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P0AGD3 (SODF_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Superoxide dismutase [Fe]

EC=1.15.1.1
Gene names
Name:sodB
Ordered Locus Names:b1656, JW1648
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length193 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

2 superoxide + 2 H+ = O2 + H2O2. Ref.9

Cofactor

Binds 1 iron ion per subunit. Ref.9

Subunit structure

Homodimer. Ref.12

Sequence similarities

Belongs to the iron/manganese superoxide dismutase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5 Ref.7 Ref.8
Chain2 – 193192Superoxide dismutase [Fe]
PRO_0000159979

Sites

Metal binding271Iron
Metal binding741Iron
Metal binding1571Iron
Metal binding1611Iron

Amino acid modifications

Modified residue511N6-acetyllysine Ref.11

Secondary structure

................................. 193
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0AGD3 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 91236D2A8FE61474

FASTA19321,266
        10         20         30         40         50         60 
MSFELPALPY AKDALAPHIS AETIEYHYGK HHQTYVTNLN NLIKGTAFEG KSLEEIIRSS 

        70         80         90        100        110        120 
EGGVFNNAAQ VWNHTFYWNC LAPNAGGEPT GKVAEAIAAS FGSFADFKAQ FTDAAIKNFG 

       130        140        150        160        170        180 
SGWTWLVKNS DGKLAIVSTS NAGTPLTTDA TPLLTVDVWE HAYYIDYRNA RPGYLEHFWA 

       190 
LVNWEFVAKN LAA 

« Hide

References

« Hide 'large scale' references
[1]"Iron superoxide dismutase. Nucleotide sequence of the gene from Escherichia coli K12 and correlations with crystal structures."
Carlioz A., Ludwig M.L., Stallings W.C., Fee J.A., Steinman H.M., Touati D.
J. Biol. Chem. 263:1555-1562(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: K12.
[2]"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map."
Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. expand/collapse author list , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.
DNA Res. 3:363-377(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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 primary structure of iron superoxide dismutase from Escherichia coli."
Schinina M.E., Maffey L., Barra D., Bossa F., Puget K., Michelson A.M.
FEBS Lett. 221:87-90(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-193.
[6]"Sequence homologies among bacterial and mitochondrial superoxide dismutases."
Steinman H.M., Hill R.L.
Proc. Natl. Acad. Sci. U.S.A. 70:3725-3729(1973) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE.
[7]"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.
[8]"Protein identification with N and C-terminal sequence tags in proteome projects."
Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C., Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L., Hochstrasser D.F.
J. Mol. Biol. 278:599-608(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-5.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[9]"Spectroscopic measurement of a long-predicted active site pK in iron-superoxide dismutase from Escherichia coli."
Sorkin D.L., Miller A.-F.
Biochemistry 36:4916-4924(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, COFACTOR.
[10]"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.
[11]"Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-51, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
[12]"Iron superoxide dismutase from Escherichia coli at 3.1-A resolution: a structure unlike that of copper/zinc protein at both monomer and dimer levels."
Stallings W.C., Powers T.B., Pattridge K.A., Fee J.A., Ludwig M.L.
Proc. Natl. Acad. Sci. U.S.A. 80:3884-3888(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH IRON ION, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J03511 Genomic DNA. Translation: AAA24637.1.
U00096 Genomic DNA. Translation: AAC74728.1.
AP009048 Genomic DNA. Translation: BAA15422.1.
PIRDSECF. A29940.
RefSeqNP_416173.1. NC_000913.3.
YP_489920.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ISAX-ray1.80A/B2-193[»]
1ISBX-ray1.85A/B2-193[»]
1ISCX-ray1.80A/B2-193[»]
1ZA5X-ray1.80A/B2-193[»]
2BKBX-ray1.70A/B/C/D2-193[»]
2NYBX-ray1.10A/B/C/D2-193[»]
ProteinModelPortalP0AGD3.
SMRP0AGD3. Positions 2-193.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP0AGD3. 6 interactions.
STRING511145.b1656.

2D gel databases

SWISS-2DPAGEP0AGD3.

Proteomic databases

PaxDbP0AGD3.
PRIDEP0AGD3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74728; AAC74728; b1656.
BAA15422; BAA15422; BAA15422.
GeneID12931271.
944953.
KEGGecj:Y75_p1633.
eco:b1656.
PATRIC32118616. VBIEscCol129921_1728.

Organism-specific databases

EchoBASEEB0947.
EcoGeneEG10954. sodB.

Phylogenomic databases

eggNOGCOG0605.
HOGENOMHOG000013584.
KOK04564.
OMADYVLERY.
OrthoDBEOG63NMNT.
PhylomeDBP0AGD3.
ProtClustDBPRK10543.

Enzyme and pathway databases

BioCycEcoCyc:SUPEROX-DISMUTFE-MONOMER.
ECOL316407:JW1648-MONOMER.
MetaCyc:SUPEROX-DISMUTFE-MONOMER.

Gene expression databases

GenevestigatorP0AGD3.

Family and domain databases

InterProIPR001189. Mn/Fe_SOD.
IPR019833. Mn/Fe_SOD_BS.
IPR019832. Mn/Fe_SOD_C.
IPR019831. Mn/Fe_SOD_N.
[Graphical view]
PANTHERPTHR11404. PTHR11404. 1 hit.
PfamPF02777. Sod_Fe_C. 1 hit.
PF00081. Sod_Fe_N. 1 hit.
[Graphical view]
PIRSFPIRSF000349. SODismutase. 1 hit.
PRINTSPR01703. MNSODISMTASE.
SUPFAMSSF46609. SSF46609. 1 hit.
SSF54719. SSF54719. 1 hit.
PROSITEPS00088. SOD_MN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0AGD3.
PROP0AGD3.

Entry information

Entry nameSODF_ECOLI
AccessionPrimary (citable) accession number: P0AGD3
Secondary accession number(s): P09157
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 79 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene