ID A0A2A9FXK2_9VIBR Unreviewed; 358 AA.
AC A0A2A9FXK2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=ATG66_1558 {ECO:0000313|EMBL:PFG55270.1};
OS Vibrio sp. ES.051.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1761909 {ECO:0000313|EMBL:PFG55270.1, ECO:0000313|Proteomes:UP000223114};
RN [1] {ECO:0000313|EMBL:PFG55270.1, ECO:0000313|Proteomes:UP000223114}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ES.051 {ECO:0000313|EMBL:PFG55270.1,
RC ECO:0000313|Proteomes:UP000223114};
RA Fredrickson J.;
RT "Microbial Interactions in Extremophilic Mat Communities.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
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:PFG55270.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PDJL01000004; PFG55270.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A9FXK2; -.
DR OrthoDB; 9802365at2; -.
DR Proteomes; UP000223114; 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; 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; PF10576; EndIII_4Fe-2S; 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.
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 358 AA; 41082 MW; F8A49BB386D96642 CRC64;
MTPFANAILK WYDAYGRKEL PWQQNKTAYS VWLSEIMLQQ TQVTTVIPYY QRFLERFPTV
VDLACAEQDE VLHLWTGLGY YARARNLHKA AKQVALKYNG EFPLDIEQMN DLPGIGRSTA
AAILSSVHKQ PHAILDGNVK RTLSRCFAVE GWPGQKKVEN QLWKIAETHT PQADVDKYNQ
AMMDMGAMVC TRSKPKCSLC PVADLCVAKK QDNVLDYPGK KPKKDKPVKQ TRFVMLHHRN
EHGHEVWLEQ RPQTGIWGGL FCFPQTEHAD VESDIELLLE QRDIQTSDIK KQQTLITFRH
TFSHYHLDIT PILIDLSNQP SMIMEGNKGL WYNLSKPEEI GLAAPVKQLL EALPYELR
//
