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Protein

Superoxide dismutase [Mn]

Gene

sodA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.

Catalytic activityi

2 superoxide + 2 H+ = O2 + H2O2.

Cofactori

Mn2+Note: Binds 1 Mn2+ ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi27 – 271Manganese
Metal bindingi82 – 821Manganese
Metal bindingi168 – 1681Manganese
Metal bindingi172 – 1721Manganese

GO - Molecular functioni

  1. antioxidant activity Source: EcoCyc
  2. DNA binding Source: EcoCyc
  3. manganese ion binding Source: EcoCyc
  4. metal ion binding Source: EcoliWiki
  5. superoxide dismutase activity Source: EcoCyc

GO - Biological processi

  1. cellular response to selenium ion Source: EcoCyc
  2. oxidation-reduction process Source: EcoliWiki
  3. removal of superoxide radicals Source: EcoliWiki
  4. response to acidic pH Source: EcoCyc
  5. response to heat Source: EcoCyc
  6. response to oxidative stress Source: EcoCyc
  7. superoxide metabolic process Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:SUPEROX-DISMUTMN-MONOMER.
ECOL316407:JW3879-MONOMER.
MetaCyc:SUPEROX-DISMUTMN-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Superoxide dismutase [Mn] (EC:1.15.1.1)
Alternative name(s):
MnSOD
Gene namesi
Name:sodA
Ordered Locus Names:b3908, JW3879
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10953. sodA.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: EcoliWiki
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 206205Superoxide dismutase [Mn]PRO_0000160030Add
BLAST

Proteomic databases

PaxDbiP00448.
PRIDEiP00448.

2D gel databases

SWISS-2DPAGEP00448.

Expressioni

Gene expression databases

GenevestigatoriP00448.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

IntActiP00448. 7 interactions.
STRINGi511145.b3908.

Structurei

Secondary structure

1
206
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni12 – 187Combined sources
Helixi21 – 299Combined sources
Helixi31 – 4313Combined sources
Helixi47 – 504Combined sources
Helixi54 – 574Combined sources
Helixi61 – 633Combined sources
Helixi66 – 683Combined sources
Helixi69 – 8719Combined sources
Helixi97 – 10711Combined sources
Helixi110 – 12314Combined sources
Beta strandi126 – 13510Combined sources
Beta strandi138 – 1458Combined sources
Helixi150 – 1523Combined sources
Helixi154 – 1574Combined sources
Beta strandi161 – 1688Combined sources
Helixi171 – 1733Combined sources
Helixi175 – 1784Combined sources
Helixi182 – 19211Combined sources
Helixi195 – 20511Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1D5NX-ray1.55A/B/C/D2-206[»]
1EN4X-ray2.00A/B/C/D2-206[»]
1EN5X-ray2.30A/B/C/D2-206[»]
1EN6X-ray2.00A/B/C/D2-206[»]
1I08X-ray2.20A/B/C/D2-206[»]
1I0HX-ray1.35A/B2-206[»]
1IX9X-ray0.90A/B2-206[»]
1IXBX-ray0.90A/B2-206[»]
1MMMX-ray2.20A/B2-206[»]
1VEWX-ray2.10A/B/C/D2-206[»]
1ZLZX-ray1.55A/B2-206[»]
3K9SX-ray1.55A/B/C/D2-206[»]
3OT7X-ray1.90A/B/C/D2-206[»]
ProteinModelPortaliP00448.
SMRiP00448. Positions 2-206.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00448.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0605.
HOGENOMiHOG000013583.
InParanoidiP00448.
KOiK04564.
OMAiKHHNAYT.
OrthoDBiEOG63NMNT.
PhylomeDBiP00448.

