FPG_STRMK
ID FPG_STRMK Reviewed; 270 AA.
AC B2FU49;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
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}; OrderedLocusNames=Smlt0090;
OS Stenotrophomonas maltophilia (strain K279a).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX NCBI_TaxID=522373;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K279a;
RX PubMed=18419807; DOI=10.1186/gb-2008-9-4-r74;
RA Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A.,
RA Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E.,
RA Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S.,
RA Quail M.A., Rajandream M.A., Harris D., Churcher C., Bentley S.D.,
RA Parkhill J., Thomson N.R., Avison M.B.;
RT "The complete genome, comparative and functional analysis of
RT Stenotrophomonas maltophilia reveals an organism heavily shielded by drug
RT resistance determinants.";
RL Genome Biol. 9:R74.1-R74.13(2008).
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; AM743169; CAQ43701.1; -; Genomic_DNA.
DR RefSeq; WP_005407488.1; NC_010943.1.
DR AlphaFoldDB; B2FU49; -.
DR SMR; B2FU49; -.
DR STRING; 522373.Smlt0090; -.
DR EnsemblBacteria; CAQ43701; CAQ43701; Smlt0090.
DR GeneID; 61464081; -.
DR KEGG; sml:Smlt0090; -.
DR eggNOG; COG0266; Bacteria.
DR HOGENOM; CLU_038423_1_1_6; -.
DR OMA; GVHLRMT; -.
DR OrthoDB; 1162346at2; -.
DR Proteomes; UP000008840; 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; Reference proteome; Zinc;
KW 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_1000094082"
FT ZN_FING 236..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 91
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00103"
FT BINDING 110
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00103"
FT BINDING 151
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00103"
SQ SEQUENCE 270 AA; 29862 MW; 96A517A23322B26C CRC64;
MPELPEVETT RRGLAPHLQG RRVHGVILRR ADLRWPIPPE VAELLPGQRI EDIRRRAKYL
LLDTAIGSAV LHLGMSGSLR VLPGDTPLRA HDHVDISLDN GRLLRFNDPR RFGSLLWQPA
GEVHPLLQGL GPEPLDDAFD GDYLFARSRG RSAPVKTFLM DQAVVVGVGN IYAAESLFKA
GISPLREAGK ISRERYQRLA DAVKEILGYA ITRGGTTLRD FISPDGAPGY FEQELLVYGR
DGLPCPNCGR ALKHATIGQR ASVWCSHCQR
