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Database: UniProt
Entry: F7VCE5_9PROT
LinkDB: F7VCE5_9PROT
Original site: F7VCE5_9PROT 
ID   F7VCE5_9PROT            Unreviewed;       390 AA.
AC   F7VCE5;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 44.
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=ATPR_1044 {ECO:0000313|EMBL:GAA08040.1};
OS   Acetobacter tropicalis NBRC 101654.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acetobacter.
OX   NCBI_TaxID=749388 {ECO:0000313|EMBL:GAA08040.1, ECO:0000313|Proteomes:UP000004319};
RN   [1] {ECO:0000313|EMBL:GAA08040.1, ECO:0000313|Proteomes:UP000004319}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101654 {ECO:0000313|EMBL:GAA08040.1,
RC   ECO:0000313|Proteomes:UP000004319};
RX   PubMed=21554859; DOI=10.1016/j.bbrc.2011.04.126;
RA   Matsutani M., Hirakawa H., Nishikura M., Soemphol W., Ali I.A.I.,
RA   Yakushi T., Matsushita K.;
RT   "Increased number of Arginine-based salt bridges contributes to the
RT   thermotolerance of thermotolerant acetic acid bacteria, Acetobacter
RT   tropicalis SKU1100.";
RL   Biochem. Biophys. Res. Commun. 409:120-124(2011).
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:GAA08040.1}.
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DR   EMBL; BABS01000021; GAA08040.1; -; Genomic_DNA.
DR   AlphaFoldDB; F7VCE5; -.
DR   Proteomes; UP000004319; 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; 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.
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:ARBA00022485}.
FT   DOMAIN          77..228
FT                   /note="HhH-GPD"
FT                   /evidence="ECO:0000259|SMART:SM00478"
SQ   SEQUENCE   390 AA;  42307 MW;  495EAC57B1BA6519 CRC64;
     MPVFALLLAE GAERVVARVF FAPVLPERLS FVITSSVKTP PARSLLDWYD RHRRVLPWRS
     GPGQTADPYA VWLSEIMLQQ TTVKAVGPYY HRFLEKFPTV QALAAADRDD VLSAWAGLGY
     YSRARNLHAC AQKVVELGGF PNTVEGLLTL PGIGAYTAAA VAAIAFGVPV VPVDGNVERI
     TSRLFAIEEP LPASRKKLAV LASGLNADKE ARKRPSDFAQ ALFDLGASLC SPRSPACGLC
     PWVEVCAAHK AGIAATLPRR APKAVKPVRY GAHFLVIDAA GQVLLRKRPE KGLLAAMTEL
     PGTPWRTEPW STEEALTHAP VQTEWQDCGM VKHVFTHFTL QVTVYAAHIS RFSNQAVQEG
     FLAPATGVDA LSLPSLMLKC IKRGLKTLAT
//
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