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Superoxide dismutase [Fe] (EC 1.15.1.1)

 SODF_ECOLI              Reviewed;         193 AA.
P0AGD3; P09157;
20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
28-MAR-2018, entry version 103.
RecName: Full=Superoxide dismutase [Fe];
EC=1.15.1.1;
Name=sodB; OrderedLocusNames=b1656, JW1648;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
STRAIN=K12;
PubMed=2447093;
Carlioz A., Ludwig M.L., Stallings W.C., Fee J.A., Steinman H.M.,
Touati D.;
"Iron superoxide dismutase. Nucleotide sequence of the gene from
Escherichia coli K12 and correlations with crystal structures.";
J. Biol. Chem. 263:1555-1562(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=9097039; DOI=10.1093/dnares/3.6.363;
Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M.,
Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K.,
Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N.,
Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J.,
Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.;
"A 570-kb DNA sequence of the Escherichia coli K-12 genome
corresponding to the 28.0-40.1 min region on the linkage map.";
DNA Res. 3:363-377(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
PROTEIN SEQUENCE OF 2-193.
PubMed=3305077; DOI=10.1016/0014-5793(87)80357-5;
Schinina M.E., Maffey L., Barra D., Bossa F., Puget K.,
Michelson A.M.;
"The primary structure of iron superoxide dismutase from Escherichia
coli.";
FEBS Lett. 221:87-90(1987).
[6]
PARTIAL PROTEIN SEQUENCE.
PubMed=4590170; DOI=10.1073/pnas.70.12.3725;
Steinman H.M., Hill R.L.;
"Sequence homologies among bacterial and mitochondrial superoxide
dismutases.";
Proc. Natl. Acad. Sci. U.S.A. 70:3725-3729(1973).
[7]
PROTEIN SEQUENCE OF 2-13.
STRAIN=K12 / EMG2;
PubMed=9298646; DOI=10.1002/elps.1150180807;
Link A.J., Robison K., Church G.M.;
"Comparing the predicted and observed properties of proteins encoded
in the genome of Escherichia coli K-12.";
Electrophoresis 18:1259-1313(1997).
[8]
PROTEIN SEQUENCE OF 2-5.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=9600841; DOI=10.1006/jmbi.1998.1726;
Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M.,
Sanchez J.-C., Gooley A.A., Walsh B.J., Bairoch A., Appel R.D.,
Williams K.L., Hochstrasser D.F.;
"Protein identification with N and C-terminal sequence tags in
proteome projects.";
J. Mol. Biol. 278:599-608(1998).
[9]
CATALYTIC ACTIVITY, AND COFACTOR.
PubMed=9125513; DOI=10.1021/bi963047z;
Sorkin D.L., Miller A.-F.;
"Spectroscopic measurement of a long-predicted active site pK in iron-
superoxide dismutase from Escherichia coli.";
Biochemistry 36:4916-4924(1997).
[10]
IDENTIFICATION BY 2D-GEL.
PubMed=9298644; DOI=10.1002/elps.1150180805;
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R.,
Neidhardt F.C.;
"Escherichia coli proteome analysis using the gene-protein database.";
Electrophoresis 18:1243-1251(1997).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-51, AND IDENTIFICATION BY
MASS SPECTROMETRY.
STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
PubMed=18723842; DOI=10.1074/mcp.M800187-MCP200;
Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
Grishin N.V., Zhao Y.;
"Lysine acetylation is a highly abundant and evolutionarily conserved
modification in Escherichia coli.";
Mol. Cell. Proteomics 8:215-225(2009).
[12]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH IRON ION, AND
SUBUNIT.
PubMed=6346322; DOI=10.1073/pnas.80.13.3884;
Stallings W.C., Powers T.B., Pattridge K.A., Fee J.A., Ludwig M.L.;
"Iron superoxide dismutase from Escherichia coli at 3.1-A resolution:
a structure unlike that of copper/zinc protein at both monomer and
dimer levels.";
Proc. Natl. Acad. Sci. U.S.A. 80:3884-3888(1983).
-!- FUNCTION: Destroys superoxide anion radicals which are normally
produced within the cells and which are toxic to biological
systems.
-!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
{ECO:0000269|PubMed:9125513}.
-!- COFACTOR:
Name=Fe cation; Xref=ChEBI:CHEBI:24875;
Evidence={ECO:0000269|PubMed:9125513};
Note=Binds 1 Fe cation per subunit. {ECO:0000269|PubMed:9125513};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:6346322}.
-!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; J03511; AAA24637.1; -; Genomic_DNA.
EMBL; U00096; AAC74728.1; -; Genomic_DNA.
EMBL; AP009048; BAA15422.1; -; Genomic_DNA.
PIR; A29940; DSECF.
RefSeq; NP_416173.1; NC_000913.3.
RefSeq; WP_000007283.1; NZ_LN832404.1.
PDB; 1ISA; X-ray; 1.80 A; A/B=2-193.
PDB; 1ISB; X-ray; 1.85 A; A/B=2-193.
PDB; 1ISC; X-ray; 1.80 A; A/B=2-193.
PDB; 1ZA5; X-ray; 1.80 A; A/B=2-193.
