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Database: UniProt
Entry: B5RGF2
LinkDB: B5RGF2
Original site: B5RGF2 
ID   FPG_SALG2               Reviewed;         269 AA.
AC   B5RGF2;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 1.
DT   11-JUN-2014, entry version 42.
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=SG3705;
OS   Salmonella gallinarum (strain 287/91 / NCTC 13346).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=550538;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=287/91 / NCTC 13346;
RX   PubMed=18583645; DOI=10.1101/gr.077404.108;
RA   Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S.,
RA   Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A.,
RA   Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B.,
RA   Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T.,
RA   Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K.,
RA   Moule S., Mungall K., Saunders M., Whitehead S., Chabalgoity J.A.,
RA   Maskell D., Humphreys T., Roberts M., Barrow P.A., Dougan G.,
RA   Parkhill J.;
RT   "Comparative genome analysis of Salmonella enteritidis PT4 and
RT   Salmonella gallinarum 287/91 provides insights into evolutionary and
RT   host adaptation pathways.";
RL   Genome Res. 18:1624-1637(2008).
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; AM933173; CAR39485.1; -; Genomic_DNA.
DR   RefSeq; YP_002228473.1; NC_011274.1.
DR   ProteinModelPortal; B5RGF2; -.
DR   SMR; B5RGF2; 2-269.
DR   STRING; 550538.SG3705; -.
DR   EnsemblBacteria; CAR39485; CAR39485; EBG00000232439.
DR   PATRIC; 18506142; VBISalEnt1629_3931.
DR   eggNOG; COG0266; -.
DR   HOGENOM; HOG000020881; -.
DR   OMA; DHVDLKL; -.
DR   OrthoDB; EOG6QP131; -.
DR   BioCyc; SENT550538:GJ93-3660-MONOMER; -.
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-HAMAP.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-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; 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   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_1000094073.
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;  30223 MW;  72BC9945527AC3E9 CRC64;
     MPELPEVETS RRGIEPHLVG ATILHAHIRN GRLRWPVSDE IYRLSDTPVL SVQRRAKYLL
     LELPDGWIII HLGMSGSLRI LSEALPAEKH DHVDLVMSNG KILRYTDPRR FGAWLWTKEL
     EGHNVLAHLG PEPLSDEFNG EYLQQKCAKK KTAIKPWLMD NKLVVGVGNI YASESLFAAG
     IHPDRLASSL STEECDLLAR VIKAVLLRSI EQGGTTLKDF LQSDGKPGYF AQELQVYGRK
     GEPCRVCGTP IVATKHAQRA TFYCRHCQK
//
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