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Database: UniProt
Entry: Q0S2E0
LinkDB: Q0S2E0
Original site: Q0S2E0 
ID   FPG_RHOSR               Reviewed;         292 AA.
AC   Q0S2E0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   01-OCT-2014, entry version 63.
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};
GN   OrderedLocusNames=RHA1_ro06523;
OS   Rhodococcus sp. (strain RHA1).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=101510;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHA1;
RX   PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA   McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M.,
RA   Fernandes C., Miyazawa D., Wong W., Lillquist A.L., Wang D.,
RA   Dosanjh M., Hara H., Petrescu A., Morin R.D., Yang G., Stott J.M.,
RA   Schein J.E., Shin H., Smailus D., Siddiqui A.S., Marra M.A.,
RA   Jones S.J.M., Holt R., Brinkman F.S.L., Miyauchi K., Fukuda M.,
RA   Davies J.E., Mohn W.W., Eltis L.D.;
RT   "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT   catabolic powerhouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
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. {ECO:0000255|HAMAP-
CC       Rule:MF_00103}.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of DNA containing ring-opened 7-
CC       methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-
CC       methyl)formamidopyrimidine. {ECO:0000255|HAMAP-Rule:MF_00103}.
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. {ECO:0000255|HAMAP-Rule:MF_00103}.
CC   -!- COFACTOR: Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-
CC       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}.
CC   -!- SIMILARITY: Contains 1 FPG-type zinc finger. {ECO:0000255|HAMAP-
CC       Rule:MF_00103}.
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DR   EMBL; CP000431; ABG98296.1; -; Genomic_DNA.
DR   RefSeq; YP_706454.1; NC_008268.1.
DR   ProteinModelPortal; Q0S2E0; -.
DR   STRING; 101510.RHA1_ro06523; -.
DR   PRIDE; Q0S2E0; -.
DR   EnsemblBacteria; ABG98296; ABG98296; RHA1_ro06523.
DR   GeneID; 4224074; -.
DR   KEGG; rha:RHA1_ro06523; -.
DR   PATRIC; 23212011; VBIRhoJos26306_6577.
DR   eggNOG; COG0266; -.
DR   HOGENOM; HOG000020884; -.
DR   KO; K10563; -.
DR   OMA; IYCSESL; -.
DR   OrthoDB; EOG6QP131; -.
DR   BioCyc; RJOS101510:GJJ1-6520-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; 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; 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;
KW   Reference proteome; Zinc; Zinc-finger.
FT   INIT_MET      1      1       Removed. {ECO:0000250}.
FT   CHAIN         2    292       Formamidopyrimidine-DNA glycosylase.
FT                                /FTId=PRO_1000008760.
FT   ZN_FING     247    281       FPG-type. {ECO:0000255|HAMAP-
FT                                Rule:MF_00103}.
FT   ACT_SITE      2      2       Schiff-base intermediate with DNA.
FT                                {ECO:0000255|HAMAP-Rule:MF_00103}.
FT   ACT_SITE      3      3       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00103}.
FT   ACT_SITE     61     61       Proton donor; for beta-elimination
FT                                activity. {ECO:0000255|HAMAP-
FT                                Rule:MF_00103}.
FT   ACT_SITE    271    271       Proton donor; for delta-elimination
FT                                activity. {ECO:0000255|HAMAP-
FT                                Rule:MF_00103}.
FT   BINDING      96     96       DNA. {ECO:0000255|HAMAP-Rule:MF_00103}.
FT   BINDING     115    115       DNA. {ECO:0000255|HAMAP-Rule:MF_00103}.
FT   BINDING     161    161       DNA. {ECO:0000255|HAMAP-Rule:MF_00103}.
SQ   SEQUENCE   292 AA;  32193 MW;  4B7F2DFC8481B1DD CRC64;
     MPELPEVEVV RRGLERHIVG ASIDSVDILH PRAIRRHLPG AADLAGQLTG ERIASADRRG
     KYLWLVLEPS TVALVVHLGM SGQMLVQPPE LPTEKHLRIR ARLDSGLDLR FVDQRTFGGW
     ALAPLVDVDG SLVPDSVAHI ARDPLDPRFD LAATVKVVRG KHTEVKRALL DQTVVSGIGN
     IYADEALWRA RIHGNRLTDR LSGPKVREVL TAAQEVMREA LTQGGTSFDA LYVNVNGESG
     YFDRSLSAYG QEDRPCPRCG TAIRREKFMN RSSFSCPKCQ PAPRRSLAKS SV
//
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