FPG_BRASB
ID FPG_BRASB Reviewed; 293 AA.
AC A5E887;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Formamidopyrimidine-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_00103};
DE Short=Fapy-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_00103};
DE EC=3.2.2.23 {ECO:0000255|HAMAP-Rule:MF_00103};
DE AltName: Full=DNA-(apurinic or apyrimidinic site) lyase MutM {ECO:0000255|HAMAP-Rule:MF_00103};
DE Short=AP lyase MutM {ECO:0000255|HAMAP-Rule:MF_00103};
DE EC=4.2.99.18 {ECO:0000255|HAMAP-Rule:MF_00103};
GN Name=mutM {ECO:0000255|HAMAP-Rule:MF_00103};
GN Synonyms=fpg {ECO:0000255|HAMAP-Rule:MF_00103};
GN OrderedLocusNames=BBta_0080;
OS Bradyrhizobium sp. (strain BTAi1 / ATCC BAA-1182).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium; unclassified Bradyrhizobium.
OX NCBI_TaxID=288000;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BTAi1 / ATCC BAA-1182;
RX PubMed=17540897; DOI=10.1126/science.1139548;
RA Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.-C.,
RA Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L.,
RA Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S., Rouy Z.,
RA Mangenot S., Segurens B., Dossat C., Franck W.L., Chang W.-S., Saunders E.,
RA Bruce D., Richardson P., Normand P., Dreyfus B., Pignol D., Stacey G.,
RA Emerich D., Vermeglio A., Medigue C., Sadowsky M.;
RT "Legumes symbioses: absence of nod genes in photosynthetic bradyrhizobia.";
RL Science 316:1307-1312(2007).
CC -!- FUNCTION: Involved in base excision repair of DNA damaged by oxidation
CC or by mutagenic agents. Acts as DNA glycosylase that recognizes and
CC removes damaged bases. Has a preference for oxidized purines, such as
CC 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase
CC activity and introduces nicks in the DNA strand. Cleaves the DNA
CC backbone by beta-delta elimination to generate a single-strand break at
CC the site of the removed base with both 3'- and 5'-phosphates.
CC {ECO:0000255|HAMAP-Rule:MF_00103}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of DNA containing ring-opened 7-methylguanine
CC residues, releasing 2,6-diamino-4-hydroxy-5-(N-
CC methyl)formamidopyrimidine.; EC=3.2.2.23;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00103};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-
CC deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-
CC dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-
CC 2'-deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:66592, Rhea:RHEA-
CC COMP:13180, Rhea:RHEA-COMP:16897, Rhea:RHEA-COMP:17067,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:136412, ChEBI:CHEBI:157695,
CC ChEBI:CHEBI:167181; EC=4.2.99.18; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00103};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00103};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00103};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00103}.
CC -!- SIMILARITY: Belongs to the FPG family. {ECO:0000255|HAMAP-
CC Rule:MF_00103}.
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DR EMBL; CP000494; ABQ32381.1; -; Genomic_DNA.
DR RefSeq; WP_011942604.1; NC_009485.1.
DR AlphaFoldDB; A5E887; -.
DR SMR; A5E887; -.
DR STRING; 288000.BBta_0080; -.
DR EnsemblBacteria; ABQ32381; ABQ32381; BBta_0080.
DR KEGG; bbt:BBta_0080; -.
DR eggNOG; COG0266; Bacteria.
DR HOGENOM; CLU_038423_1_1_5; -.
DR OMA; GVHLRMT; -.
DR OrthoDB; 1162346at2; -.
DR Proteomes; UP000000246; Chromosome.
DR GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0008534; F:oxidized purine nucleobase lesion DNA N-glycosylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR Gene3D; 3.20.190.10; -; 1.
DR HAMAP; MF_00103; Fapy_DNA_glycosyl; 1.
DR InterPro; IPR015886; DNA_glyclase/AP_lyase_DNA-bd.
DR InterPro; IPR015887; DNA_glyclase_Znf_dom_DNA_BS.
DR InterPro; IPR020629; Formamido-pyr_DNA_Glyclase.
DR InterPro; IPR012319; FPG_cat.
DR InterPro; IPR035937; MutM-like_N-ter.
DR InterPro; IPR010979; Ribosomal_S13-like_H2TH.
DR InterPro; IPR000214; Znf_DNA_glyclase/AP_lyase.
DR InterPro; IPR010663; Znf_FPG/IleRS.
DR Pfam; PF01149; Fapy_DNA_glyco; 1.
DR Pfam; PF06831; H2TH; 1.
DR Pfam; PF06827; zf-FPG_IleRS; 1.
DR SMART; SM00898; Fapy_DNA_glyco; 1.
DR SMART; SM01232; H2TH; 1.
DR SUPFAM; SSF46946; SSF46946; 1.
DR SUPFAM; SSF81624; SSF81624; 1.
DR TIGRFAMs; TIGR00577; fpg; 1.
DR PROSITE; PS51068; FPG_CAT; 1.
DR PROSITE; PS01242; ZF_FPG_1; 1.
DR PROSITE; PS51066; ZF_FPG_2; 1.
PE 3: Inferred from homology;
KW DNA damage; DNA repair; DNA-binding; Glycosidase; Hydrolase; Lyase;
KW Metal-binding; Multifunctional enzyme; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..293
FT /note="Formamidopyrimidine-DNA glycosylase"
FT /id="PRO_1000008678"
FT ZN_FING 257..293
FT /note="FPG-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00103"
FT ACT_SITE 2
FT /note="Schiff-base intermediate with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00103"
FT ACT_SITE 3
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00103"
FT ACT_SITE 58
FT /note="Proton donor; for beta-elimination activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00103"
FT ACT_SITE 283
FT /note="Proton donor; for delta-elimination activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00103"
FT BINDING 104
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00103"
FT BINDING 123
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00103"
FT BINDING 166
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00103"
SQ SEQUENCE 293 AA; 32548 MW; A8AEE4D9B0B55DB0 CRC64;
MPELPEVETV RRGLQPVMEG AKIVAAEARR GDLRFPFQPD FAKRLQGQTV RGLGRRAKYL
LADLSSGDVL LMHLGMSGSF RVIKQDDEET PGEFHYPRGK DSVHDHVVFH MSSGADIVFN
DPRRFGFMKI IGRGEIEREP HLKDLGPEPL GNEFDAAMLA TACAGKKTSL KAALLDQRVV
AGLGNIYVCE ALFRAHLSPR RLAATLATRK GEPTDHARRL VEAIHAVLNE AIRAGGSSLR
DHRQTSGELG YFQHSFQVYD REGEPCRTDG CGGVVKRFVQ NGRSTFWCPK CQR
