ID   A0A086YZF1_9BIFI        Unreviewed;       303 AA.
AC   A0A086YZF1;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=Adenine DNA glycosylase {ECO:0000256|ARBA:ARBA00022023};
DE            EC=3.2.2.31 {ECO:0000256|ARBA:ARBA00012045};
GN   ORFNames=BACT_0351 {ECO:0000313|EMBL:KFI39651.1};
OS   Bifidobacterium actinocoloniiforme DSM 22766.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=1437605 {ECO:0000313|EMBL:KFI39651.1, ECO:0000313|Proteomes:UP000029015};
RN   [1] {ECO:0000313|EMBL:KFI39651.1, ECO:0000313|Proteomes:UP000029015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22766 {ECO:0000313|EMBL:KFI39651.1,
RC   ECO:0000313|Proteomes:UP000029015};
RA   Ventura M., Milani C., Lugli G.A.;
RT   "Genomics of Bifidobacteria.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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;
CC         Evidence={ECO:0000256|ARBA:ARBA00000843};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- SIMILARITY: Belongs to the Nth/MutY family.
CC       {ECO:0000256|ARBA:ARBA00008343}.
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:KFI39651.1}.
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DR   EMBL; JGYK01000001; KFI39651.1; -; Genomic_DNA.
DR   RefSeq; WP_051905186.1; NZ_JGYK01000001.1.
DR   AlphaFoldDB; A0A086YZF1; -.
DR   STRING; 1437605.AB656_00370; -.
DR   KEGG; bact:AB656_00370; -.
DR   PATRIC; fig|1437605.7.peg.72; -.
DR   eggNOG; COG1194; Bacteria.
DR   OrthoDB; 9802365at2; -.
DR   Proteomes; UP000029015; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:InterPro.
DR   CDD; cd00056; ENDO3c; 1.
DR   Gene3D; 1.10.1670.10; Helix-hairpin-Helix base-excision DNA repair enzymes (C-terminal); 1.
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   PANTHER; PTHR42944; ADENINE DNA GLYCOSYLASE; 1.
DR   PANTHER; PTHR42944:SF1; ADENINE DNA GLYCOSYLASE; 1.
DR   Pfam; PF10576; EndIII_4Fe-2S; 1.
DR   Pfam; PF00633; HHH; 1.
DR   Pfam; PF00730; HhH-GPD; 1.
DR   SMART; SM00478; ENDO3c; 1.
DR   SMART; SM00525; FES; 1.
DR   SUPFAM; SSF48150; DNA-glycosylase; 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};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Lyase {ECO:0000313|EMBL:KFI39651.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029015}.
FT   DOMAIN          48..200
FT                   /note="HhH-GPD"
FT                   /evidence="ECO:0000259|SMART:SM00478"
SQ   SEQUENCE   303 AA;  33064 MW;  C27F79F452E86946 CRC64;
     MTQTAQVELT DARRAYRLLA AWWEGNARDL PWRFGRTTPW GILVSEVMSQ QTQMSRVVPY
     WVEWMRAWPT PEALAAASGA EVITAWGRLG YPRRALRLQA CAKTVVEEYG GKLPQDYETL
     LTLPGVGDYT ASAVVSFAYG KRIAVIDTNI RRVLGRVFAG KESRGGAASA DERTLAQRAL
     PEDDAESVVW NQSVMELGAT VCAAKSPACE ECPLNGICAF LAAGRPGLGE RRTRPRQRFK
     GTDRQVRGLI LAALRELPPG GSLPISRLDS LWPDQAQLGA CLASLDEDGL VEIHQGGSVS
     LPE
//