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C6EEY9 (C6EEY9_ECOBD) Unreviewed, UniProtKB/TrEMBL

Last modified April 16, 2014. Version 31. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Superoxide dismutase RuleBase RU000414

EC=1.15.1.1 RuleBase RU000414
Gene names
Name:sodA EMBL ACT45587.1
Ordered Locus Names:B21_03743 EMBL CAQ34260.1, ECBD_4115 EMBL ACT31098.1, ECD_03794 EMBL ACT45587.1
OrganismEscherichia coli (strain B / BL21-DE3) [Complete proteome] [HAMAP]
Taxonomic identifier469008 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length206 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Destroys radicals which are normally produced within the cells and which are toxic to biological systems By similarity. RuleBase RU000414

Catalytic activity

2 superoxide + 2 H+ = O2 + H2O2. RuleBase RU000414

Sequence similarities

Belongs to the iron/manganese superoxide dismutase family. RuleBase RU004477

Ontologies

Keywords
   Molecular functionOxidoreductase RuleBase RU000414 EMBL ACT31098.1
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processsuperoxide metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: InterPro

superoxide dismutase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequences

Sequence LengthMass (Da)Tools
C6EEY9 [UniParc].

Last modified September 1, 2009. Version 1.
Checksum: 082CFE13FF3C15CC

FASTA20623,079
        10         20         30         40         50         60 
MSYTLPSLPY AYDALEPHFD KQTMEIHHTK HHQTYVNNAN AALESLPEFA NLPVEELITK 

        70         80         90        100        110        120 
LDQLPADKKT VLRNNAGGHA NHSLFWKGLK KGTTLQGDLK AAIERDFGSV DNFKAEFEKA 

       130        140        150        160        170        180 
AASRFGSGWA WLVLKGDKLA VVSTANQDSP LMGEAISGAS GFPILGLDVW EHAYYLKFQN 

       190        200 
RRPDYIKEFW NVVNWDEAAA RFAAKK 

« Hide

References

« Hide 'large scale' references
[1]"Sequencing and gene expression analysis of Escherichia coli BL21(DE3)."
Krempl P.M., Mairhofer J., Eisenkolb M., Specht T., Leparc G.G., Kreil D.P., Bayer K., Striedner G.
Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: BL21 EMBL CAQ34260.1.
[2]"Genome sequences of Escherichia coli B strains REL606 and BL21(DE3)."
Jeong H., Barbe V., Lee C.H., Vallenet D., Yu D.S., Choi S.H., Couloux A., Lee S.W., Yoon S.H., Cattolico L., Hur C.G., Park H.S., Segurens B., Kim S.C., Oh T.K., Lenski R.E., Studier F.W., Daegelen P., Kim J.F.
J. Mol. Biol. 394:644-652(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: B / BL21-DE3 [Korea] and BL21 EMBL ACT45587.1.
[3]"Sequencing and gene expression analysis of Escherichia coli BL21."
Leparc G., Striedner G., Bayer K., Kreil D., Krempl P.M.
Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: B / BL21-DE3 [Austria].
[4]"Complete sequence of Escherichia coli 'BL21-Gold(DE3)pLysS AG'."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., LaButti K.M., Clum A., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I., Sorek R., Rubin E.
Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: BL21-Gold EMBL ACT31098.1.
[5]"Complete sequence of Escherichia coli BL21(DE3)."
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., LaButti K.M., Clum A., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I., Sorek R., Rubin E.
Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: B / BL21-DE3 [JGI].
[6]Jeong H., Shim J.-H., Studier F.W., Oh T.K., Kim J.F.
Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: BL21.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001665 Genomic DNA. Translation: ACT31098.1.
CP001509 Genomic DNA. Translation: ACT45587.1.
AM946981 Genomic DNA. Translation: CAQ34260.1.
RefSeqYP_003001476.1. NC_012892.2.
YP_003038283.1. NC_012947.1.
YP_003056358.1. NC_012971.2.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING469008.ECBD_4115.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACT31098; ACT31098; ECBD_4115.
ACT45587; ACT45587; ECD_03794.
CAQ34260; CAQ34260; B21_03743.
GeneID8113849.
8158545.
8183499.
KEGGebd:ECBD_4115.
ebe:B21_03743.
ebl:ECD_03794.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0605.
HOGENOMHOG000013583.
KOK04564.
OMADYISAFW.
ProtClustDBPRK10925.

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...

Entry information

Entry nameC6EEY9_ECOBD
AccessionPrimary (citable) accession number: C6EEY9
Secondary accession number(s): C5WBE9
Entry history
Integrated into UniProtKB/TrEMBL: September 1, 2009
Last sequence update: September 1, 2009
Last modified: April 16, 2014
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)