Family and domain databases

InterProiIPR001189. Mn/Fe_SOD.
IPR019833. Mn/Fe_SOD_BS.
IPR019832. Mn/Fe_SOD_C.
IPR019831. Mn/Fe_SOD_N.
[Graphical view]
PANTHERiPTHR11404. PTHR11404. 1 hit.
PfamiPF02777. Sod_Fe_C. 1 hit.
PF00081. Sod_Fe_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000349. SODismutase. 1 hit.
PRINTSiPR01703. MNSODISMTASE.
SUPFAMiSSF46609. SSF46609. 1 hit.
SSF54719. SSF54719. 1 hit.
PROSITEiPS00088. SOD_MN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00448-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSYTLPSLPY AYDALEPHFD KQTMEIHHTK HHQTYVNNAN AALESLPEFA
60 70 80 90 100
NLPVEELITK LDQLPADKKT VLRNNAGGHA NHSLFWKGLK KGTTLQGDLK
110 120 130 140 150
AAIERDFGSV DNFKAEFEKA AASRFGSGWA WLVLKGDKLA VVSTANQDSP
160 170 180 190 200
LMGEAISGAS GFPIMGLDVW EHAYYLKFQN RRPDYIKEFW NVVNWDEAAA

RFAAKK
Length:206
Mass (Da):23,097
Last modified:January 23, 2007 - v2
Checksum:i082DAF56EA3C15CC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti81 – 822NH → HN (PubMed:1339463).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti165 – 1651M → L in strain: B.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03951 Genomic DNA. Translation: CAA27580.1.
M20984 Genomic DNA. No translation available.
L19201 Genomic DNA. Translation: AAB03041.1.
U00096 Genomic DNA. Translation: AAC76890.1.
AP009048 Genomic DNA. Translation: BAE77401.1.
X60699 Genomic DNA. Translation: CAA43108.1.
M85158 Genomic DNA. Translation: AAA24528.1. Sequence problems.
PIRiA24141. DSECN.
RefSeqiNP_418344.3. NC_000913.3.
YP_491542.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76890; AAC76890; b3908.
BAE77401; BAE77401; BAE77401.
GeneIDi12933233.
948403.
KEGGiecj:Y75_p3278.
eco:b3908.
PATRICi32123327. VBIEscCol129921_4024.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03951 Genomic DNA. Translation: CAA27580.1.
M20984 Genomic DNA. No translation available.
L19201 Genomic DNA. Translation: AAB03041.1.
U00096 Genomic DNA. Translation: AAC76890.1.
AP009048 Genomic DNA. Translation: BAE77401.1.
X60699 Genomic DNA. Translation: CAA43108.1.
M85158 Genomic DNA. Translation: AAA24528.1. Sequence problems.
PIRiA24141. DSECN.
RefSeqiNP_418344.3. NC_000913.3.
YP_491542.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1D5NX-ray1.55A/B/C/D2-206[»]
1EN4X-ray2.00A/B/C/D2-206[»]
1EN5X-ray2.30A/B/C/D2-206[»]
1EN6X-ray2.00A/B/C/D2-206[»]
1I08X-ray2.20A/B/C/D2-206[»]
1I0HX-ray1.35A/B2-206[»]
1IX9X-ray0.90A/B2-206[»]
1IXBX-ray0.90A/B2-206[»]
1MMMX-ray2.20A/B2-206[»]
1VEWX-ray2.10A/B/C/D2-206[»]
1ZLZX-ray1.55A/B2-206[»]
3K9SX-ray1.55A/B/C/D2-206[»]
3OT7X-ray1.90A/B/C/D2-206[»]
ProteinModelPortaliP00448.
SMRiP00448. Positions 2-206.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP00448. 7 interactions.
STRINGi511145.b3908.

2D gel databases

SWISS-2DPAGEP00448.

Proteomic databases

PaxDbiP00448.
PRIDEiP00448.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76890; AAC76890; b3908.
BAE77401; BAE77401; BAE77401.
GeneIDi12933233.
948403.
KEGGiecj:Y75_p3278.
eco:b3908.
PATRICi32123327. VBIEscCol129921_4024.

Organism-specific databases

EchoBASEiEB0946.
EcoGeneiEG10953. sodA.

Phylogenomic databases

eggNOGiCOG0605.
HOGENOMiHOG000013583.
InParanoidiP00448.
KOiK04564.
OMAiKHHNAYT.
OrthoDBiEOG63NMNT.
PhylomeDBiP00448.

