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 03-AUG-2022, entry version 125.
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; DOI=10.1016/s0021-9258(19)57340-9;
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., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT 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., Mau B.,
RA 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 MG1655
RT 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., 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 in the
RT 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., Sanchez J.-C.,
RA Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L.,
RA Hochstrasser D.F.;
RT "Protein identification with N and C-terminal sequence tags in proteome
RT 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., 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 MASS
RP 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: a
RT structure unlike that of copper/zinc protein at both monomer and dimer
RT 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 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 Evidence={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 family.
CC {ECO:0000305}.
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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_STEB01000003.1.
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 AlphaFoldDB; P0AGD3; -.
DR BMRB; P0AGD3; -.
DR SMR; P0AGD3; -.
DR BioGRID; 4260265; 63.
DR IntAct; P0AGD3; 6.
DR STRING; 511145.b1656; -.
DR iPTMnet; P0AGD3; -.
DR SWISS-2DPAGE; P0AGD3; -.
DR jPOST; 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 eggNOG; COG0605; Bacteria.
DR HOGENOM; CLU_031625_0_0_6; -.
DR InParanoid; P0AGD3; -.
DR OMA; YLHSIFW; -.
DR PhylomeDB; P0AGD3; -.
DR BioCyc; EcoCyc:SUPEROX-DISMUTFE-MON; -.
DR BioCyc; MetaCyc:SUPEROX-DISMUTFE-MON; -.
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: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; 3.55.40.20; -; 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; Direct protein sequencing; Iron; Metal-binding;
KW Oxidoreductase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3305077,
FT ECO:0000269|PubMed:9298646, ECO:0000269|PubMed:9600841"
FT CHAIN 2..193
FT /note="Superoxide dismutase [Fe]"
FT /id="PRO_0000159979"
FT BINDING 27
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 74
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 157
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 161
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT MOD_RES 51
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT TURN 12..18
FT /evidence="ECO:0007829|PDB:2NYB"
FT HELIX 21..29
FT /evidence="ECO:0007829|PDB:2NYB"
FT HELIX 31..43
FT /evidence="ECO:0007829|PDB:2NYB"
FT TURN 47..50
FT /evidence="ECO:0007829|PDB:2NYB"
FT HELIX 53..57
FT /evidence="ECO:0007829|PDB:2NYB"
FT HELIX 62..79
FT /evidence="ECO:0007829|PDB:2NYB"
FT HELIX 91..101
FT /evidence="ECO:0007829|PDB:2NYB"
FT HELIX 104..117
FT /evidence="ECO:0007829|PDB:2NYB"
FT STRAND 120..128
FT /evidence="ECO:0007829|PDB:2NYB"
FT STRAND 134..140
FT /evidence="ECO:0007829|PDB:2NYB"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:2NYB"
FT STRAND 151..157
FT /evidence="ECO:0007829|PDB:2NYB"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:2NYB"
FT HELIX 164..167
FT /evidence="ECO:0007829|PDB:2NYB"
FT HELIX 171..179
FT /evidence="ECO:0007829|PDB:2NYB"
FT HELIX 184..192
FT /evidence="ECO:0007829|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
