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O58954 (AGOG_PYRHO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 68. 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:
N-glycosylase/DNA lyase
Alternative name(s):
8-oxoguanine DNA glycosylase
EC=3.2.2.-
AGOG
DNA-(apurinic or apyrimidinic site) lyase
Short name=AP lyase
EC=4.2.99.18
Gene names
Ordered Locus Names:PH1229
OrganismPyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) [Complete proteome] [HAMAP]
Taxonomic identifier70601 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

Protein attributes

Sequence length239 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

DNA repair enzyme that is part of the base excision repair (BER) pathway; protects from oxidative damage by removing the major product of DNA oxidation, 8-oxoguanine (GO), from single- and double-stranded DNA substrates By similarity. HAMAP-Rule MF_01168

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_01168

Domain

Contains two alpha-helical subdomains, with the 8-oxoguanine binding site located in a cleft at their interface. Contains a helix-hairpin-helix (HhH) structural motif and a Gly/Pro-rich sequence followed by a conserved Asp (HhH-GPD motif). HAMAP-Rule MF_01168

Sequence similarities

Belongs to the archaeal N-glycosylase/DNA lyase (AGOG) family.

Ontologies

Keywords
   Biological processDNA damage
DNA excision
DNA repair
   Molecular functionHydrolase
Lyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processbase-excision repair

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functionDNA-(apurinic or apyrimidinic site) lyase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

oxidized base lesion DNA N-glycosylase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 239239N-glycosylase/DNA lyase HAMAP-Rule MF_01168
PRO_0000185115

Regions

Region118 – 18265Helix-hairpin-helix HAMAP-Rule MF_01168

Sites

Active site1421Schiff-base intermediate with DNA By similarity
Active site1741 Potential
Binding site2418-oxoguanine By similarity
Binding site5118-oxoguanine; via carbonyl oxygen By similarity
Binding site6218-oxoguanine By similarity
Binding site14618-oxoguanine By similarity
Binding site17218-oxoguanine; via carbonyl oxygen By similarity
Binding site20818-oxoguanine By similarity
Binding site21218-oxoguanine By similarity

Sequences

Sequence LengthMass (Da)Tools
O58954 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 5EC26389EBB5B99E

FASTA23928,191
        10         20         30         40         50         60 
MIAELIREIG IEGARFIEEN IDEQFKALSY LSEGMDRVNF VRLVIANALV SYQLTGKGEM 

        70         80         90        100        110        120 
WWWEFAKYFK GKEVKTIYSA YKEFLPNSKF NRRLIQQKLL RIKKIEPFLS TLTEESIERY 

       130        140        150        160        170        180 
YEDMTLLWKA IAKVLKVDRE SKTVVFSVKM FGYAARIVLS KFNPYPMEIP IPEDVRIIKL 

       190        200        210        220        230 
TRKLTNERPR DFWMKIAKES NVPPLHIDSI LWPLLGGARV EEAPPELKEK LEKLIRVIR 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000001 Genomic DNA. Translation: BAA30329.1.
PIRG71066.
RefSeqNP_143123.1. NC_000961.1.

3D structure databases

ProteinModelPortalO58954.
SMRO58954. Positions 2-238.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING70601.PH1229.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAA30329; BAA30329; BAA30329.
GeneID1443551.
KEGGpho:PH1229.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG4047.
HOGENOMHOG000254352.
KOK01741.
OMAVKMFGYA.
ProtClustDBPRK13280.

Enzyme and pathway databases

BioCycPHOR70601:GJWR-1224-MONOMER.

Family and domain databases

Gene3D1.10.1670.10. 1 hit.
1.10.340.30. 1 hit.
HAMAPMF_01168. AGOG.
InterProIPR011257. DNA_glycosylase.
IPR023170. HTH_base_excis_C.
IPR015254. N-Glyclase/DNA_lyase-like_arc.
IPR016544. N-Glyclase/DNA_lyase_arc.
[Graphical view]
PfamPF09171. DUF1886. 1 hit.
[Graphical view]
PIRSFPIRSF008955. AGOG. 1 hit.
SUPFAMSSF48150. SSF48150. 1 hit.
ProtoNetSearch...

Entry information

Entry nameAGOG_PYRHO
AccessionPrimary (citable) accession number: O58954
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: August 1, 1998
Last modified: February 19, 2014
This is version 68 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