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Database: UniProt
Entry: A0A073J3S3_9RHOB
LinkDB: A0A073J3S3_9RHOB
Original site: A0A073J3S3_9RHOB 
ID   A0A073J3S3_9RHOB        Unreviewed;       347 AA.
AC   A0A073J3S3;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 33.
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=SUH3_10835 {ECO:0000313|EMBL:KEJ97263.1};
OS   Pseudosulfitobacter pseudonitzschiae.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Pseudosulfitobacter.
OX   NCBI_TaxID=1402135 {ECO:0000313|EMBL:KEJ97263.1, ECO:0000313|Proteomes:UP000027746};
RN   [1] {ECO:0000313|EMBL:KEJ97263.1, ECO:0000313|Proteomes:UP000027746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H3 {ECO:0000313|EMBL:KEJ97263.1,
RC   ECO:0000313|Proteomes:UP000027746};
RA   Lai Q., Hong Z.;
RT   "Sulfitobacter sp. H3 (MCCC 1A00686) Genome Sequencing.";
RL   Submitted (JAN-2014) 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:KEJ97263.1}.
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DR   EMBL; JAMD01000002; KEJ97263.1; -; Genomic_DNA.
DR   RefSeq; WP_051694016.1; NZ_WKFG01000017.1.
DR   AlphaFoldDB; A0A073J3S3; -.
DR   GeneID; 68871709; -.
DR   OrthoDB; 9802365at2; -.
DR   Proteomes; UP000027746; 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; 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   SUPFAM; SSF48150; DNA-glycosylase; 1.
DR   SUPFAM; SSF55811; Nudix; 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, 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027746}.
FT   DOMAIN          45..194
FT                   /note="HhH-GPD"
FT                   /evidence="ECO:0000259|SMART:SM00478"
SQ   SEQUENCE   347 AA;  38155 MW;  6CC384853DE670CE CRC64;
     MRERAKDLLD WYDVHARVMP WRTPPADKRA GTRPDPYAVW LSEVMLQQTT VAAVKDYFTR
     FTTRWPTVAD LAAAEDGDVM AEWAGLGYYA RARNLLKCAR AVVADHGGQF PADHAALLAL
     PGIGPYTAAA ISSIAFDLPH AVLDGNVERV MARIYDEHTP LPVAKPILMA HAEALTPAER
     PGDYAQAVMD LGATICTPKS PACGICPWRD PCLACQRGTA AELPKKTPKK AKPIRHGTVY
     VARRPDGAYL LERRPDRGLL GGMLGWPGSD WVDVSMDRPA GTPPVNADWT VLQGEVRHTF
     THFHLILTVM LAETDAEPDT GRFMTQAEFG PSDLPTVMRK AFDLTRH
//
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