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 03-AUG-2022, entry version 194.
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 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 2-11.
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 [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 in the
RT 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., 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., Jameson G.B.;
RT "Outer sphere mutations perturb metal reactivity in manganese superoxide
RT 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., 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 manganese
RT 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., 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 [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 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 SMR; P00448; -.
DR BioGRID; 4262227; 66.
DR IntAct; P00448; 7.
DR STRING; 511145.b3908; -.
DR SWISS-2DPAGE; P00448; -.
DR jPOST; 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 eggNOG; COG0605; Bacteria.
DR HOGENOM; CLU_031625_0_1_6; -.
DR InParanoid; P00448; -.
DR OMA; YEGWKGE; -.
DR PhylomeDB; P00448; -.
DR BioCyc; EcoCyc:SUPEROX-DISMUTMN-MON; -.
DR BioCyc; MetaCyc:SUPEROX-DISMUTMN-MON; -.
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: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; 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; 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:9298646, ECO:0000269|Ref.9"
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 81..82
FT /note="NH -> HN (in Ref. 6)"
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
