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Database: UniProt/SWISS-PROT
Entry: SODM_ECOLI
LinkDB: SODM_ECOLI
Original site: SODM_ECOLI 
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   28-MAR-2018, entry version 172.
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; Proteobacteria; 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
RT   region 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.,
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 2-206.
RC   STRAIN=B;
RX   PubMed=363708;
RA   Steinman H.M.;
RT   "The amino acid sequence of mangano superoxide dismutase from
RT   Escherichia 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;
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
RT   typhimurium 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
RT   superoxide dismutase biosynthesis in Escherichia coli, studied with
RT   operon and protein fusions.";
RL   J. Bacteriol. 170:2511-2520(1988).
RN   [9]
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.,
RA   Frutiger S., Paquet N., Wilkins M., Appel R.D., Bairoch A.,
RA   Hochstrasser D.F.;
RL   Submitted (SEP-1994) to UniProtKB.
RN   [10]
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   [11]
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   [12]
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.,
RA   Jameson G.B.;
RT   "Outer sphere mutations perturb metal reactivity in manganese
RT   superoxide dismutase.";
RL   Biochemistry 40:15-27(2001).
RN   [13]
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.,
RA   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   [14]
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
RT   manganese superoxide dismutase from Escherichia coli.";
RL   FEBS Lett. 401:15-19(1997).
RN   [15]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RA   Edwards R.A., Baker H.M., Whittaker M.M., Whittaker J.W.,
RA   Jameson G.B., Baker E.N.;
RT   "Crystal structure of Escherichia coli manganese superoxide dismutase
RT   at 2.1-A resolution.";
RL   J. Biol. Inorg. Chem. 3:161-171(1998).
RN   [16]
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
CC       systems.
CC   -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
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
CC       family. {ECO:0000305}.
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_LN832404.1.
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   ProteinModelPortal; P00448; -.
DR   SMR; P00448; -.
DR   BioGrid; 4262227; 66.
DR   IntAct; P00448; 7.
DR   STRING; 316385.ECDH10B_4098; -.
DR   SWISS-2DPAGE; P00448; -.
DR   EPD; P00448; -.
DR   PaxDb; P00448; -.
DR   PRIDE; P00448; -.
DR   EnsemblBacteria; AAC76890; AAC76890; b3908.
DR   EnsemblBacteria; BAE77401; BAE77401; BAE77401.
DR   GeneID; 948403; -.
DR   KEGG; ecj:JW3879; -.
DR   KEGG; eco:b3908; -.
DR   PATRIC; fig|1411691.4.peg.2797; -.
DR   EchoBASE; EB0946; -.
DR   EcoGene; EG10953; sodA.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013583; -.
DR   InParanoid; P00448; -.
DR   KO; K04564; -.
DR   OMA; YEGWKGE; -.
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   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:0004784; F:superoxide dismutase activity; IDA:EcoCyc.
DR   GO; GO:0071291; P:cellular response to selenium ion; IEP:EcoCyc.
DR   GO; GO:0055114; P:oxidation-reduction process; IDA:EcoliWiki.
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; -; 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; Complete proteome; Direct protein sequencing; Manganese;
KW   Metal-binding; Oxidoreductase; Reference proteome.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:363708,
FT                                ECO:0000269|PubMed:9298646,
FT                                ECO:0000269|Ref.9}.
FT   CHAIN         2    206       Superoxide dismutase [Mn].
FT                                /FTId=PRO_0000160030.
FT   METAL        27     27       Manganese.
FT   METAL        82     82       Manganese.
FT   METAL       168    168       Manganese.
FT   METAL       172    172       Manganese.
FT   VARIANT     165    165       M -> L (in strain: B).
FT   CONFLICT     81     82       NH -> HN (in Ref. 6). {ECO:0000305}.
FT   TURN         12     18       {ECO:0000244|PDB:1IX9}.
FT   HELIX        21     29       {ECO:0000244|PDB:1IX9}.
FT   HELIX        31     43       {ECO:0000244|PDB:1IX9}.
FT   HELIX        47     50       {ECO:0000244|PDB:1IX9}.
FT   HELIX        54     57       {ECO:0000244|PDB:1IX9}.
FT   HELIX        61     63       {ECO:0000244|PDB:1IX9}.
FT   HELIX        66     68       {ECO:0000244|PDB:1IX9}.
FT   HELIX        69     87       {ECO:0000244|PDB:1IX9}.
FT   HELIX        97    107       {ECO:0000244|PDB:1IX9}.
FT   HELIX       110    123       {ECO:0000244|PDB:1IX9}.
FT   STRAND      126    135       {ECO:0000244|PDB:1IX9}.
FT   STRAND      138    145       {ECO:0000244|PDB:1IX9}.
FT   HELIX       150    152       {ECO:0000244|PDB:1IX9}.
FT   HELIX       154    157       {ECO:0000244|PDB:1IX9}.
FT   STRAND      161    168       {ECO:0000244|PDB:1IX9}.
FT   HELIX       171    173       {ECO:0000244|PDB:1IX9}.
FT   HELIX       175    178       {ECO:0000244|PDB:1IX9}.
FT   HELIX       182    192       {ECO:0000244|PDB:1IX9}.
FT   HELIX       195    205       {ECO:0000244|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
//
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