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P00448

- SODM_ECOLI

UniProt

P00448 - SODM_ECOLI

Protein

Superoxide dismutase [Mn]

Gene

sodA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    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

    Binds 1 manganese 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

    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

    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 – 187
    Helixi21 – 299
    Helixi31 – 4313
    Helixi47 – 504
    Helixi54 – 574
    Helixi61 – 633
    Helixi66 – 683
    Helixi69 – 8719
    Helixi97 – 10711
    Helixi110 – 12314
    Beta strandi126 – 13510
    Beta strandi138 – 1458
    Helixi150 – 1523
    Helixi154 – 1574
    Beta strandi161 – 1688
    Helixi171 – 1733
    Helixi175 – 1784
    Helixi182 – 19211
    Helixi195 – 20511

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    KOiK04564.
    OMAiPLPYDYN.
    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

    MSYTLPSLPY AYDALEPHFD KQTMEIHHTK HHQTYVNNAN AALESLPEFA    50
    NLPVEELITK LDQLPADKKT VLRNNAGGHA NHSLFWKGLK KGTTLQGDLK 100
    AAIERDFGSV DNFKAEFEKA AASRFGSGWA WLVLKGDKLA VVSTANQDSP 150
    LMGEAISGAS GFPIMGLDVW EHAYYLKFQN RRPDYIKEFW NVVNWDEAAA 200
    RFAAKK 206
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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.
    PIRi A24141. DSECN.
    RefSeqi NP_418344.3. NC_000913.3.
    YP_491542.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1D5N X-ray 1.55 A/B/C/D 2-206 [» ]
    1EN4 X-ray 2.00 A/B/C/D 2-206 [» ]
    1EN5 X-ray 2.30 A/B/C/D 2-206 [» ]
    1EN6 X-ray 2.00 A/B/C/D 2-206 [» ]
    1I08 X-ray 2.20 A/B/C/D 2-206 [» ]
    1I0H X-ray 1.35 A/B 2-206 [» ]
    1IX9 X-ray 0.90 A/B 2-206 [» ]
    1IXB X-ray 0.90 A/B 2-206 [» ]
    1MMM X-ray 2.20 A/B 2-206 [» ]
    1VEW X-ray 2.10 A/B/C/D 2-206 [» ]
    1ZLZ X-ray 1.55 A/B 2-206 [» ]
    3K9S X-ray 1.55 A/B/C/D 2-206 [» ]
    3OT7 X-ray 1.90 A/B/C/D 2-206 [» ]
    ProteinModelPortali P00448.
    SMRi P00448. Positions 2-206.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P00448. 7 interactions.
    STRINGi 511145.b3908.

    2D gel databases

    SWISS-2DPAGE P00448.

    Proteomic databases

    PaxDbi P00448.
    PRIDEi P00448.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76890 ; AAC76890 ; b3908 .
    BAE77401 ; BAE77401 ; BAE77401 .
    GeneIDi 12933233.
    948403.
    KEGGi ecj:Y75_p3278.
    eco:b3908.
    PATRICi 32123327. VBIEscCol129921_4024.

    Organism-specific databases

    EchoBASEi EB0946.
    EcoGenei EG10953. sodA.

    Phylogenomic databases

    eggNOGi COG0605.
    HOGENOMi HOG000013583.
    KOi K04564.
    OMAi PLPYDYN.
    OrthoDBi EOG63NMNT.
    PhylomeDBi P00448.

    Enzyme and pathway databases

    BioCyci EcoCyc:SUPEROX-DISMUTMN-MONOMER.
    ECOL316407:JW3879-MONOMER.
    MetaCyc:SUPEROX-DISMUTMN-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P00448.
    PROi P00448.

    Gene expression databases

    Genevestigatori P00448.

    Family and domain databases

    InterProi IPR001189. Mn/Fe_SOD.
    IPR019833. Mn/Fe_SOD_BS.
    IPR019832. Mn/Fe_SOD_C.
    IPR019831. Mn/Fe_SOD_N.
    [Graphical view ]
    PANTHERi PTHR11404. PTHR11404. 1 hit.
    Pfami PF02777. Sod_Fe_C. 1 hit.
    PF00081. Sod_Fe_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000349. SODismutase. 1 hit.
    PRINTSi PR01703. MNSODISMTASE.
    SUPFAMi SSF46609. SSF46609. 1 hit.
    SSF54719. SSF54719. 1 hit.
    PROSITEi PS00088. SOD_MN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 148 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