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Reviewed, UniProtKB/Swiss-Prot O58954 (AGOG_PYRHO)

Last modified November 3, 2009. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    N-glycosylase/DNA lyase
Alternative name(s):
    AGOG
    8-oxoguanine DNA glycosylase
    EC=3.2.2.-
    DNA-(apurinic or apyrimidinic site) lyase
      Short name=AP lyase
    EC=4.2.99.18
Gene names
Ordered Locus Names: PH1229
OrganismPyrococcus horikoshii [Complete proteome] [HAMAP]
Taxonomic identifier53953 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

Protein attributes

Sequence length239 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

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 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 MF_01168

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

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

Regions

Region118 – 18265Helix-hairpin-helix HAMAP 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
O58954-1 [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

[1]"Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3."
Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S., Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K., Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T. expand/collapse author list , Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T., Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.
DNA Res. 5:55-76(1998) [PubMed: 9679194] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: OT3.

Cross-references

Sequence databases

BA000001 Genomic DNA. Translation: BAA30329.1.
PIRG71066.
RefSeqNP_143123.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID1443551.
GenomeReviewsGene locus PH1229 in contig BA000001_GR.
KEGGpho:PH1229.
NMPDRfig|70601.1.peg.1204.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMO58954.
OMAPLHIDSI.

Enzyme and pathway databases

BRENDA4.2.99.18. 74679.

Family and domain databases

HAMAPMF_01168.
[Tree]
InterProIPR015254. N-Glyclase/DNA_lyase-like_arc.
IPR016544. N-Glyclase/DNA_lyase_arc.
[Graphical view]
PfamPF09171. DUF1886. 1 hit.
[Graphical view]
PIRSFPIRSF008955. AGOG. 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: November 3, 2009
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents