sequence of the gene from
RT   Escherichia coli K12 and correlations with crystal structures.";
RL   J. Biol. Chem. 263:1555-1562(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA   Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA   Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M.,
RA   Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K.,
RA   Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N.,
RA   Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J.,
RA   Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.;
RT   "A 570-kb DNA sequence of the Escherichia coli K-12 genome
RT   corresponding to the 28.0-40.1 min region on the linkage map.";
RL   DNA Res. 3:363-377(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   PROTEIN SEQUENCE OF 2-193.
RX   PubMed=3305077; DOI=10.1016/0014-5793(87)80357-5;
RA   Schinina M.E., Maffey L., Barra D., Bossa F., Puget K.,
RA   Michelson A.M.;
RT   "The primary structure of iron superoxide dismutase from Escherichia
RT   coli.";
RL   FEBS Lett. 221:87-90(1987).
RN   [6]
RP   PARTIAL PROTEIN SEQUENCE.
RX   PubMed=4590170; DOI=10.1073/pnas.70.12.3725;
RA   Steinman H.M., Hill R.L.;
RT   "Sequence homologies among bacterial and mitochondrial superoxide
RT   dismutases.";
RL   Proc. Natl. Acad. Sci. U.S.A. 70:3725-3729(1973).
RN   [7]
RP   PROTEIN SEQUENCE OF 2-13.
RC   STRAIN=K12 / EMG2;
RX   PubMed=9298646; DOI=10.1002/elps.1150180807;
RA   Link A.J., Robison K., Church G.M.;
RT   "Comparing the predicted and observed properties of proteins encoded
RT   in the genome of Escherichia coli K-12.";
RL   Electrophoresis 18:1259-1313(1997).
RN   [8]
RP   PROTEIN SEQUENCE OF 2-5.
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9600841; DOI=10.1006/jmbi.1998.1726;
RA   Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M.,
RA   Sanchez J.-C., Gooley A.A., Walsh B.J., Bairoch A., Appel R.D.,
RA   Williams K.L., Hochstrasser D.F.;
RT   "Protein identification with N and C-terminal sequence tags in
RT   proteome projects.";
RL   J. Mol. Biol. 278:599-608(1998).
RN   [9]
RP   CATALYTIC ACTIVITY, AND COFACTOR.
RX   PubMed=9125513; DOI=10.1021/bi963047z;
RA   Sorkin D.L., Miller A.-F.;
RT   "Spectroscopic measurement of a long-predicted active site pK in iron-
RT   superoxide dismutase from Escherichia coli.";
RL   Biochemistry 36:4916-4924(1997).
RN   [10]
RP   IDENTIFICATION BY 2D-GEL.
RX   PubMed=9298644; DOI=10.1002/elps.1150180805;
RA   VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R.,
RA   Neidhardt F.C.;
RT   "Escherichia coli proteome analysis using the gene-protein database.";
RL   Electrophoresis 18:1243-1251(1997).
RN   [11]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-51, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
RX   PubMed=18723842; DOI=10.1074/mcp.M800187-MCP200;
RA   Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
RA   Grishin N.V., Zhao Y.;
RT   "Lysine acetylation is a highly abundant and evolutionarily conserved
RT   modification in Escherichia coli.";
RL   Mol. Cell. Proteomics 8:215-225(2009).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH IRON ION, AND
RP   SUBUNIT.
RX   PubMed=6346322; DOI=10.1073/pnas.80.13.3884;
RA   Stallings W.C., Powers T.B., Pattridge K.A., Fee J.A., Ludwig M.L.;
RT   "Iron superoxide dismutase from Escherichia coli at 3.1-A resolution:
RT   a structure unlike that of copper/zinc protein at both monomer and
RT   dimer levels.";
RL   Proc. Natl. Acad. Sci. U.S.A. 80:3884-3888(1983).
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       {ECO:0000269|PubMed:9125513}.
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000269|PubMed:9125513};
CC       Note=Binds 1 Fe cation per subunit. {ECO:0000269|PubMed:9125513};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:6346322}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
DR   EMBL; J03511; AAA24637.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC74728.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA15422.1; -; Genomic_DNA.
DR   PIR; A29940; DSECF.
DR   RefSeq; NP_416173.1; NC_000913.3.
DR   RefSeq; WP_000007283.1; NZ_LN832404.1.
DR   PDB; 1ISA; X-ray; 1.80 A; A/B=2-193.
DR   PDB; 1ISB; X-ray; 1.85 A; A/B=2-193.
DR   PDB; 1ISC; X-ray; 1.80 A; A/B=2-193.
DR   PDB; 1ZA5; X-ray; 1.80 A; A/B=2-193.
DR   PDB; 2BKB; X-ray; 1.70 A; A/B/C/D=2-193.
DR   PDB; 2NYB; X-ray; 1.10 A; A/B/C/D=2-193.
DR   PDBsum; 1ISA; -.
DR   PDBsum; 1ISB; -.
