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P0AGD3

- SODF_ECOLI

UniProt

P0AGD3 - SODF_ECOLI

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Protein

Superoxide dismutase [Fe]

Gene
sodB, b1656, JW1648
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 + H2O2.1 Publication

Cofactori

Binds 1 iron ion per subunit.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi27 – 271Iron
Metal bindingi74 – 741Iron
Metal bindingi157 – 1571Iron
Metal bindingi161 – 1611Iron

GO - Molecular functioni

  1. iron ion binding Source: EcoCyc
  2. oxidoreductase activity Source: EcoliWiki
  3. superoxide dismutase activity Source: EcoCyc

GO - Biological processi

  1. oxidation-reduction process Source: EcoliWiki
  2. removal of superoxide radicals Source: EcoliWiki
  3. response to superoxide Source: EcoliWiki
  4. superoxide metabolic process Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Superoxide dismutase [Fe] (EC:1.15.1.1)
Gene namesi
Name:sodB
Ordered Locus Names:b1656, JW1648
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10954. sodB.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: EcoliWiki
  2. cytosol Source: UniProtKB
  3. membrane Source: UniProtKB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 193192Superoxide dismutase [Fe]PRO_0000159979Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei51 – 511N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP0AGD3.
PRIDEiP0AGD3.

2D gel databases

SWISS-2DPAGEP0AGD3.

Expressioni

Gene expression databases

GenevestigatoriP0AGD3.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

IntActiP0AGD3. 6 interactions.
STRINGi511145.b1656.

Structurei

Secondary structure

1
193
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni12 – 187
Helixi21 – 299
Helixi31 – 4313
Turni47 – 504
Helixi53 – 575
Helixi62 – 7918
Helixi91 – 10111
Helixi104 – 11714
Beta strandi120 – 1289
Beta strandi134 – 1407
Helixi145 – 1473
Beta strandi151 – 1577
Helixi160 – 1623
Helixi164 – 1674
Helixi171 – 1799
Helixi184 – 1929

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP0AGD3.
SMRiP0AGD3. Positions 2-193.

Miscellaneous databases

EvolutionaryTraceiP0AGD3.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0605.
HOGENOMiHOG000013584.
KOiK04564.
OMAiWTWLVKG.
OrthoDBiEOG63NMNT.
PhylomeDBiP0AGD3.

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.

P0AGD3-1 [UniParc]FASTAAdd to Basket

« Hide

MSFELPALPY AKDALAPHIS AETIEYHYGK HHQTYVTNLN NLIKGTAFEG    50
KSLEEIIRSS EGGVFNNAAQ VWNHTFYWNC LAPNAGGEPT GKVAEAIAAS 100
FGSFADFKAQ FTDAAIKNFG SGWTWLVKNS DGKLAIVSTS NAGTPLTTDA 150
TPLLTVDVWE HAYYIDYRNA RPGYLEHFWA LVNWEFVAKN LAA 193
Length:193
Mass (Da):21,266
Last modified:January 23, 2007 - v2
Checksum:i91236D2A8FE61474
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J03511 Genomic DNA. Translation: AAA24637.1.
U00096 Genomic DNA. Translation: AAC74728.1.
AP009048 Genomic DNA. Translation: BAA15422.1.
PIRiA29940. DSECF.
RefSeqiNP_416173.1. NC_000913.3.
YP_489920.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC74728; AAC74728; b1656.
BAA15422; BAA15422; BAA15422.
GeneIDi12931271.
944953.
KEGGiecj:Y75_p1633.
eco:b1656.
PATRICi32118616. VBIEscCol129921_1728.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J03511 Genomic DNA. Translation: AAA24637.1 .
U00096 Genomic DNA. Translation: AAC74728.1 .
AP009048 Genomic DNA. Translation: BAA15422.1 .
PIRi A29940. DSECF.
RefSeqi NP_416173.1. NC_000913.3.
YP_489920.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ISA X-ray 1.80 A/B 2-193 [» ]
1ISB X-ray 1.85 A/B 2-193 [» ]
1ISC X-ray 1.80 A/B 2-193 [» ]
1ZA5 X-ray 1.80 A/B 2-193 [» ]
2BKB X-ray 1.70 A/B/C/D 2-193 [» ]
2NYB X-ray 1.10 A/B/C/D 2-193 [» ]
ProteinModelPortali P0AGD3.
SMRi P0AGD3. Positions 2-193.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P0AGD3. 6 interactions.
STRINGi 511145.b1656.

2D gel databases

SWISS-2DPAGE P0AGD3.

Proteomic databases

PaxDbi P0AGD3.
PRIDEi P0AGD3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC74728 ; AAC74728 ; b1656 .
BAA15422 ; BAA15422 ; BAA15422 .
GeneIDi 12931271.
944953.
KEGGi ecj:Y75_p1633.
eco:b1656.
PATRICi 32118616. VBIEscCol129921_1728.

Organism-specific databases

EchoBASEi EB0947.
EcoGenei EG10954. sodB.

Phylogenomic databases

eggNOGi COG0605.
HOGENOMi HOG000013584.
KOi K04564.
OMAi WTWLVKG.
OrthoDBi EOG63NMNT.
PhylomeDBi P0AGD3.

Enzyme and pathway databases

BioCyci EcoCyc:SUPEROX-DISMUTFE-MONOMER.
ECOL316407:JW1648-MONOMER.
MetaCyc:SUPEROX-DISMUTFE-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0AGD3.
PROi P0AGD3.

Gene expression databases

Genevestigatori P0AGD3.

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. "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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  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 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. 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.

Entry informationi

Entry nameiSODF_ECOLI
AccessioniPrimary (citable) accession number: P0AGD3
Secondary accession number(s): P09157
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 80 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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