AGOG_PYRAB
ID AGOG_PYRAB Reviewed; 239 AA.
AC Q9UZY0; G8ZII3;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=PYRAB10170; ORFNames=PAB1695;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
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; AJ248286; CAB49926.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE70424.1; -; Genomic_DNA.
DR PIR; A75078; A75078.
DR RefSeq; WP_010868134.1; NC_000868.1.
DR AlphaFoldDB; Q9UZY0; -.
DR SMR; Q9UZY0; -.
DR STRING; 272844.PAB1695; -.
DR EnsemblBacteria; CAB49926; CAB49926; PAB1695.
DR GeneID; 1496368; -.
DR KEGG; pab:PAB1695; -.
DR PATRIC; fig|272844.11.peg.1069; -.
DR eggNOG; arCOG04144; Archaea.
DR HOGENOM; CLU_085935_0_0_2; -.
DR OMA; VKMFGYA; -.
DR OrthoDB; 108705at2157; -.
DR PhylomeDB; Q9UZY0; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; 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.
FT CHAIN 1..239
FT /note="N-glycosylase/DNA lyase"
FT /id="PRO_0000185113"
FT REGION 118..182
FT /note="Helix-hairpin-helix"
FT ACT_SITE 142
FT /note="Schiff-base intermediate with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01168"
FT ACT_SITE 174
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01168"
FT BINDING 24
FT /ligand="8-oxoguanine"
FT /ligand_id="ChEBI:CHEBI:52617"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01168"
FT BINDING 51
FT /ligand="8-oxoguanine"
FT /ligand_id="ChEBI:CHEBI:52617"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01168"
FT BINDING 62
FT /ligand="8-oxoguanine"
FT /ligand_id="ChEBI:CHEBI:52617"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01168"
FT BINDING 146
FT /ligand="8-oxoguanine"
FT /ligand_id="ChEBI:CHEBI:52617"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01168"
FT BINDING 172
FT /ligand="8-oxoguanine"
FT /ligand_id="ChEBI:CHEBI:52617"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01168"
FT BINDING 208
FT /ligand="8-oxoguanine"
FT /ligand_id="ChEBI:CHEBI:52617"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01168"
FT BINDING 212
FT /ligand="8-oxoguanine"
FT /ligand_id="ChEBI:CHEBI:52617"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01168"
SQ SEQUENCE 239 AA; 27662 MW; 8C9F4D3656DEC791 CRC64;
MIARIIGEIG IEGARFIEEN IDEQFKALRY LSKGIDSETF VKLVIANSLV SYQLTGKGEQ
WWWEFAKYFY GRDVKSIYLA YKEFLPNSRF NRRLIPQKLS RIRRVETFLS TLTEERIEEY
YGDMSSLWGS IARALGVDKE SKTVVFSVKM FGYAARIVLS TFNPYPMEIP IPEDSRIVKL
TKKLTNEKPR KFWMKIARES GVPPLHIDSI LWPLLGGASI DSAPPELRDK LAELIKIIR
