ID   SODM_ECOLI              Reviewed;         206 AA.
AC   P00448; Q2M8K5;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   27-MAR-2024, entry version 202.
DE   RecName: Full=Superoxide dismutase [Mn];
DE            EC=1.15.1.1;
DE   AltName: Full=MnSOD;
GN   Name=sodA; OrderedLocusNames=b3908, JW3879;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3520487; DOI=10.1093/nar/14.11.4577;
RA   Takeda Y., Avila H.;
RT   "Structure and gene expression of the E. coli Mn-superoxide dismutase
RT   gene.";
RL   Nucleic Acids Res. 14:4577-4589(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=8346018; DOI=10.1093/nar/21.15.3391;
RA   Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.;
RT   "Analysis of the Escherichia coli genome. III. DNA sequence of the region
RT   from 87.2 to 89.2 minutes.";
RL   Nucleic Acids Res. 21:3391-3398(1993).
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 2-206.
RC   STRAIN=B;
RX   PubMed=363708; DOI=10.1016/s0021-9258(17)34235-7;
RA   Steinman H.M.;
RT   "The amino acid sequence of mangano superoxide dismutase from Escherichia
RT   coli B.";
RL   J. Biol. Chem. 253:8708-8720(1978).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-96.
RC   STRAIN=K12;
RX   PubMed=1339463; DOI=10.1099/00221287-138-6-1109;
RA   Garcia C., Baldoma L., Badia J., Aguilar J.;
RT   "Nucleotide sequence of the rhaR-sodA interval specifying rhaT in
RT   Escherichia coli.";
RL   J. Gen. Microbiol. 138:1109-1116(1992).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-63.
RC   STRAIN=K12;
RX   PubMed=1551902; DOI=10.1016/s0021-9258(19)50517-8;
RA   Tate C.G., Muiry J.A.R., Henderson P.J.F.;
RT   "Mapping, cloning, expression, and sequencing of the rhaT gene, which
RT   encodes a novel L-rhamnose-H+ transport protein in Salmonella typhimurium
RT   and Escherichia coli.";
RL   J. Biol. Chem. 267:6923-6932(1992).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-2.
RX   PubMed=3131302; DOI=10.1128/jb.170.6.2511-2520.1988;
RA   Touati D.;
RT   "Transcriptional and posttranscriptional regulation of manganese superoxide
RT   dismutase biosynthesis in Escherichia coli, studied with operon and protein
RT   fusions.";
RL   J. Bacteriol. 170:2511-2520(1988).
RN   [9]
RP   PROTEIN SEQUENCE OF 2-30.
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   [10]
RP   PROTEIN SEQUENCE OF 2-11.
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA   Pasquali C., Sanchez J.-C., Ravier F., Golaz O., Hughes G.J., Frutiger S.,
RA   Paquet N., Wilkins M., Appel R.D., Bairoch A., Hochstrasser D.F.;
RL   Submitted (SEP-1994) to UniProtKB.
RN   [11]
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   [12]
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   [13]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANTS PHE-35; LEU-147 AND
RP   HIS-147.
RX   PubMed=11141052; DOI=10.1021/bi0018943;
RA   Edwards R.A., Whittaker M.M., Whittaker J.W., Baker E.N., Jameson G.B.;
RT   "Outer sphere mutations perturb metal reactivity in manganese superoxide
RT   dismutase.";
RL   Biochemistry 40:15-27(2001).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF MUTANTS ALA-31 AND PHE-175.
RX   PubMed=11294629; DOI=10.1021/bi002403h;
RA   Edwards R.A., Whittaker M.M., Whittaker J.W., Baker E.N., Jameson G.B.;
RT   "Removing a hydrogen bond in the dimer interface of Escherichia coli
RT   manganese superoxide dismutase alters structure and reactivity.";
RL   Biochemistry 40:4622-4632(2001).
RN   [15]
RP   STRUCTURE BY NMR.
RX   PubMed=9003797; DOI=10.1016/s0014-5793(96)31420-2;
RA   Renault J.P., Verchere-Beau R., Morgenstern-Badarau I., Piccioli M.;
RT   "Paramagnetic NMR spectroscopy of native and cobalt substituted manganese
RT   superoxide dismutase from Escherichia coli.";
RL   FEBS Lett. 401:15-19(1997).
RN   [16]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RA   Edwards R.A., Baker H.M., Whittaker M.M., Whittaker J.W., Jameson G.B.,
RA   Baker E.N.;
RT   "Crystal structure of Escherichia coli manganese superoxide dismutase at
RT   2.1-A resolution.";
RL   J. Biol. Inorg. Chem. 3:161-171(1998).
