ID FPG_RHIWR Reviewed; 270 AA. AC A5VG06; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 10-JUL-2007, sequence version 1. DT 27-MAR-2024, entry version 97. 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=Swit_4885; OS Rhizorhabdus wittichii (strain DSM 6014 / CCUG 31198 / JCM 15750 / NBRC OS 105917 / EY 4224 / RW1) (Sphingomonas wittichii). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Rhizorhabdus. OX NCBI_TaxID=392499; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 6014 / CCUG 31198 / JCM 15750 / NBRC 105917 / EY 4224 / RC RW1; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., RA Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C., RA Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Kim E., Halden R.U., Miller T.R., Salzberg S.L., Eisen J.A., RA Richardson P.; RT "Complete sequence of chromosome of Sphingomonas wittichii RW1."; RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in base excision repair of DNA damaged by oxidation CC or by mutagenic agents. Acts as a 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; Evidence={ECO:0000255|HAMAP- CC 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000699; ABQ71222.1; -; Genomic_DNA. DR AlphaFoldDB; A5VG06; -. DR SMR; A5VG06; -. DR STRING; 392499.Swit_4885; -. DR PaxDb; 392499-Swit_4885; -. DR KEGG; swi:Swit_4885; -. DR eggNOG; COG0266; Bacteria. DR HOGENOM; CLU_038423_1_1_5; -. DR OrthoDB; 9800855at2; -. DR Proteomes; UP000001989; 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 CDD; cd08966; EcFpg-like_N; 1. DR Gene3D; 1.10.8.50; -; 1. DR Gene3D; 3.20.190.10; MutM-like, N-terminal; 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_uS13-like_H2TH. DR InterPro; IPR000214; Znf_DNA_glyclase/AP_lyase. DR InterPro; IPR010663; Znf_FPG/IleRS. DR NCBIfam; TIGR00577; fpg; 1. DR PANTHER; PTHR22993:SF9; ENDONUCLEASE 8-LIKE 1; 1. DR PANTHER; PTHR22993; FORMAMIDOPYRIMIDINE-DNA GLYCOSYLASE; 1. 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; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1. DR SUPFAM; SSF81624; N-terminal domain of MutM-like DNA repair proteins; 1. DR SUPFAM; SSF46946; S13-like H2TH domain; 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..270 FT /note="Formamidopyrimidine-DNA glycosylase" FT /id="PRO_1000008784" FT ZN_FING 237..270 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 260 FT /note="Proton donor; for delta-elimination activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00103" FT BINDING 90 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00103" FT BINDING 109 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00103" FT BINDING 152 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00103" SQ SEQUENCE 270 AA; 29739 MW; 1AB6F865A6E58B51 CRC64; MPELPEVETT VRGLRPPLEG RRLTRVETRR ADLRRPFPAD LRQRMTGATI TGLGRRAKYG LIETDRGDVM VFHLGMSGRW RIDPSEIGAH DHLVLETDEG RTLSLCDPRR FGSVDLVRGE ELAGFGPFKA LGPEPLGPDL TGAHLAGALE GRVAPIKAML LDQRIVAGLG NIYVCEALHM TGIAPTTMAG RIAKKRLDRL VDSIREVLAA AIEAGGSTLR DYARPDGELG YFAKQWRVYG REGEPCHCGT VIRRRVDGGR STFYCPKCQK //