ID FPG_VIBF1 Reviewed; 272 AA.
AC Q5E8M1;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 01-MAY-2013, entry version 63.
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=VF_0130;
OS Vibrio fischeri (strain ATCC 700601 / ES114).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC Vibrionaceae; Aliivibrio.
OX NCBI_TaxID=312309;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700601 / ES114;
RX PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium
RT with pathogenic congeners.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005).
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; CP000020; AAW84625.1; -; Genomic_DNA.
DR RefSeq; YP_203513.1; NC_006840.2.
DR ProteinModelPortal; Q5E8M1; -.
DR SMR; Q5E8M1; 2-269.
DR STRING; 312309.VF_0130; -.
DR GeneID; 3278022; -.
DR KEGG; vfi:VF_0130; -.
DR PATRIC; 20110743; VBIVibFis127983_0129.
DR eggNOG; COG0266; -.
DR HOGENOM; HOG000020881; -.
DR KO; K10563; -.
DR OMA; VLRYNDP; -.
DR ProtClustDB; PRK01103; -.
DR BioCyc; AFIS312309:GIWP-131-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; 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;
KW Reference proteome; Zinc; Zinc-finger.
FT INIT_MET 1 1 Removed (By similarity).
FT CHAIN 2 272 Formamidopyrimidine-DNA glycosylase.
FT /FTId=PRO_0000228481.
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 272 AA; 30459 MW; 22CA4B3080044A8B CRC64;
MPELPEVETS RLGITPHLQG QTIKAIVVRT DKLRWPIPQE LQKLVGQRVQ SIRRRAKYLM
IDTPKGSAII HLGMSGSLRV LDEEVPSAKH DHVDLVLENG KVLRYNDPRK FGAWLYSEVG
VAHQVLSKLG PEPLTNEFNS EYFAEKAKNK KTVVKQFIMN NAVVVGVGNI YASESLFMAQ
IHPKTSVGSL KASQITLLVA EIKKVLETAI KQGGTTLKDF NQVDGKPGYF AQELHVYGRA
KKKCLLCSSI IQEEKIGQRN TFWCGHCQPF NK
//
