AGOG_METMP
ID AGOG_METMP Reviewed; 252 AA.
AC Q6M0G7;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=N-glycosylase/DNA lyase {ECO:0000255|HAMAP-Rule:MF_01168};
DE AltName: Full=8-oxoguanine DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_01168};
DE EC=3.2.2.- {ECO:0000255|HAMAP-Rule:MF_01168};
DE AltName: Full=AGOG {ECO:0000255|HAMAP-Rule:MF_01168};
DE AltName: Full=DNA-(apurinic or apyrimidinic site) lyase {ECO:0000255|HAMAP-Rule:MF_01168};
DE Short=AP lyase {ECO:0000255|HAMAP-Rule:MF_01168};
DE EC=4.2.99.18 {ECO:0000255|HAMAP-Rule:MF_01168};
GN OrderedLocusNames=MMP0304;
OS Methanococcus maripaludis (strain S2 / LL).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=267377;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2 / LL;
RX PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA Olson M.V., Leigh J.A.;
RT "Complete genome sequence of the genetically tractable hydrogenotrophic
RT methanogen Methanococcus maripaludis.";
RL J. Bacteriol. 186:6956-6969(2004).
CC -!- FUNCTION: DNA repair enzyme that is part of the base excision repair
CC (BER) pathway; protects from oxidative damage by removing the major
CC product of DNA oxidation, 8-oxoguanine (GO), from single- and double-
CC stranded DNA substrates. {ECO:0000255|HAMAP-Rule:MF_01168}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-
CC deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-
CC dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-
CC 2'-deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:66592, Rhea:RHEA-
CC COMP:13180, Rhea:RHEA-COMP:16897, Rhea:RHEA-COMP:17067,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:136412, ChEBI:CHEBI:157695,
CC ChEBI:CHEBI:167181; EC=4.2.99.18; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01168};
CC -!- DOMAIN: Contains two alpha-helical subdomains, with the 8-oxoguanine
CC binding site located in a cleft at their interface. Contains a helix-
CC hairpin-helix (HhH) structural motif and a Gly/Pro-rich sequence
CC followed by a conserved Asp (HhH-GPD motif).
CC -!- SIMILARITY: Belongs to the archaeal N-glycosylase/DNA lyase (AGOG)
CC family. {ECO:0000255|HAMAP-Rule:MF_01168}.
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DR EMBL; BX950229; CAF29860.1; -; Genomic_DNA.
DR RefSeq; WP_011170248.1; NC_005791.1.
DR AlphaFoldDB; Q6M0G7; -.
DR SMR; Q6M0G7; -.
DR STRING; 267377.MMP0304; -.
DR EnsemblBacteria; CAF29860; CAF29860; MMP0304.
DR GeneID; 2761855; -.
DR KEGG; mmp:MMP0304; -.
DR PATRIC; fig|267377.15.peg.307; -.
DR eggNOG; arCOG04144; Archaea.
DR HOGENOM; CLU_085935_0_0_2; -.
DR OMA; VKMFGYA; -.
DR OrthoDB; 108705at2157; -.
DR BioCyc; MMAR267377:MMP_RS01630-MON; -.
DR Proteomes; UP000000590; Chromosome.
DR GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0000702; F:oxidized base lesion DNA N-glycosylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006284; P:base-excision repair; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01168; AGOG; 1.
DR InterPro; IPR016544; AGOG.
DR InterPro; IPR015254; AGOG-like.
DR InterPro; IPR011257; DNA_glycosylase.
DR Pfam; PF09171; AGOG; 1.
DR PIRSF; PIRSF008955; AGOG; 1.
DR SUPFAM; SSF48150; SSF48150; 1.
PE 3: Inferred from homology;
KW DNA damage; DNA excision; DNA repair; Hydrolase; Lyase; Reference proteome.
FT CHAIN 1..252
FT /note="N-glycosylase/DNA lyase"
FT /id="PRO_0000185109"
FT REGION 129..193
FT /note="Helix-hairpin-helix"
FT ACT_SITE 153
FT /note="Schiff-base intermediate with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01168"
FT ACT_SITE 185
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01168"
FT BINDING 32
FT /ligand="8-oxoguanine"
FT /ligand_id="ChEBI:CHEBI:52617"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01168"
FT BINDING 60
FT /ligand="8-oxoguanine"
FT /ligand_id="ChEBI:CHEBI:52617"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01168"
FT BINDING 71
FT /ligand="8-oxoguanine"
FT /ligand_id="ChEBI:CHEBI:52617"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01168"
FT BINDING 157
FT /ligand="8-oxoguanine"
FT /ligand_id="ChEBI:CHEBI:52617"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01168"
FT BINDING 183
FT /ligand="8-oxoguanine"
FT /ligand_id="ChEBI:CHEBI:52617"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01168"
FT BINDING 219
FT /ligand="8-oxoguanine"
FT /ligand_id="ChEBI:CHEBI:52617"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01168"
FT BINDING 223
FT /ligand="8-oxoguanine"
FT /ligand_id="ChEBI:CHEBI:52617"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01168"
SQ SEQUENCE 252 AA; 30106 MW; 400E65728A8E63E9 CRC64;
MRNLEKINEL LEIFGHFDVN FAKTMEEKID TQYFVLENLK NSMNNDEMFI KLVILNSIVS
YQLCTTGELW WEEFSKYWSK HDANNENLGE SYVNFLENSK GNKRLLNVKI KRIERITPFL
ENLNLLDFKT YYSDMEKLLE NLSKYLNSKK NSKTVVFAVK MFGYASRIVF NEFFPYPMNI
EIPKDSRIEK YTLKFTDENP IKFWNEVSKT AKIPPLHIDS IIWPVLGRNF DFKSCENKLD
ENFRYLLKLT EL
