ID F4FAI3_MICM1 Unreviewed; 285 AA. AC F4FAI3; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAR-2024, entry version 70. DE RecName: Full=Formamidopyrimidine-DNA glycosylase {ECO:0000256|HAMAP-Rule:MF_00103}; DE Short=Fapy-DNA glycosylase {ECO:0000256|HAMAP-Rule:MF_00103}; DE EC=3.2.2.23 {ECO:0000256|HAMAP-Rule:MF_00103}; DE AltName: Full=DNA-(apurinic or apyrimidinic site) lyase MutM {ECO:0000256|HAMAP-Rule:MF_00103}; DE Short=AP lyase MutM {ECO:0000256|HAMAP-Rule:MF_00103}; DE EC=4.2.99.18 {ECO:0000256|HAMAP-Rule:MF_00103}; GN Name=mutM {ECO:0000256|HAMAP-Rule:MF_00103}; GN Synonyms=fpg {ECO:0000256|HAMAP-Rule:MF_00103}; GN OrderedLocusNames=VAB18032_11480 {ECO:0000313|EMBL:AEB43410.1}; OS Micromonospora maris (strain DSM 45365 / JCM 31040 / NBRC 109089 / NRRL OS B-24793 / AB-18-032) (Verrucosispora maris). OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales; OC Micromonosporaceae; Micromonospora. OX NCBI_TaxID=263358 {ECO:0000313|EMBL:AEB43410.1, ECO:0000313|Proteomes:UP000008308}; RN [1] {ECO:0000313|EMBL:AEB43410.1, ECO:0000313|Proteomes:UP000008308} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AB-18-032 {ECO:0000313|EMBL:AEB43410.1, RC ECO:0000313|Proteomes:UP000008308}; RX PubMed=21551311; DOI=10.1128/JB.05041-11; RA Roh H., Uguru G.C., Ko H.J., Kim S., Kim B.Y., Goodfellow M., Bull A.T., RA Kim K.H., Bibb M.J., Choi I.G., Stach J.E.; RT "Genome sequence of the abyssomicin- and proximicin-producing marine RT actinomycete Verrucosispora maris AB-18-032."; RL J. Bacteriol. 193:3391-3392(2011). 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:0000256|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; CC Evidence={ECO:0000256|ARBA:ARBA00024490, ECO:0000256|HAMAP- CC 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:0000256|ARBA:ARBA00001668, ECO:0000256|HAMAP- CC Rule:MF_00103}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00103}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00103}; CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245, ECO:0000256|HAMAP- CC Rule:MF_00103}. CC -!- SIMILARITY: Belongs to the FPG family. {ECO:0000256|ARBA:ARBA00009409, CC ECO:0000256|HAMAP-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; CP002638; AEB43410.1; -; Genomic_DNA. DR RefSeq; WP_013732080.1; NC_015434.1. DR AlphaFoldDB; F4FAI3; -. DR STRING; 263358.VAB18032_11480; -. DR KEGG; vma:VAB18032_11480; -. DR eggNOG; COG0266; Bacteria. DR HOGENOM; CLU_038423_1_2_11; -. DR Proteomes; UP000008308; 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; 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; PS51066; ZF_FPG_2; 1. PE 3: Inferred from homology; KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP- KW Rule:MF_00103}; KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP- KW Rule:MF_00103}; KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP- KW Rule:MF_00103}; KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|HAMAP- KW Rule:MF_00103}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00103}; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00103}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00103}; KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP- KW Rule:MF_00103}; Reference proteome {ECO:0000313|Proteomes:UP000008308}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00103}; KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|HAMAP- KW Rule:MF_00103}. FT DOMAIN 2..118 FT /note="Formamidopyrimidine-DNA glycosylase catalytic" FT /evidence="ECO:0000259|PROSITE:PS51068" FT DOMAIN 243..277 FT /note="FPG-type" FT /evidence="ECO:0000259|PROSITE:PS51066" FT ACT_SITE 2 FT /note="Schiff-base intermediate with DNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00103" FT ACT_SITE 3 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00103" FT ACT_SITE 61 FT /note="Proton donor; for beta-elimination activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00103" FT ACT_SITE 267 FT /note="Proton donor; for delta-elimination activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00103" FT BINDING 95 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00103" FT BINDING 115 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00103" FT BINDING 157 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00103" SQ SEQUENCE 285 AA; 31500 MW; AFE08BDFBAA5E285 CRC64; MPELPEVETV RQGLARWVTG RRIESVEVRH PRAVRRHVAG GAHFADVLAG RTVLDVCRRG KYLWLPLDSG DAVIGHLGMS GQLLLQPATA PEEPHLRVRF RFTDDGPELR FVDQRTFGGL SVSEGGATLP AEIAHIARDP LDPQFSDADF VTAMRRRRTE VKRALLDQTL ISGVGNIYAD EALWRAGLHG TRPTDALTGP AVRRLLGHVR DVLTEAITAG GTSFDALYVN VNGQSGYFDR SLNVYGREGQ PCRRCGAPIR REAFMNRSSY SCPRCQPRPR ATLRG //