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Entry: A0A1Z9T757_9BACT
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ID   A0A1Z9T757_9BACT        Unreviewed;       369 AA.
AC   A0A1Z9T757;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Adenine DNA glycosylase {ECO:0000256|ARBA:ARBA00022023};
DE            EC=3.2.2.31 {ECO:0000256|ARBA:ARBA00012045};
GN   ORFNames=CBE26_04825 {ECO:0000313|EMBL:OUX36713.1};
OS   Kiritimatiellaceae bacterium TMED266.
OC   Bacteria; Kiritimatiellota; Kiritimatiellia; Kiritimatiellales;
OC   Kiritimatiellaceae.
OX   NCBI_TaxID=1987167 {ECO:0000313|EMBL:OUX36713.1, ECO:0000313|Proteomes:UP000198223};
RN   [1] {ECO:0000313|EMBL:OUX36713.1, ECO:0000313|Proteomes:UP000198223}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TMED266 {ECO:0000313|EMBL:OUX36713.1};
RA   Tully B.J., Sachdeva R., Graham E.D., Heidelberg J.F.;
RT   "290 Metagenome-assembled Genomes from the Mediterranean Sea: a resource
RT   for marine microbiology.";
RL   Submitted (MAY-2017) 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=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR603561-2};
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:OUX36713.1}.
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DR   EMBL; NHLL01000027; OUX36713.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z9T757; -.
DR   Proteomes; UP000198223; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro.
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   CDD; cd03425; MutT_pyrophosphohydrolase; 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; IPR003651; Endonuclease3_FeS-loop_motif.
DR   InterPro; IPR003265; HhH-GPD_domain.
DR   InterPro; IPR023170; HhH_base_excis_C.
DR   InterPro; IPR044298; MIG/MutY.
DR   InterPro; IPR003561; Mutator_MutT.
DR   InterPro; IPR029119; MutY_C.
DR   InterPro; IPR020476; Nudix_hydrolase.
DR   InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR   InterPro; IPR020084; NUDIX_hydrolase_CS.
DR   InterPro; IPR000086; NUDIX_hydrolase_dom.
DR   NCBIfam; TIGR00586; mutt; 1.
DR   NCBIfam; TIGR01084; mutY; 1.
DR   PANTHER; PTHR42944; ADENINE DNA GLYCOSYLASE; 1.
DR   PANTHER; PTHR42944:SF1; ADENINE DNA GLYCOSYLASE; 1.
DR   Pfam; PF00730; HhH-GPD; 1.
DR   Pfam; PF14815; NUDIX_4; 1.
DR   PRINTS; PR00502; NUDIXFAMILY.
DR   SMART; SM00478; ENDO3c; 1.
DR   SMART; SM00525; FES; 1.
DR   SUPFAM; SSF48150; DNA-glycosylase; 1.
DR   SUPFAM; SSF55811; Nudix; 1.
DR   PROSITE; PS51462; NUDIX; 1.
DR   PROSITE; PS00893; NUDIX_BOX; 1.
PE   3: Inferred from homology;
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   Magnesium {ECO:0000256|PIRSR:PIRSR603561-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR603561-2}.
FT   DOMAIN          232..359
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000259|PROSITE:PS51462"
FT   BINDING         254
FT                   /ligand="8-oxo-dGTP"
FT                   /ligand_id="ChEBI:CHEBI:77896"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603561-1"
FT   BINDING         265..268
FT                   /ligand="8-oxo-dGTP"
FT                   /ligand_id="ChEBI:CHEBI:77896"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603561-1"
FT   BINDING         268
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603561-2"
FT   BINDING         288
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603561-2"
SQ   SEQUENCE   369 AA;  42152 MW;  BA0A907B0750D36A CRC64;
     MKSLAPLNEA IQHQLLPWFD QNQRMMPWRK RRTPYRVWIS ELMLQQTRVA QAIPYYQRFM
     RRFPSLKKLA EASQSEVLKA WEGLGYYSRA RNLHKAAQII RDQHSGRFPC DPQEISKLPG
     VGPYTTAAIG SLAFNLNLAV VDGNVMRVLA RLRMIEDDIA QPSTKKKFQK LADQLLVKGE
     AGKFNEALME LGATVCLPQN PSCDVCPLST ACQAKLLDDV SRFPVKQKKK RIPHIIVGAA
     VVHNRDGKIL VAQRRNDQML GGLWEFPGGK IESNETIEEG VIRELNEELG ISISVEEKII
     TVKHTYSHFT MEMHTFWARI ESGTPVAIEC QDVRWKELYE LSELPFSKAD LKVIDALKAN
     LYHEKKEKM
//
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