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-MAY-2013, entry version 55.
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=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 (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; CP000431; ABG98296.1; -; Genomic_DNA.
DR RefSeq; YP_706454.1; NC_008268.1.
DR ProteinModelPortal; Q0S2E0; -.
DR STRING; 101510.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; RREKFMN; -.
DR ProtClustDB; PRK01103; -.
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: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; 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; FALSE_NEG.
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 2 292 Formamidopyrimidine-DNA glycosylase.
FT /FTId=PRO_1000008760.
FT ZN_FING 247 281 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 61 61 Proton donor; for beta-elimination
FT activity (By similarity).
FT ACT_SITE 271 271 Proton donor; for delta-elimination
FT activity (By similarity).
FT BINDING 96 96 DNA (By similarity).
FT BINDING 115 115 DNA (By similarity).
FT BINDING 161 161 DNA (By similarity).
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
//