RN   [17]
RP   X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS).
RX   PubMed=10686094; DOI=10.1006/jmbi.1999.3506;
RA   Borgstahl G.E., Pokross M., Chehab R., Sekher A., Snell E.H.;
RT   "Cryo-trapping the six-coordinate, distorted-octahedral active site of
RT   manganese superoxide dismutase.";
RL   J. Mol. Biol. 296:951-959(2000).
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   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC       Note=Binds 1 Mn(2+) ion per subunit.;
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC       {ECO:0000305}.
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DR   EMBL; X03951; CAA27580.1; -; Genomic_DNA.
DR   EMBL; M20984; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; L19201; AAB03041.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76890.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77401.1; -; Genomic_DNA.
DR   EMBL; X60699; CAA43108.1; -; Genomic_DNA.
DR   EMBL; M85158; AAA24528.1; ALT_SEQ; Genomic_DNA.
DR   PIR; A24141; DSECN.
DR   RefSeq; NP_418344.3; NC_000913.3.
DR   RefSeq; WP_000122641.1; NZ_SSZK01000014.1.
DR   PDB; 1D5N; X-ray; 1.55 A; A/B/C/D=2-206.
DR   PDB; 1EN4; X-ray; 2.00 A; A/B/C/D=2-206.
DR   PDB; 1EN5; X-ray; 2.30 A; A/B/C/D=2-206.
DR   PDB; 1EN6; X-ray; 2.00 A; A/B/C/D=2-206.
DR   PDB; 1I08; X-ray; 2.20 A; A/B/C/D=2-206.
DR   PDB; 1I0H; X-ray; 1.35 A; A/B=2-206.
DR   PDB; 1IX9; X-ray; 0.90 A; A/B=2-206.
DR   PDB; 1IXB; X-ray; 0.90 A; A/B=2-206.
DR   PDB; 1MMM; X-ray; 2.20 A; A/B=2-206.
DR   PDB; 1VEW; X-ray; 2.10 A; A/B/C/D=2-206.
DR   PDB; 1ZLZ; X-ray; 1.55 A; A/B=2-206.
DR   PDB; 3K9S; X-ray; 1.55 A; A/B/C/D=2-206.
DR   PDB; 3OT7; X-ray; 1.90 A; A/B/C/D=2-206.
DR   PDBsum; 1D5N; -.
DR   PDBsum; 1EN4; -.
DR   PDBsum; 1EN5; -.
DR   PDBsum; 1EN6; -.
DR   PDBsum; 1I08; -.
DR   PDBsum; 1I0H; -.
DR   PDBsum; 1IX9; -.
DR   PDBsum; 1IXB; -.
DR   PDBsum; 1MMM; -.
DR   PDBsum; 1VEW; -.
DR   PDBsum; 1ZLZ; -.
DR   PDBsum; 3K9S; -.
DR   PDBsum; 3OT7; -.
DR   AlphaFoldDB; P00448; -.
DR   SASBDB; P00448; -.
DR   SMR; P00448; -.
DR   BioGRID; 4262227; 66.
DR   IntAct; P00448; 7.
DR   STRING; 511145.b3908; -.
DR   jPOST; P00448; -.
DR   PaxDb; 511145-b3908; -.
DR   EnsemblBacteria; AAC76890; AAC76890; b3908.
DR   GeneID; 948403; -.
DR   KEGG; ecj:JW3879; -.
DR   KEGG; eco:b3908; -.
DR   PATRIC; fig|1411691.4.peg.2797; -.
DR   EchoBASE; EB0946; -.
DR   eggNOG; COG0605; Bacteria.
DR   HOGENOM; CLU_031625_0_1_6; -.
DR   InParanoid; P00448; -.
DR   OMA; GSYEGWK; -.
DR   OrthoDB; 9803125at2; -.
DR   PhylomeDB; P00448; -.
DR   BioCyc; EcoCyc:SUPEROX-DISMUTMN-MONOMER; -.
DR   BioCyc; MetaCyc:SUPEROX-DISMUTMN-MONOMER; -.
DR   BRENDA; 1.15.1.1; 2026.
DR   EvolutionaryTrace; P00448; -.
DR   PHI-base; PHI:9764; -.
DR   PRO; PR:P00448; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0016209; F:antioxidant activity; IMP:EcoCyc.
DR   GO; GO:0003677; F:DNA binding; IDA:EcoCyc.
DR   GO; GO:0030145; F:manganese ion binding; IDA:EcoCyc.