DR   PDBsum; 1ISC; -.
DR   PDBsum; 1ZA5; -.
DR   PDBsum; 2BKB; -.
DR   PDBsum; 2NYB; -.
DR   ProteinModelPortal; P0AGD3; -.
DR   SMR; P0AGD3; -.
DR   BioGrid; 4260265; 63.
DR   IntAct; P0AGD3; 6.
DR   STRING; 316385.ECDH10B_1790; -.
DR   iPTMnet; P0AGD3; -.
DR   SWISS-2DPAGE; P0AGD3; -.
DR   EPD; P0AGD3; -.
DR   PaxDb; P0AGD3; -.
DR   PRIDE; P0AGD3; -.
DR   EnsemblBacteria; AAC74728; AAC74728; b1656.
DR   EnsemblBacteria; BAA15422; BAA15422; BAA15422.
DR   GeneID; 944953; -.
DR   KEGG; ecj:JW1648; -.
DR   KEGG; eco:b1656; -.
DR   PATRIC; fig|1411691.4.peg.602; -.
DR   EchoBASE; EB0947; -.
DR   EcoGene; EG10954; sodB.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013584; -.
DR   InParanoid; P0AGD3; -.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   PhylomeDB; P0AGD3; -.
DR   BioCyc; EcoCyc:SUPEROX-DISMUTFE-MONOMER; -.
DR   BioCyc; MetaCyc:SUPEROX-DISMUTFE-MONOMER; -.
DR   BRENDA; 1.15.1.1; 2026.
DR   EvolutionaryTrace; P0AGD3; -.
DR   PRO; PR:P0AGD3; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR   GO; GO:0005829; C:cytosol; HDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005506; F:iron ion binding; IDA:EcoCyc.
DR   GO; GO:0016491; F:oxidoreductase activity; IDA:EcoliWiki.
DR   GO; GO:0004784; F:superoxide dismutase activity; IDA:EcoliWiki.
DR   GO; GO:0055114; P:oxidation-reduction process; IDA:EcoliWiki.
DR   GO; GO:0019430; P:removal of superoxide radicals; IDA:EcoliWiki.
DR   GO; GO:0000303; P:response to superoxide; IDA:EcoliWiki.
DR   GO; GO:0006801; P:superoxide metabolic process; IDA:EcoliWiki.
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   1: Evidence at protein level;
KW   3D-structure; Acetylation; Complete proteome;
KW   Direct protein sequencing; Iron; Metal-binding; Oxidoreductase;
KW   Reference proteome.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:3305077,
FT                                ECO:0000269|PubMed:9298646,
FT                                ECO:0000269|PubMed:9600841}.
FT   CHAIN         2    193       Superoxide dismutase [Fe].
FT                                /FTId=PRO_0000159979.
FT   METAL        27     27       Iron.
FT   METAL        74     74       Iron.
FT   METAL       157    157       Iron.
FT   METAL       161    161       Iron.
FT   MOD_RES      51     51       N6-acetyllysine.
FT                                {ECO:0000269|PubMed:18723842}.
FT   TURN         12     18       {ECO:0000244|PDB:2NYB}.
FT   HELIX        21     29       {ECO:0000244|PDB:2NYB}.
FT   HELIX        31     43       {ECO:0000244|PDB:2NYB}.
FT   TURN         47     50       {ECO:0000244|PDB:2NYB}.
FT   HELIX        53     57       {ECO:0000244|PDB:2NYB}.
FT   HELIX        62     79       {ECO:0000244|PDB:2NYB}.
FT   HELIX        91    101       {ECO:0000244|PDB:2NYB}.
FT   HELIX       104    117       {ECO:0000244|PDB:2NYB}.
FT   STRAND      120    128       {ECO:0000244|PDB:2NYB}.
FT   STRAND      134    140       {ECO:0000244|PDB:2NYB}.
FT   HELIX       145    147       {ECO:0000244|PDB:2NYB}.
FT   STRAND      151    157       {ECO:0000244|PDB:2NYB}.
FT   HELIX       160    162       {ECO:0000244|PDB:2NYB}.
FT   HELIX       164    167       {ECO:0000244|PDB:2NYB}.
FT   HELIX       171    179       {ECO:0000244|PDB:2NYB}.
FT   HELIX       184    192       {ECO:0000244|PDB:2NYB}.
SQ   SEQUENCE   193 AA;  21266 MW;  91236D2A8FE61474 CRC64;
     MSFELPALPY AKDALAPHIS AETIEYHYGK HHQTYVTNLN NLIKGTAFEG KSLEEIIRSS
     EGGVFNNAAQ VWNHTFYWNC LAPNAGGEPT GKVAEAIAAS FGSFADFKAQ FTDAAIKNFG
     SGWTWLVKNS DGKLAIVSTS NAGTPLTTDA TPLLTVDVWE HAYYIDYRNA RPGYLEHFWA
     LVNWEFVAKN LAA
//
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