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Database: UniProt
Entry: A0A0P0NML3_9SPHI
LinkDB: A0A0P0NML3_9SPHI
Original site: A0A0P0NML3_9SPHI 
ID   A0A0P0NML3_9SPHI        Unreviewed;       350 AA.
AC   A0A0P0NML3;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
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=AQ505_25475 {ECO:0000313|EMBL:ALL08527.1};
OS   Pedobacter sp. PACM 27299.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=1727164 {ECO:0000313|EMBL:ALL08527.1, ECO:0000313|Proteomes:UP000062859};
RN   [1] {ECO:0000313|EMBL:ALL08527.1, ECO:0000313|Proteomes:UP000062859}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PAMC 27299 {ECO:0000313|EMBL:ALL08527.1,
RC   ECO:0000313|Proteomes:UP000062859};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) 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; CP012996; ALL08527.1; -; Genomic_DNA.
DR   RefSeq; WP_062550756.1; NZ_CP012996.1.
DR   AlphaFoldDB; A0A0P0NML3; -.
DR   STRING; 1727164.AQ505_25475; -.
DR   KEGG; pep:AQ505_25475; -.
DR   OrthoDB; 9802365at2; -.
DR   Proteomes; UP000062859; Chromosome.
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; 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.
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:UP000062859}.
FT   DOMAIN          35..186
FT                   /note="HhH-GPD"
FT                   /evidence="ECO:0000259|SMART:SM00478"
SQ   SEQUENCE   350 AA;  40537 MW;  2B274D0939C81BED CRC64;
     MSFQREIVKW YSINKRELPW RDTTDAYVIW LSEIILQQTR VEQGLPYFQR FLQNYPTVDD
     FANATEAQIL KLWQGLGYYS RGRNMLFTAR QIQENYGGVF PQKYEELVQL KGVGEYTAAA
     ISSFSANESR AVLDGNVFRV LSRYFGIETA INSTEGKKEF TALANALIEG QNPSIYNQAI
     MEFGALQCKP KSPDCVSCPV QSSCYARAND RVNVLPLKLK KLKKRTRYFN YFVCQDGENL
     LVKKRIAGDV WQELYDFPLI ETEKNYLETH ESFLSELKNN FGSDCLISPI TQQKHLLTHQ
     TIYVQFFVLD NYIINFKKDA EIKWVSLAEF EELPQPKVIA NFMNSNSIKQ
//
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