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A4YHC9 (OGG1_METS5) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
Probable N-glycosylase/DNA lyase

Including the following 2 domains:

  1. 8-oxoguanine DNA glycosylase
    EC=3.2.2.-
  2. DNA-(apurinic or apyrimidinic site) lyase
    Short name=AP lyase
    EC=4.2.99.18
Gene names
Name:ogg
Ordered Locus Names:Msed_1676
OrganismMetallosphaera sedula (strain ATCC 51363 / DSM 5348) [Complete proteome] [HAMAP]
Taxonomic identifier399549 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeMetallosphaera

Protein attributes

Sequence length201 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Responsible for removing an oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine = 7-oxoG) from DNA. Also nicks DNA at apurinic/apyrimidinic sites (AP sites) By similarity. HAMAP-Rule MF_00241

Catalytic activity

The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate. HAMAP-Rule MF_00241

Sequence similarities

Belongs to the type-2 OGG1 family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 201201Probable N-glycosylase/DNA lyase HAMAP-Rule MF_00241
PRO_1000071834

Sites

Active site1261 By similarity

Sequences

Sequence LengthMass (Da)Tools
A4YHC9 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: CF5A8E7C4E5936A1

FASTA20123,384
        10         20         30         40         50         60 
MLRKVVRDAR LRARVLERVE EFRLNKRASE RVWFRELVLC ILTANSSFIG AFTALQYLGD 

        70         80         90        100        110        120 
LILYGSIEEI SSALKNAGYR FPNLKARYII ESRSYYGKLR EIGRVADRDQ IEAREILLEI 

       130        140        150        160        170        180 
KGLGMKEASH FLRNMGYLDL AIIDRHILRF FSDYLEDQKI SSKSKYFELE SVFRSIASAL 

       190        200 
DLPVGVLDLY VWYLKTGKLA K 

« Hide

References

[1]"The genome sequence of the metal-mobilizing, extremely thermoacidophilic archaeon Metallosphaera sedula provides insights into bioleaching-associated metabolism."
Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.
Appl. Environ. Microbiol. 74:682-692(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51363 / DSM 5348.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000682 Genomic DNA. Translation: ABP95831.1.
RefSeqYP_001191755.1. NC_009440.1.

3D structure databases

ProteinModelPortalA4YHC9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING399549.Msed_1676.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABP95831; ABP95831; Msed_1676.
GeneID5105322.
KEGGmse:Msed_1676.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1059.
HOGENOMHOG000224507.
KOK03653.
OMALDLYLWY.

Enzyme and pathway databases

BioCycMSED399549:GH1O-1699-MONOMER.

Family and domain databases

Gene3D1.10.340.30. 1 hit.
HAMAPMF_00241. Ogg.
InterProIPR012092. DNA_glyclase/DNA_lyase_thermo.
IPR011257. DNA_glycosylase.
IPR003265. HhH-GPD_domain.
[Graphical view]
PIRSFPIRSF005954. Thrmst_ogg. 1 hit.
SMARTSM00478. ENDO3c. 1 hit.
[Graphical view]
SUPFAMSSF48150. SSF48150. 1 hit.
ProtoNetSearch...

Entry information

Entry nameOGG1_METS5
AccessionPrimary (citable) accession number: A4YHC9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: May 29, 2007
Last modified: May 14, 2014
This is version 37 of the entry and version 1 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