ID FPG_SHIFL Reviewed; 269 AA.
AC P64149; Q8XDA9;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 01-MAY-2013, entry version 70.
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=SF3674, S4094;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H.,
RA Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J.,
RA Sun L., Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S.,
RA Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y.,
RA Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/IAI.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W.,
RA Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A.,
RA Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S.,
RA Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella
RT flexneri serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
CC -!- FUNCTION: Involved in base excision repair of DNA damaged by
CC oxidation or by mutagenic agents. Acts as DNA glycosylase that
CC recognizes and removes damaged bases. Has a preference for
CC oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has
CC AP (apurinic/apyrimidinic) lyase activity and introduces nicks in
CC the DNA strand. Cleaves the DNA backbone by beta-delta elimination
CC to generate a single-strand break at the site of the removed base
CC with both 3'- and 5'-phosphates (By similarity).
CC -!- CATALYTIC ACTIVITY: Hydrolysis of DNA containing ring-opened 7-
CC methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-
CC methyl)formamidopyrimidine.
CC -!- CATALYTIC ACTIVITY: The C-O-P bond 3' to the apurinic or
CC apyrimidinic site in DNA is broken by a beta-elimination reaction,
CC leaving a 3'-terminal unsaturated sugar and a product with a
CC terminal 5'-phosphate.
CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC -!- SUBUNIT: Monomer (By similarity).
CC -!- SIMILARITY: Belongs to the FPG family.
CC -!- SIMILARITY: Contains 1 FPG-type zinc finger.
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DR EMBL; AE005674; AAN45121.2; -; Genomic_DNA.
DR EMBL; AE014073; AAP19071.1; -; Genomic_DNA.
DR RefSeq; NP_709414.2; NC_004337.2.
DR RefSeq; NP_839260.1; NC_004741.1.
DR ProteinModelPortal; P64149; -.
DR SMR; P64149; 2-269.
DR STRING; 198214.SF3674; -.
DR EnsemblBacteria; EBESCT00000086171; EBESCP00000082993; EBESCG00000085216.
DR EnsemblBacteria; EBESCT00000093320; EBESCP00000089956; EBESCG00000092364.
DR GeneID; 1026213; -.
DR GeneID; 1080301; -.
DR KEGG; sfl:SF3674; -.
DR KEGG; sfx:S4094; -.
DR PATRIC; 18710100; VBIShiFle31049_4457.
DR eggNOG; COG0266; -.
DR HOGENOM; HOG000020881; -.
DR KO; K10563; -.
DR ProtClustDB; PRK01103; -.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0008534; F:oxidized purine nucleobase lesion DNA N-glycosylase activity; IEA:HAMAP.
DR GO; GO:0008270; F:zinc ion binding; IEA:HAMAP.
DR GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
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; IPR000191; DNA_glycosylase/AP_lyase.
DR InterPro; IPR012319; DNA_glycosylase/AP_lyase_cat.
DR InterPro; IPR020629; Formamido-pyr_DNA_Glyclase.
DR InterPro; IPR010979; Ribosomal_S13-like_H2TH.
DR InterPro; IPR000214; Znf_DNA_glyclase/AP_lyase.
DR InterPro; IPR010663; Znf_DNA_glyclase/IsotRNA_synth.
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 SUPFAM; SSF81624; Form_DNAglyc_cat; 1.
DR SUPFAM; SSF46946; Ribosomal_H2TH; 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 Complete proteome; DNA damage; DNA repair; DNA-binding; Glycosidase;
KW Hydrolase; Lyase; Metal-binding; Multifunctional enzyme; Zinc;
KW Zinc-finger.
FT INIT_MET 1 1 Removed (By similarity).
FT CHAIN 2 269 Formamidopyrimidine-DNA glycosylase.
FT /FTId=PRO_0000170863.
FT ZN_FING 235 269 FPG-type.
FT ACT_SITE 2 2 Schiff-base intermediate with DNA (By
FT similarity).
FT ACT_SITE 3 3 Proton donor (By similarity).
FT ACT_SITE 57 57 Proton donor; for beta-elimination
FT activity (By similarity).
FT ACT_SITE 259 259 Proton donor; for delta-elimination
FT activity (By similarity).
FT BINDING 90 90 DNA (By similarity).
FT BINDING 109 109 DNA (By similarity).
FT BINDING 150 150 DNA (By similarity).
SQ SEQUENCE 269 AA; 30260 MW; EF83DF7E15473DEC CRC64;
MPELPEVETS RRGIEPHLVG ATILHAVVRN GRLRWPVSEE IYRLSDQPVL SVQRRAKYLL
LELPEGWIII HLGMSGSLRI LPEELPPEKH DHVDLVMSNG KVLRYTDPRR FGAWLWTKEL
EGHNVLAHLG PEPLSDDFNG EYLHQKCAKK KTAIKPWLMD NKLVVGVGNI YASESLFAAG
IHPDRLASSL SLAECELLAR VIKAVLLRSI EQGGTTLKDF LQSDGKPGYF AQELQVYGRK
GEPCRVCGTP IVATKHAQRA TFYCRQCQK
//
