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P00448

- SODM_ECOLI

UniProt

P00448 - SODM_ECOLI

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Protein
Superoxide dismutase [Mn]
Gene
sodA, b3908, JW3879
Organism
Escherichia coli (strain K12)
Status
Reviewed - 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

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. DNA binding Source: EcoCyc
  2. antioxidant activity 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 acidity 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

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.

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

Natural variant

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti81 – 822NH → HN1 Publication

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

« 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: May 14, 2014
This is version 147 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

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