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Database: UniProt
Entry: A0A1F4F0R1_9PROT
LinkDB: A0A1F4F0R1_9PROT
Original site: A0A1F4F0R1_9PROT 
ID   A0A1F4F0R1_9PROT        Unreviewed;       345 AA.
AC   A0A1F4F0R1;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Adenine DNA glycosylase {ECO:0000256|ARBA:ARBA00022023, ECO:0000256|RuleBase:RU365096};
DE            EC=3.2.2.31 {ECO:0000256|ARBA:ARBA00012045, ECO:0000256|RuleBase:RU365096};
GN   ORFNames=A3F77_06255 {ECO:0000313|EMBL:OGA66983.1};
OS   Betaproteobacteria bacterium RIFCSPLOWO2_12_FULL_67_28.
OC   Bacteria; Pseudomonadota; Betaproteobacteria.
OX   NCBI_TaxID=1797503 {ECO:0000313|EMBL:OGA66983.1, ECO:0000313|Proteomes:UP000177406};
RN   [1] {ECO:0000313|EMBL:OGA66983.1, ECO:0000313|Proteomes:UP000177406}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
CC   -!- FUNCTION: Adenine glycosylase active on G-A mispairs. MutY also
CC       corrects error-prone DNA synthesis past GO lesions which are due to the
CC       oxidatively damaged form of guanine: 7,8-dihydro-8-oxoguanine (8-oxo-
CC       dGTP). {ECO:0000256|ARBA:ARBA00002933}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolyzes free adenine bases from 7,8-dihydro-8-
CC         oxoguanine:adenine mismatched double-stranded DNA, leaving an
CC         apurinic site.; EC=3.2.2.31; Evidence={ECO:0000256|ARBA:ARBA00000843,
CC         ECO:0000256|RuleBase:RU365096};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|RuleBase:RU365096};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000256|RuleBase:RU365096};
CC   -!- SIMILARITY: Belongs to the Nth/MutY family.
CC       {ECO:0000256|ARBA:ARBA00008343, ECO:0000256|RuleBase:RU365096}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OGA66983.1}.
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DR   EMBL; MERO01000114; OGA66983.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F4F0R1; -.
DR   STRING; 1797503.A3F77_06255; -.
DR   Proteomes; UP000177406; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000701; F:purine-specific mismatch base pair DNA N-glycosylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006284; P:base-excision repair; IEA:UniProtKB-UniRule.
DR   CDD; cd03431; DNA_Glycosylase_C; 1.
DR   CDD; cd00056; ENDO3c; 1.
DR   Gene3D; 1.10.1670.10; Helix-hairpin-Helix base-excision DNA repair enzymes (C-terminal); 1.
DR   Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR   InterPro; IPR005760; A/G_AdeGlyc_MutY.
DR   InterPro; IPR011257; DNA_glycosylase.
DR   InterPro; IPR004036; Endonuclease-III-like_CS2.
DR   InterPro; IPR003651; Endonuclease3_FeS-loop_motif.
DR   InterPro; IPR004035; Endouclease-III_FeS-bd_BS.
DR   InterPro; IPR003265; HhH-GPD_domain.
DR   InterPro; IPR023170; HhH_base_excis_C.
DR   InterPro; IPR000445; HhH_motif.
DR   InterPro; IPR044298; MIG/MutY.
DR   InterPro; IPR029119; MutY_C.
DR   InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR   NCBIfam; TIGR01084; mutY; 1.
DR   PANTHER; PTHR42944; ADENINE DNA GLYCOSYLASE; 1.
DR   PANTHER; PTHR42944:SF1; ADENINE DNA GLYCOSYLASE; 1.
DR   Pfam; PF00633; HHH; 1.
DR   Pfam; PF00730; HhH-GPD; 1.
DR   Pfam; PF14815; NUDIX_4; 1.
DR   SMART; SM00478; ENDO3c; 1.
DR   SMART; SM00525; FES; 1.
DR   SUPFAM; SSF48150; DNA-glycosylase; 1.
DR   SUPFAM; SSF55811; Nudix; 1.
DR   PROSITE; PS00764; ENDONUCLEASE_III_1; 1.
DR   PROSITE; PS01155; ENDONUCLEASE_III_2; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU365096};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU365096};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU365096};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          37..188
FT                   /note="HhH-GPD"
FT                   /evidence="ECO:0000259|SMART:SM00478"
SQ   SEQUENCE   345 AA;  38136 MW;  8ABF6EA81CD7B421 CRC64;
     MRDFARSIVR WQRQRGRRGM PWQGVRDPYR VWLSEIMLQQ TRVDAVTGYY LRFLARFPDV
     GALAQASQHE VLQLWSGLGY YARARNLHAA ARELVAARAG RFPRSAEALA ALPGVGRSTA
     AAIAVFAFGR RAAILDGNVK RVLARCFGVA GFPGETAVAR QLWMLAERLV PARGVRAYTQ
     GLMDLGATVC RRVRPLCGAC PVAAHCVALR EGRIAQLPAP RPRLALPLRK AHWLIALHAG
     RVLLERRPPS GLWGGLWAFP EAHGRDARAL GRAVGCEIAS LRRLPPLEHG FTHFRLRVQP
     LVCQVRRCTP RAEQGGRLWL DLADAAGSAV PAPVRTLLLR LAPRR
//
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