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Database: UniProt
Entry: A0A1S9PAP8_9SPHI
LinkDB: A0A1S9PAP8_9SPHI
Original site: A0A1S9PAP8_9SPHI 
ID   A0A1S9PAP8_9SPHI        Unreviewed;       348 AA.
AC   A0A1S9PAP8;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
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=BC343_12460 {ECO:0000313|EMBL:OOQ57897.1};
OS   Mucilaginibacter pedocola.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Mucilaginibacter.
OX   NCBI_TaxID=1792845 {ECO:0000313|EMBL:OOQ57897.1, ECO:0000313|Proteomes:UP000189739};
RN   [1] {ECO:0000313|EMBL:OOQ57897.1, ECO:0000313|Proteomes:UP000189739}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TBZ30 {ECO:0000313|EMBL:OOQ57897.1,
RC   ECO:0000313|Proteomes:UP000189739};
RA   Huang J., Tang J.;
RT   "Genomic analysis of zinc-resistant bacterium Mucilaginibacter pedocola
RT   TBZ30.";
RL   Submitted (JUL-2016) 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}.
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:OOQ57897.1}.
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DR   EMBL; MBTF01000035; OOQ57897.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1S9PAP8; -.
DR   STRING; 1792845.BC343_12460; -.
DR   OrthoDB; 9802365at2; -.
DR   Proteomes; UP000189739; 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; 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; 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.
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:UP000189739}.
FT   DOMAIN          35..186
FT                   /note="HhH-GPD"
FT                   /evidence="ECO:0000259|SMART:SM00478"
SQ   SEQUENCE   348 AA;  40041 MW;  0E398DFB436EDF26 CRC64;
     MNISAELIGW YEANKRDLPW RNTTDAYIIW LSEIILQQTR VEQGLPYFER FADKYPTVSH
     FAAAPEDDIL RLWQGLGYYS RGRNMLKTAQ LVQQHYNGVF PTAYEQLIKL KGIGEYTAAA
     ISSFSANEAR AVVDGNVYRV LARYFGIDEP INSPKGKKLF QQLANEVLDH ERPAQHNQAM
     MEFGAMLCKP KNPACGICPI RLGCVAFKTN ATTSLPVKLK TVKVRKRYFN YLLITEGDKV
     LLNKRGETDI WANMYDLPLI ETDGTVEPHK LFELPDVQQI YGNGIAIRNI EPEIKHVLTH
     QQLFIRFIVL NGQPEKLQPG WFYTKVDNLN KLAMPKRIFI FIKDFFNF
//
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