PDB; 2BKB; X-ray; 1.70 A; A/B/C/D=2-193.
PDB; 2NYB; X-ray; 1.10 A; A/B/C/D=2-193.
PDBsum; 1ISA; -.
PDBsum; 1ISB; -.
PDBsum; 1ISC; -.
PDBsum; 1ZA5; -.
PDBsum; 2BKB; -.
PDBsum; 2NYB; -.
ProteinModelPortal; P0AGD3; -.
SMR; P0AGD3; -.
BioGrid; 4260265; 63.
IntAct; P0AGD3; 6.
STRING; 316385.ECDH10B_1790; -.
iPTMnet; P0AGD3; -.
SWISS-2DPAGE; P0AGD3; -.
EPD; P0AGD3; -.
PaxDb; P0AGD3; -.
PRIDE; P0AGD3; -.
EnsemblBacteria; AAC74728; AAC74728; b1656.
EnsemblBacteria; BAA15422; BAA15422; BAA15422.
GeneID; 944953; -.
KEGG; ecj:JW1648; -.
KEGG; eco:b1656; -.
PATRIC; fig|1411691.4.peg.602; -.
EchoBASE; EB0947; -.
EcoGene; EG10954; sodB.
eggNOG; ENOG4105CK4; Bacteria.
eggNOG; COG0605; LUCA.
HOGENOM; HOG000013584; -.
InParanoid; P0AGD3; -.
KO; K04564; -.
OMA; KWGSFDK; -.
PhylomeDB; P0AGD3; -.
BioCyc; EcoCyc:SUPEROX-DISMUTFE-MONOMER; -.
BioCyc; MetaCyc:SUPEROX-DISMUTFE-MONOMER; -.
BRENDA; 1.15.1.1; 2026.
EvolutionaryTrace; P0AGD3; -.
PRO; PR:P0AGD3; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
GO; GO:0005829; C:cytosol; HDA:UniProtKB.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005506; F:iron ion binding; IDA:EcoCyc.
GO; GO:0016491; F:oxidoreductase activity; IDA:EcoliWiki.
GO; GO:0004784; F:superoxide dismutase activity; IDA:EcoliWiki.
GO; GO:0055114; P:oxidation-reduction process; IDA:EcoliWiki.
GO; GO:0019430; P:removal of superoxide radicals; IDA:EcoliWiki.
GO; GO:0000303; P:response to superoxide; IDA:EcoliWiki.
GO; GO:0006801; P:superoxide metabolic process; IDA:EcoliWiki.
Gene3D; 1.10.287.990; -; 1.
Gene3D; 2.40.500.20; -; 1.
InterPro; IPR001189; Mn/Fe_SOD.
InterPro; IPR019833; Mn/Fe_SOD_BS.
InterPro; IPR019832; Mn/Fe_SOD_C.
InterPro; IPR019831; Mn/Fe_SOD_N.
InterPro; IPR036324; Mn/Fe_SOD_N_sf.
InterPro; IPR036314; SOD_C_sf.
Pfam; PF02777; Sod_Fe_C; 1.
Pfam; PF00081; Sod_Fe_N; 1.
PIRSF; PIRSF000349; SODismutase; 1.
PRINTS; PR01703; MNSODISMTASE.
SUPFAM; SSF46609; SSF46609; 1.
SUPFAM; SSF54719; SSF54719; 1.
PROSITE; PS00088; SOD_MN; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome;
Direct protein sequencing; Iron; Metal-binding; Oxidoreductase;
Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:3305077,
ECO:0000269|PubMed:9298646,
ECO:0000269|PubMed:9600841}.
CHAIN 2 193 Superoxide dismutase [Fe].
/FTId=PRO_0000159979.
METAL 27 27 Iron.
METAL 74 74 Iron.
METAL 157 157 Iron.
METAL 161 161 Iron.
MOD_RES 51 51 N6-acetyllysine.
{ECO:0000269|PubMed:18723842}.
TURN 12 18 {ECO:0000244|PDB:2NYB}.
HELIX 21 29 {ECO:0000244|PDB:2NYB}.
HELIX 31 43 {ECO:0000244|PDB:2NYB}.
TURN 47 50 {ECO:0000244|PDB:2NYB}.
HELIX 53 57 {ECO:0000244|PDB:2NYB}.
HELIX 62 79 {ECO:0000244|PDB:2NYB}.
HELIX 91 101 {ECO:0000244|PDB:2NYB}.
HELIX 104 117 {ECO:0000244|PDB:2NYB}.
STRAND 120 128 {ECO:0000244|PDB:2NYB}.
STRAND 134 140 {ECO:0000244|PDB:2NYB}.
HELIX 145 147 {ECO:0000244|PDB:2NYB}.
STRAND 151 157 {ECO:0000244|PDB:2NYB}.
HELIX 160 162 {ECO:0000244|PDB:2NYB}.
HELIX 164 167 {ECO:0000244|PDB:2NYB}.
HELIX 171 179 {ECO:0000244|PDB:2NYB}.
HELIX 184 192 {ECO:0000244|PDB:2NYB}.
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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