AGOG_PYRAE
ID AGOG_PYRAE Reviewed; 256 AA.
AC Q8ZVK6;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=N-glycosylase/DNA lyase;
DE AltName: Full=8-oxoguanine DNA glycosylase;
DE EC=3.2.2.-;
DE AltName: Full=AGOG;
DE AltName: Full=DNA-(apurinic or apyrimidinic site) lyase;
DE Short=AP lyase;
DE EC=4.2.99.18;
DE AltName: Full=Pa-AGOG;
GN OrderedLocusNames=PAE2237;
OS Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS 104966 / NBRC 100827 / IM2).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=178306;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX PubMed=11792869; DOI=10.1073/pnas.241636498;
RA Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA Miller J.H.;
RT "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT aerophilum.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF LYS-140; LYS-147; ASP-166 AND ASP-172.
RX PubMed=15604455; DOI=10.1093/nar/gkh995;
RA Sartori A.A., Lingaraju G.M., Hunziker P., Winkler F.K., Jiricny J.;
RT "Pa-AGOG, the founding member of a new family of archaeal 8-oxoguanine DNA-
RT glycosylases.";
RL Nucleic Acids Res. 32:6531-6539(2004).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH
RP 8-OXOGUANOSINE, AND DOMAIN.
RX PubMed=15642264; DOI=10.1016/j.str.2004.10.011;
RA Lingaraju G.M., Sartori A.A., Kostrewa D., Prota A.E., Jiricny J.,
RA Winkler F.K.;
RT "A DNA glycosylase from Pyrobaculum aerophilum with an 8-oxoguanine binding
RT mode and a noncanonical helix-hairpin-helix structure.";
RL Structure 13:87-98(2005).
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:0000269|PubMed:15604455}.
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;
CC Evidence={ECO:0000269|PubMed:15604455};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Highly thermostable. No decrease in activity was observed after
CC heating 15 minutes at 80 degrees Celsius.
CC {ECO:0000269|PubMed:15604455};
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 {ECO:0000269|PubMed:15642264}.
CC -!- SIMILARITY: Belongs to the archaeal N-glycosylase/DNA lyase (AGOG)
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE009441; AAL64050.1; -; Genomic_DNA.
DR PDB; 1XQO; X-ray; 1.03 A; A=1-256.
DR PDB; 1XQP; X-ray; 1.69 A; A=1-256.
DR PDBsum; 1XQO; -.
DR PDBsum; 1XQP; -.
DR AlphaFoldDB; Q8ZVK6; -.
DR SMR; Q8ZVK6; -.
DR STRING; 178306.PAE2237; -.
DR EnsemblBacteria; AAL64050; AAL64050; PAE2237.
DR KEGG; pai:PAE2237; -.
DR PATRIC; fig|178306.9.peg.1663; -.
DR eggNOG; arCOG04144; Archaea.
DR HOGENOM; CLU_085935_0_0_2; -.
DR InParanoid; Q8ZVK6; -.
DR OMA; VKMFGYA; -.
DR BRENDA; 3.2.2.B5; 5239.
DR BRENDA; 4.2.99.18; 5239.
DR EvolutionaryTrace; Q8ZVK6; -.
DR Proteomes; UP000002439; 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 Gene3D; 1.10.1670.10; -; 1.
DR HAMAP; MF_01168; AGOG; 1.
DR InterPro; IPR016544; AGOG.
DR InterPro; IPR015254; AGOG-like.
DR InterPro; IPR011257; DNA_glycosylase.
DR InterPro; IPR023170; HhH_base_excis_C.
DR Pfam; PF09171; AGOG; 1.
DR PIRSF; PIRSF008955; AGOG; 1.
DR SUPFAM; SSF48150; SSF48150; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA damage; DNA excision; DNA repair; Hydrolase; Lyase;
KW Reference proteome.
FT CHAIN 1..256
FT /note="N-glycosylase/DNA lyase"
FT /id="PRO_0000185112"
FT REGION 125..184
FT /note="Helix-hairpin-helix"
FT ACT_SITE 140
FT /note="Schiff-base intermediate with DNA"
FT ACT_SITE 172
FT /evidence="ECO:0000255"
FT BINDING 31
FT /ligand="8-oxoguanine"
FT /ligand_id="ChEBI:CHEBI:52617"
FT BINDING 58
FT /ligand="8-oxoguanine"
FT /ligand_id="ChEBI:CHEBI:52617"
FT BINDING 69
FT /ligand="8-oxoguanine"
FT /ligand_id="ChEBI:CHEBI:52617"
FT BINDING 144
FT /ligand="8-oxoguanine"
FT /ligand_id="ChEBI:CHEBI:52617"
FT /evidence="ECO:0000255"
FT BINDING 170
FT /ligand="8-oxoguanine"
FT /ligand_id="ChEBI:CHEBI:52617"
FT BINDING 218
FT /ligand="8-oxoguanine"
FT /ligand_id="ChEBI:CHEBI:52617"
FT BINDING 222
FT /ligand="8-oxoguanine"
FT /ligand_id="ChEBI:CHEBI:52617"
FT MUTAGEN 140
FT /note="K->Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:15604455"
FT MUTAGEN 147
FT /note="K->Q: Great decrease in activity and
FT thermostability."
FT /evidence="ECO:0000269|PubMed:15604455"
FT MUTAGEN 166
FT /note="D->N: No effect."
FT /evidence="ECO:0000269|PubMed:15604455"
FT MUTAGEN 172
FT /note="D->N: Loss of activity."
FT /evidence="ECO:0000269|PubMed:15604455"
FT HELIX 3..14
FT /evidence="ECO:0007829|PDB:1XQO"
FT HELIX 19..26
FT /evidence="ECO:0007829|PDB:1XQO"
FT HELIX 30..42
FT /evidence="ECO:0007829|PDB:1XQO"
FT HELIX 44..56
FT /evidence="ECO:0007829|PDB:1XQO"
FT HELIX 65..77
FT /evidence="ECO:0007829|PDB:1XQO"
FT HELIX 84..94
FT /evidence="ECO:0007829|PDB:1XQO"
FT HELIX 102..112
FT /evidence="ECO:0007829|PDB:1XQO"
FT HELIX 122..133
FT /evidence="ECO:0007829|PDB:1XQO"
FT HELIX 140..157
FT /evidence="ECO:0007829|PDB:1XQO"
FT HELIX 173..181
FT /evidence="ECO:0007829|PDB:1XQO"
FT HELIX 189..194
FT /evidence="ECO:0007829|PDB:1XQO"
FT HELIX 196..210
FT /evidence="ECO:0007829|PDB:1XQO"
FT HELIX 214..228
FT /evidence="ECO:0007829|PDB:1XQO"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:1XQO"
FT HELIX 239..244
FT /evidence="ECO:0007829|PDB:1XQO"
SQ SEQUENCE 256 AA; 29467 MW; E188433A957C9A16 CRC64;
MAAESQLKRV IETLRRLGIE EVLKLERRDP QYRAVCNVVK RHGETVGSRL AMLNALISYR
LTGKGEEHWE YFGKYFSQLE VIDLCRDFLK YIETSPFLKI GVEARKKRAL KACDYVPNLE
DLGLTLRQLS HIVGARREQK TLVFTIKILN YAYMCSRGVN RVLPFDIPIP VDYRVARLTW
CAGLIDFPPE EALRRYEAVQ KIWDAVARET GIPPLHLDTL LWLAGRAVLY GENLHGVPKE
VIALFQWRGG CRPPSE
