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Q6M0G7 (AGOG_METMP) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 53. 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:MMP0304
OrganismMethanococcus maripaludis (strain S2 / LL) [Complete proteome] [HAMAP]
Taxonomic identifier267377 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanococciMethanococcalesMethanococcaceaeMethanococcus

Protein attributes

Sequence length252 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 – 252252N-glycosylase/DNA lyase HAMAP-Rule MF_01168
PRO_0000185109

Regions

Region129 – 19365Helix-hairpin-helix HAMAP-Rule MF_01168

Sites

Active site1531Schiff-base intermediate with DNA By similarity
Active site1851 Potential
Binding site3218-oxoguanine By similarity
Binding site6018-oxoguanine; via carbonyl oxygen By similarity
Binding site7118-oxoguanine By similarity
Binding site15718-oxoguanine By similarity
Binding site18318-oxoguanine; via carbonyl oxygen By similarity
Binding site21918-oxoguanine By similarity
Binding site22318-oxoguanine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6M0G7 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 400E65728A8E63E9

FASTA25230,106
        10         20         30         40         50         60 
MRNLEKINEL LEIFGHFDVN FAKTMEEKID TQYFVLENLK NSMNNDEMFI KLVILNSIVS 

        70         80         90        100        110        120 
YQLCTTGELW WEEFSKYWSK HDANNENLGE SYVNFLENSK GNKRLLNVKI KRIERITPFL 

       130        140        150        160        170        180 
ENLNLLDFKT YYSDMEKLLE NLSKYLNSKK NSKTVVFAVK MFGYASRIVF NEFFPYPMNI 

       190        200        210        220        230        240 
EIPKDSRIEK YTLKFTDENP IKFWNEVSKT AKIPPLHIDS IIWPVLGRNF DFKSCENKLD 

       250 
ENFRYLLKLT EL 

« Hide

References

[1]"Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis."
Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J., Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M., Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A., Moore B.C. expand/collapse author list , Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D., Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W., Olson M.V., Leigh J.A.
J. Bacteriol. 186:6956-6969(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: S2 / LL.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX950229 Genomic DNA. Translation: CAF29860.1.
RefSeqNP_987424.1. NC_005791.1.

3D structure databases

ProteinModelPortalQ6M0G7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING267377.MMP0304.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAF29860; CAF29860; MMP0304.
GeneID2761855.
KEGGmmp:MMP0304.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG4047.
HOGENOMHOG000254352.
KOK01741.
OMAVKMFGYA.
ProtClustDBPRK13280.

Enzyme and pathway databases

BioCycMMAR267377:GJ77-326-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_METMP
AccessionPrimary (citable) accession number: Q6M0G7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: July 5, 2004
Last modified: February 19, 2014
This is version 53 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