ID A0A1F8ST14_9CHLR Unreviewed; 356 AA.
AC A0A1F8ST14;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-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=A2Z45_03035 {ECO:0000313|EMBL:OGO63037.1};
OS Chloroflexi bacterium RBG_19FT_COMBO_55_16.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797669 {ECO:0000313|EMBL:OGO63037.1, ECO:0000313|Proteomes:UP000177674};
RN [1] {ECO:0000313|EMBL:OGO63037.1, ECO:0000313|Proteomes:UP000177674}
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 -!- 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:OGO63037.1}.
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DR EMBL; MGOK01000132; OGO63037.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8ST14; -.
DR STRING; 1797669.A2Z45_03035; -.
DR Proteomes; UP000177674; Unassembled WGS sequence.
DR GO; GO:0051536; F:iron-sulfur cluster 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; IPR003265; HhH-GPD_domain.
DR InterPro; IPR023170; HhH_base_excis_C.
DR InterPro; IPR044298; MIG/MutY.
DR InterPro; IPR029119; MutY_C.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
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 SMART; SM00478; ENDO3c; 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}.
FT DOMAIN 227..350
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
SQ SEQUENCE 356 AA; 39395 MW; 798B01924E163B66 CRC64;
MSSPFAERLL EWYAAHARRL PWRGHPDPYA VWVAEIMLQQ TRVETVIPYF ERWMARFPTL
ETLAAASQGE VLGAWEGLGY YSRARNLQRA AQIVVTEHSG ELPRQAKALR RLPGIGRYTA
AAISSTAFGL DEATLDGNIR RVLARVFDIR QPARSPEGER RLWELAAVHL PPGWAADYNQ
AMMDLGATVC TPRAPDCPRC PLKDLCAACA LGVQDQRPVS QAKPPLPHHI VTAAVIQRDG
QVLIAQRPPQ GLLGGLWEFP GGKVQPGEQL VACLQREIGE ELGAEIEVGG ALGVYRHAYT
HFRVTLHAFS CTLLDGEPRN LQHSALSWVA PTALRDYPMG KIDRLIANQL SEISEQ
//