DR   GO; GO:0046872; F:metal ion binding; IDA:EcoliWiki.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:EcoCyc.
DR   GO; GO:0004784; F:superoxide dismutase activity; IDA:EcoCyc.
DR   GO; GO:0071291; P:cellular response to selenium ion; IEP:EcoCyc.
DR   GO; GO:0019430; P:removal of superoxide radicals; IDA:EcoliWiki.
DR   GO; GO:0010447; P:response to acidic pH; IMP:EcoCyc.
DR   GO; GO:0009408; P:response to heat; IMP:EcoCyc.
DR   GO; GO:0006979; P:response to oxidative stress; IMP:EcoCyc.
DR   GO; GO:0006801; P:superoxide metabolic process; IDA:EcoliWiki.
DR   Gene3D; 1.10.287.990; Fe,Mn superoxide dismutase (SOD) domain; 1.
DR   Gene3D; 3.55.40.20; Iron/manganese superoxide dismutase, C-terminal domain; 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   PANTHER; PTHR43595; 37S RIBOSOMAL PROTEIN S26, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43595:SF2; 37S RIBOSOMAL PROTEIN S26, MITOCHONDRIAL; 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; SSF54719; Fe,Mn superoxide dismutase (SOD), C-terminal domain; 1.
DR   SUPFAM; SSF46609; Fe,Mn superoxide dismutase (SOD), N-terminal domain; 1.
DR   PROSITE; PS00088; SOD_MN; 1.
DR   SWISS-2DPAGE; P00448; -.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Manganese; Metal-binding;
KW   Oxidoreductase; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:363708,
FT                   ECO:0000269|PubMed:4590170, ECO:0000269|PubMed:9298646,
FT                   ECO:0000269|Ref.10"
FT   CHAIN           2..206
FT                   /note="Superoxide dismutase [Mn]"
FT                   /id="PRO_0000160030"
FT   BINDING         27
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT   BINDING         82
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT   BINDING         168
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT   BINDING         172
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT   VARIANT         165
FT                   /note="M -> L (in strain: B)"
FT   CONFLICT        26
FT                   /note="I -> L (in Ref. 9; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   TURN            12..18
FT                   /evidence="ECO:0007829|PDB:1IX9"
FT   HELIX           21..29
FT                   /evidence="ECO:0007829|PDB:1IX9"
FT   HELIX           31..43
FT                   /evidence="ECO:0007829|PDB:1IX9"
FT   HELIX           47..50
FT                   /evidence="ECO:0007829|PDB:1IX9"
FT   HELIX           54..57
FT                   /evidence="ECO:0007829|PDB:1IX9"
FT   HELIX           61..63
FT                   /evidence="ECO:0007829|PDB:1IX9"
FT   HELIX           66..68
FT                   /evidence="ECO:0007829|PDB:1IX9"
FT   HELIX           69..87
FT                   /evidence="ECO:0007829|PDB:1IX9"
FT   HELIX           97..107
FT                   /evidence="ECO:0007829|PDB:1IX9"
FT   HELIX           110..123
FT                   /evidence="ECO:0007829|PDB:1IX9"
FT   STRAND          126..135
FT                   /evidence="ECO:0007829|PDB:1IX9"
FT   STRAND          138..145
FT                   /evidence="ECO:0007829|PDB:1IX9"
FT   HELIX           150..152
FT                   /evidence="ECO:0007829|PDB:1IX9"
FT   HELIX           154..157
FT                   /evidence="ECO:0007829|PDB:1IX9"
FT   STRAND          161..168
FT                   /evidence="ECO:0007829|PDB:1IX9"
FT   HELIX           171..173
FT                   /evidence="ECO:0007829|PDB:1IX9"
FT   HELIX           175..178
FT                   /evidence="ECO:0007829|PDB:1IX9"
FT   HELIX           182..192
FT                   /evidence="ECO:0007829|PDB:1IX9"
FT   HELIX           195..205
FT                   /evidence="ECO:0007829|PDB:1IX9"
SQ   SEQUENCE   206 AA;  23097 MW;  082DAF56EA3C15CC CRC64;
     MSYTLPSLPY AYDALEPHFD KQTMEIHHTK HHQTYVNNAN AALESLPEFA NLPVEELITK
     LDQLPADKKT VLRNNAGGHA NHSLFWKGLK KGTTLQGDLK AAIERDFGSV DNFKAEFEKA
     AASRFGSGWA WLVLKGDKLA VVSTANQDSP LMGEAISGAS GFPIMGLDVW EHAYYLKFQN
     RRPDYIKEFW NVVNWDEAAA RFAAKK
//