ID A0A1Y5TPB9_9RHOB Unreviewed; 356 AA.
AC A0A1Y5TPB9;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-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 Name=mutY {ECO:0000313|EMBL:SLN68838.1};
GN ORFNames=AQS8620_03261 {ECO:0000313|EMBL:SLN68838.1};
OS Aquimixticola soesokkakensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Aquimixticola.
OX NCBI_TaxID=1519096 {ECO:0000313|EMBL:SLN68838.1, ECO:0000313|Proteomes:UP000193862};
RN [1] {ECO:0000313|EMBL:SLN68838.1, ECO:0000313|Proteomes:UP000193862}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8620 {ECO:0000313|EMBL:SLN68838.1,
RC ECO:0000313|Proteomes:UP000193862};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-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}.
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DR EMBL; FWFS01000014; SLN68838.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y5TPB9; -.
DR Proteomes; UP000193862; 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; 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 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, ECO:0000313|EMBL:SLN68838.1};
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:UP000193862}.
FT DOMAIN 38..187
FT /note="HhH-GPD"
FT /evidence="ECO:0000259|SMART:SM00478"
SQ SEQUENCE 356 AA; 38958 MW; D63EA050CE1DC1DE CRC64;
MLDWYDTHAR AMPWRVGPAD RRAGQRPDPY AVWLSEVMLQ QTTVATVRDY FRRFIALWPT
VDDLAAAEDA DVMAAWAGLG YYARARNLLK CARVVSRDLE GRFPASLAGL LQLPGIGPYT
AAALASIAFD LPETVVDGNV ERVISRIFRV ETPLPTAKPE LTALAQRLTP AQRPGDYAQA
IMDLGATICT PRNPACGICP WRAGCAAQAA GVQADLPRKV PKAVKPTRRG EVYVTRNASG
DWLLETRPER GLLGGMLAFP TSDWSQDPAP APPFEADWCS IGTVKHTFTH FHLLLEVHTA
DAGQKNPTRG TFIPDSRFRA ADLPTLMRKA FDLAQATSDN AQASHKRPVN PVPEVP
//
