AGOG_METKA
ID AGOG_METKA Reviewed; 242 AA.
AC Q8TXW8;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=MK0541;
OS Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC Methanopyrus.
OX NCBI_TaxID=190192;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX PubMed=11930014; DOI=10.1073/pnas.032671499;
RA Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA Koonin E.V., Kozyavkin S.A.;
RT "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT monophyly of archaeal methanogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
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; AE009439; AAM01756.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8TXW8; -.
DR SMR; Q8TXW8; -.
DR STRING; 190192.MK0541; -.
DR EnsemblBacteria; AAM01756; AAM01756; MK0541.
DR KEGG; mka:MK0541; -.
DR PATRIC; fig|190192.8.peg.576; -.
DR HOGENOM; CLU_085935_0_0_2; -.
DR OMA; VKMFGYA; -.
DR Proteomes; UP000001826; 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..242
FT /note="N-glycosylase/DNA lyase"
FT /id="PRO_0000185110"
FT REGION 119..183
FT /note="Helix-hairpin-helix"
FT ACT_SITE 143
FT /note="Schiff-base intermediate with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01168"
FT ACT_SITE 175
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01168"
FT BINDING 25
FT /ligand="8-oxoguanine"
FT /ligand_id="ChEBI:CHEBI:52617"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01168"
FT BINDING 52
FT /ligand="8-oxoguanine"
FT /ligand_id="ChEBI:CHEBI:52617"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01168"
FT BINDING 63
FT /ligand="8-oxoguanine"
FT /ligand_id="ChEBI:CHEBI:52617"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01168"
FT BINDING 147
FT /ligand="8-oxoguanine"
FT /ligand_id="ChEBI:CHEBI:52617"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01168"
FT BINDING 173
FT /ligand="8-oxoguanine"
FT /ligand_id="ChEBI:CHEBI:52617"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01168"
FT BINDING 209
FT /ligand="8-oxoguanine"
FT /ligand_id="ChEBI:CHEBI:52617"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01168"
FT BINDING 213
FT /ligand="8-oxoguanine"
FT /ligand_id="ChEBI:CHEBI:52617"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01168"
SQ SEQUENCE 242 AA; 28614 MW; 25FF075E3383719E CRC64;
MTVPTFLRKV TLREICVIEE YVDVQYRAIE ALMDTLPSTD LVRLTVANAL VSYQLSSSGE
DWWREFSSYF RERRPRDIVR EYARFLPRSR GNRRLIRQKL RRLHRAKAFL EELSWQDAKS
YYRDMNRLRL DLARVLNADP ESKTIVFTVK MFGYALRAIT GRFRPYPFEI PIPVDARIER
ITRRITNDDP QLYWDSIARR TGIPPLHLDS ILWVGTSRDP EVKRLLAKVL PKLIGELEML
GN
