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Database: UniProt
Entry: A0A1T4MZQ8_9FIRM
LinkDB: A0A1T4MZQ8_9FIRM
Original site: A0A1T4MZQ8_9FIRM 
ID   A0A1T4MZQ8_9FIRM        Unreviewed;       351 AA.
AC   A0A1T4MZQ8;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
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=SAMN02745973_01497 {ECO:0000313|EMBL:SJZ72381.1};
OS   Garciella nitratireducens DSM 15102.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae; Garciella.
OX   NCBI_TaxID=1121911 {ECO:0000313|EMBL:SJZ72381.1, ECO:0000313|Proteomes:UP000196365};
RN   [1] {ECO:0000313|EMBL:SJZ72381.1, ECO:0000313|Proteomes:UP000196365}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15102 {ECO:0000313|EMBL:SJZ72381.1,
RC   ECO:0000313|Proteomes:UP000196365};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Adenine glycosylase active on G-A mispairs.
CC       {ECO:0000256|RuleBase:RU365096}.
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}.
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DR   EMBL; FUWV01000009; SJZ72381.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T4MZQ8; -.
DR   Proteomes; UP000196365; 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; 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   SUPFAM; SSF48150; DNA-glycosylase; 1.
DR   SUPFAM; SSF55811; Nudix; 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:ARBA00022485};
KW   Reference proteome {ECO:0000313|Proteomes:UP000196365}.
FT   DOMAIN          41..192
FT                   /note="HhH-GPD"
FT                   /evidence="ECO:0000259|SMART:SM00478"
SQ   SEQUENCE   351 AA;  40765 MW;  FE2E36F18760AA31 CRC64;
     MNVEEMKYFS NELLKWYDQN ARILPWREHP SAYRVWISEV MLQQTRVNAV KPYFERFMKE
     CSTIQDLAHI SEDKLLKLWE GLGYYNRAKN LKRAAQIIEE KFGGRLPSDR KCLQSLPGIG
     PYTAGAISSI AFGHKVPAVD GNVLRVMSRV LANKEDITCT AVKKEIEKII YKILPEKRAG
     DFNQALMELG AVICVPNGAP KCTACPLSPI CQGYQQGIEE KLPIKAKKKK RTIEKKTIFL
     LVYEEYILIR QRPNKGLLSN MWEFPNVEGY LSNQKCKEKM QQWKIDVKQI LPLNSSKHIF
     THKEWRMIGY LIIINKKPKE LKGIWVTKQQ ILDKYSIPSA FQHYLKILFL Q
//
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