ID FPG_SYNY3 Reviewed; 287 AA. AC P74290; Q55328; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 159. DE RecName: Full=Formamidopyrimidine-DNA glycosylase; DE Short=Fapy-DNA glycosylase; DE EC=3.2.2.23; DE AltName: Full=DNA-(apurinic or apyrimidinic site) lyase MutM; DE Short=AP lyase MutM; DE EC=4.2.99.18; GN Name=mutM; Synonyms=fpg; OrderedLocusNames=slr1689; OS Synechocystis sp. (strain PCC 6803 / Kazusa). OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae; OC Synechocystis. OX NCBI_TaxID=1111708; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 6803 / Kazusa; RX PubMed=8905231; DOI=10.1093/dnares/3.3.109; RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S., RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.; RT "Sequence analysis of the genome of the unicellular cyanobacterium RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire RT genome and assignment of potential protein-coding regions."; RL DNA Res. 3:109-136(1996). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-169. RX PubMed=2509456; DOI=10.1016/s0021-9258(18)51474-5; RA Chitnis P.R., Reilly P.A., Miedel M.C., Nelson N.; RT "Structure and targeted mutagenesis of the gene encoding 8-kDa subunit of RT photosystem I from the cyanobacterium Synechocystis sp. PCC 6803."; RL J. Biol. Chem. 264:18374-18380(1989). 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 (By CC similarity). {ECO:0000250}. 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 -!- 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; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- SUBUNIT: Monomer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the FPG family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA88630.1; Type=Frameshift; Evidence={ECO:0000305}; 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; BA000022; BAA18384.1; -; Genomic_DNA. DR EMBL; J05079; AAA88630.1; ALT_FRAME; Genomic_DNA. DR PIR; S75925; S75925. DR AlphaFoldDB; P74290; -. DR SMR; P74290; -. DR STRING; 1148.gene:10499260; -. DR PaxDb; 1148-1653470; -. DR EnsemblBacteria; BAA18384; BAA18384; BAA18384. DR KEGG; syn:slr1689; -. DR eggNOG; COG0266; Bacteria. DR InParanoid; P74290; -. DR PhylomeDB; P74290; -. DR Proteomes; UP000001425; Chromosome. DR GO; GO:0034039; F:8-oxo-7,8-dihydroguanine DNA N-glycosylase activity; IBA:GO_Central. 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:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0006284; P:base-excision repair; IBA:GO_Central. 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; Reference proteome; Zinc; KW Zinc-finger. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250" FT CHAIN 2..287 FT /note="Formamidopyrimidine-DNA glycosylase" FT /id="PRO_0000170879" FT ZN_FING 249..283 FT /note="FPG-type" FT ACT_SITE 2 FT /note="Schiff-base intermediate with DNA" FT /evidence="ECO:0000250" FT ACT_SITE 3 FT /note="Proton donor" FT /evidence="ECO:0000250" FT ACT_SITE 60 FT /note="Proton donor; for beta-elimination activity" FT /evidence="ECO:0000250" FT ACT_SITE 273 FT /note="Proton donor; for delta-elimination activity" FT /evidence="ECO:0000250" FT BINDING 100 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000250" FT BINDING 119 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000250" FT CONFLICT 129..130 FT /note="GD -> AI (in Ref. 2; AAA88630)" FT /evidence="ECO:0000305" SQ SEQUENCE 287 AA; 32062 MW; FB9B4FE65916CC08 CRC64; MPELPEVETV CRGLNRLTLE QTIGGGEVLL DRSLAYPVSV EDFQKQITGC RLVGWQRRGK YLLGELRSNQ APGPAGWLGC HLRMTGQLLW TERDQQRPRH TRVVLHFEGG WELRFVDTRT FGKVWLLPGD RPWAEVMTGL GQLGPEPFGA DFTAEYLYEK LKSSRRPLKN ALLDQRLVAG LGNIYADEVL FFCGFHPTMA SNQVSLQDCE LIHQQIQATL TAAIEAGGTS FSDYRQVTGI NGNYGGMAQV YGREGEPCRH CGTVIAKIKL GGRSAHFCPQ CQPKLER //