Enzyme and pathway databases

BioCyciEcoCyc:SUPEROX-DISMUTMN-MONOMER.
ECOL316407:JW3879-MONOMER.
MetaCyc:SUPEROX-DISMUTMN-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP00448.
PROiP00448.

Gene expression databases

GenevestigatoriP00448.

Family and domain databases

InterProiIPR001189. Mn/Fe_SOD.
IPR019833. Mn/Fe_SOD_BS.
IPR019832. Mn/Fe_SOD_C.
IPR019831. Mn/Fe_SOD_N.
[Graphical view]
PANTHERiPTHR11404. PTHR11404. 1 hit.
PfamiPF02777. Sod_Fe_C. 1 hit.
PF00081. Sod_Fe_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000349. SODismutase. 1 hit.
PRINTSiPR01703. MNSODISMTASE.
SUPFAMiSSF46609. SSF46609. 1 hit.
SSF54719. SSF54719. 1 hit.
PROSITEiPS00088. SOD_MN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structure and gene expression of the E. coli Mn-superoxide dismutase gene."
    Takeda Y., Avila H.
    Nucleic Acids Res. 14:4577-4589(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes."
    Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.
    Nucleic Acids Res. 21:3391-3398(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "The amino acid sequence of mangano superoxide dismutase from Escherichia coli B."
    Steinman H.M.
    J. Biol. Chem. 253:8708-8720(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-206.
    Strain: B.
  6. "Nucleotide sequence of the rhaR-sodA interval specifying rhaT in Escherichia coli."
    Garcia C., Baldoma L., Badia J., Aguilar J.
    J. Gen. Microbiol. 138:1109-1116(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-96.
    Strain: K12.
  7. "Mapping, cloning, expression, and sequencing of the rhaT gene, which encodes a novel L-rhamnose-H+ transport protein in Salmonella typhimurium and Escherichia coli."
    Tate C.G., Muiry J.A.R., Henderson P.J.F.
    J. Biol. Chem. 267:6923-6932(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-63.
    Strain: K12.
  8. "Transcriptional and posttranscriptional regulation of manganese superoxide dismutase biosynthesis in Escherichia coli, studied with operon and protein fusions."
    Touati D.
    J. Bacteriol. 170:2511-2520(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-2.
  9. Cited for: PROTEIN SEQUENCE OF 2-11.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  10. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-13.
    Strain: K12 / EMG2.
  11. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  12. "Outer sphere mutations perturb metal reactivity in manganese superoxide dismutase."
    Edwards R.A., Whittaker M.M., Whittaker J.W., Baker E.N., Jameson G.B.
    Biochemistry 40:15-27(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANTS PHE-35; LEU-147 AND HIS-147.
  13. "Removing a hydrogen bond in the dimer interface of Escherichia coli manganese superoxide dismutase alters structure and reactivity."
    Edwards R.A., Whittaker M.M., Whittaker J.W., Baker E.N., Jameson G.B.
    Biochemistry 40:4622-4632(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF MUTANTS ALA-31 AND PHE-175.
  14. "Paramagnetic NMR spectroscopy of native and cobalt substituted manganese superoxide dismutase from Escherichia coli."
    Renault J.P., Verchere-Beau R., Morgenstern-Badarau I., Piccioli M.
    FEBS Lett. 401:15-19(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  15. "Crystal structure of Escherichia coli manganese superoxide dismutase at 2.1-A resolution."
    Edwards R.A., Baker H.M., Whittaker M.M., Whittaker J.W., Jameson G.B., Baker E.N.
    J. Biol. Inorg. Chem. 3:161-171(1998)
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
  16. "Cryo-trapping the six-coordinate, distorted-octahedral active site of manganese superoxide dismutase."
    Borgstahl G.E., Pokross M., Chehab R., Sekher A., Snell E.H.
    J. Mol. Biol. 296:951-959(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS).

Entry informationi

Entry nameiSODM_ECOLI
AccessioniPrimary (citable) accession number: P00448
Secondary accession number(s): Q2M8K5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: January 7, 2015
This is version 151 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.