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Database: UniProt
Entry: F5RCA7_METUF
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ID   F5RCA7_METUF            Unreviewed;       362 AA.
AC   F5RCA7;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   24-JAN-2024, entry version 51.
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=METUNv1_01910 {ECO:0000313|EMBL:EGK71687.1};
OS   Methyloversatilis universalis (strain ATCC BAA-1314 / JCM 13912 / FAM5).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Sterolibacteriaceae; Methyloversatilis.
OX   NCBI_TaxID=1000565 {ECO:0000313|EMBL:EGK71687.1, ECO:0000313|Proteomes:UP000005019};
RN   [1] {ECO:0000313|EMBL:EGK71687.1, ECO:0000313|Proteomes:UP000005019}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1314 / JCM 13912 / FAM5
RC   {ECO:0000313|Proteomes:UP000005019};
RX   PubMed=21725020; DOI=10.1128/JB.05331-11;
RA   Kittichotirat W., Good N.M., Hall R., Bringel F., Lajus A., Medigue C.,
RA   Smalley N.E., Beck D., Bumgarner R., Vuilleumier S., Kalyuzhnaya M.G.;
RT   "Genome sequence of Methyloversatilis universalis FAM5T, a methylotrophic
RT   representative of the order Rhodocyclales.";
RL   J. Bacteriol. 193:4541-4542(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:EGK71687.1}.
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DR   EMBL; AFHG01000048; EGK71687.1; -; Genomic_DNA.
DR   RefSeq; WP_008061102.1; NZ_AFHG01000048.1.
DR   AlphaFoldDB; F5RCA7; -.
DR   STRING; 1000565.METUNv1_01910; -.
DR   eggNOG; COG1194; Bacteria.
DR   OrthoDB; 9802365at2; -.
DR   Proteomes; UP000005019; 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; 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; PF00633; HHH; 1.
DR   Pfam; PF00730; HhH-GPD; 1.
DR   Pfam; PF14815; NUDIX_4; 1.
DR   SMART; SM00478; ENDO3c; 1.
DR   SMART; SM00525; FES; 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:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005019}.
FT   DOMAIN          45..196
FT                   /note="HhH-GPD"
FT                   /evidence="ECO:0000259|SMART:SM00478"
SQ   SEQUENCE   362 AA;  39567 MW;  18AA5B13D305FA42 CRC64;
     MNTPSEVAAS DDFAATLVRW QRQHGRHDLP WQTGQAYGVW VSEIMLQQTQ VQTVIGYYAR
     FMQRFPTLAA LAAADEAAVM ESWSGLGYYA RARNLHRAAR EVMSRFGGDF PRTVDDIESL
     PGIGRSTASA IATFCFGARA PILDGNVKRV FARVFGIDGF PGTRAVEQRM WALAHKLMPD
     QDGAAYTQAL MDLGATVCTR NRPRCDACPV AGRCVARAQG RQRELPAPRP ARVRPLRLVH
     ALLLRTPDAV LLERRPGQGI WGGLLSLPEL AAQSEAEALA EAQRWLAVRG LAAHQVQVLP
     AVSHGFTHFE LRLVPLLAHL AMATPFAADS TLHWQPLGTL ATAALPAPVR RLLDTLVPTG
     HD
//
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