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H2GQF6 (H2GQF6_CORDB) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 13. 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 attributes

Sequence length199 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.

Catalytic activity

2 superoxide + 2 H+ = O2 + H2O2.

Sequence similarities

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

Ontologies

Keywords
   Molecular functionOxidoreductase RuleBase RU000414 EMBL AEX49760.1
   Technical termComplete proteome
Gene Ontology (GO)
   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
H2GQF6 [UniParc].

Last modified March 21, 2012. Version 1.
Checksum: 2CCDBB82205ACB42

FASTA19921,947
        10         20         30         40         50         60 
MTYTLPELDY AYDALEPHIA AEIMELHHSK HHANYVNGAN TALEKLQKAR ENGEIGAVVT 

        70         80         90        100        110        120 
ALSKDLAFNL GGHTNHSIFW KNLSPNGGGE PTGALAEAIA KEFGSFEKFK DHFSAAALGL 

       130        140        150        160        170        180 
QGSGWAVLGY DHIGGRLVIE QLTDQQGNIS ANLTPLLMLD MWEHAFYLQY KNVKADYVKA 

       190 
VWNVFNWDDV AARFEAATK 

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References

[1]"Pangenomic Study of Corynebacterium diphtheriae That Provides Insights into the Genomic Diversity of Pathogenic Isolates from Cases of Classical Diphtheria, Endocarditis, and Pneumonia."
Trost E., Blom J., de Castro Soares S., Huang I.H., Al-Dilaimi A., Schroder J., Jaenicke S., Dorella F.A., Rocha F.S., Miyoshi A., Azevedo V., Schneider M.P., Silva A., Camello T.C., Sabbadini P.S., Santos C.S., Santos L.S., Hirata R.Jr. expand/collapse author list , Mattos-Guaraldi A.L., Efstratiou A., Schmitt M.P., Ton-That H., Tauch A.
J. Bacteriol. 194:3199-3215(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BH8 EMBL AEX49760.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP003209 Genomic DNA. Translation: AEX49760.1.
RefSeqYP_005161327.1. NC_016800.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEX49760; AEX49760; CDBH8_2247.
GeneID11734688.
KEGGcdb:CDBH8_2247.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK04564.

Enzyme and pathway databases

BioCycCDIP698973:GHAI-2305-MONOMER.

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 nameH2GQF6_CORDB
AccessionPrimary (citable) accession number: H2GQF6
Entry history
Integrated into UniProtKB/TrEMBL: March 21, 2012
Last sequence update: March 21, 2012
Last modified: July 9, 2014
This is version 13 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)