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Q9UZY0 (AGOG_PYRAB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 64. 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:PYRAB10170
ORF Names:PAB1695
OrganismPyrococcus abyssi (strain GE5 / Orsay) [Complete proteome] [HAMAP]
Taxonomic identifier272844 [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_0000185113

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
Q9UZY0 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 8C9F4D3656DEC791

FASTA23927,662
        10         20         30         40         50         60 
MIARIIGEIG IEGARFIEEN IDEQFKALRY LSKGIDSETF VKLVIANSLV SYQLTGKGEQ 

        70         80         90        100        110        120 
WWWEFAKYFY GRDVKSIYLA YKEFLPNSRF NRRLIPQKLS RIRRVETFLS TLTEERIEEY 

       130        140        150        160        170        180 
YGDMSSLWGS IARALGVDKE SKTVVFSVKM FGYAARIVLS TFNPYPMEIP IPEDSRIVKL 

       190        200        210        220        230 
TKKLTNEKPR KFWMKIARES GVPPLHIDSI LWPLLGGASI DSAPPELRDK LAELIKIIR 

« Hide

References

« Hide 'large scale' references
[1]"An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi."
Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O., Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J., Weissenbach J., Zivanovic Y., Forterre P.
Mol. Microbiol. 47:1495-1512(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GE5 / Orsay.
[2]"Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638."
Gao J., Wang J.
Curr. Microbiol. 64:118-129(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: GE5 / Orsay.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ248286 Genomic DNA. Translation: CAB49926.1.
HE613800 Genomic DNA. Translation: CCE70424.1.
PIRA75078.
RefSeqNP_126695.1. NC_000868.1.

3D structure databases

ProteinModelPortalQ9UZY0.
SMRQ9UZY0. Positions 2-238.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272844.PAB1695.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB49926; CAB49926; PAB1695.
GeneID1496368.
KEGGpab:PAB1695.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG4047.
HOGENOMHOG000254352.
KOK01741.
OMAVKMFGYA.

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_PYRAB
AccessionPrimary (citable) accession number: Q9UZY0
Secondary accession number(s): G8ZII3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: May 1, 2000
Last modified: May 14, 2014
This is version 64 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