ID FPG_TERTT Reviewed; 272 AA.
AC C5BLG1;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 29-MAY-2013, entry version 30.
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=TERTU_0178;
OS Teredinibacter turnerae (strain ATCC 39867 / T7901).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Alteromonadales genera incertae sedis; Teredinibacter.
OX NCBI_TaxID=377629;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39867 / T7901;
RX PubMed=19568419; DOI=10.1371/journal.pone.0006085;
RA Yang J.C., Madupu R., Durkin A.S., Ekborg N.A., Pedamallu C.S.,
RA Hostetler J.B., Radune D., Toms B.S., Henrissat B., Coutinho P.M.,
RA Schwarz S., Field L., Trindade-Silva A.E., Soares C.A.G.,
RA Elshahawi S., Hanora A., Schmidt E.W., Haygood M.G., Posfai J.,
RA Benner J., Madinger C., Nove J., Anton B., Chaudhary K., Foster J.,
RA Holman A., Kumar S., Lessard P.A., Luyten Y.A., Slatko B., Wood N.,
RA Wu B., Teplitski M., Mougous J.D., Ward N., Eisen J.A., Badger J.H.,
RA Distel D.L.;
RT "The complete genome of Teredinibacter turnerae T7901: an
RT intracellular endosymbiont of marine wood-boring bivalves
RT (shipworms).";
RL PLoS ONE 4:E6085-E6085(2009).
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; CP001614; ACR12438.1; -; Genomic_DNA.
DR RefSeq; YP_003071862.1; NC_012997.1.
DR STRING; 377629.TERTU_0178; -.
DR GeneID; 8214325; -.
DR KEGG; ttu:TERTU_0178; -.
DR PATRIC; 23867607; VBITerTur118718_0166.
DR eggNOG; COG0266; -.
DR HOGENOM; HOG000020881; -.
DR KO; K10563; -.
DR OMA; NIHASEA; -.
DR ProtClustDB; PRK01103; -.
DR BioCyc; TTUR377629:GHSU-161-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; Zinc;
KW Zinc-finger.
FT INIT_MET 1 1 Removed (By similarity).
FT CHAIN 2 272 Formamidopyrimidine-DNA glycosylase.
FT /FTId=PRO_1000202831.
FT ZN_FING 238 272 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 58 58 Proton donor; for beta-elimination
FT activity (By similarity).
FT ACT_SITE 262 262 Proton donor; for delta-elimination
FT activity (By similarity).
FT BINDING 92 92 DNA (By similarity).
FT BINDING 111 111 DNA (By similarity).
FT BINDING 153 153 DNA (By similarity).
SQ SEQUENCE 272 AA; 30375 MW; D8B9774910206C31 CRC64;
MPELPEVETT RRGIAPHILH HPITAVTLRH TQLRWPIDKA LSRNLPGRTL VRADRRGKYL
LLAVDDGRTL IWHLGMSGSL RIVEPTEPPG KHDHIDLRFA HGRVLRYHDP RRFGAFLATA
DDPAQHALIC HLGPEPLTDD FNGEYLYERS RKRSTAVKSW IMDSRVVVGV GNIYANESLF
LAKIHPLRAA GKLTRPACHR LADIIKAVLA RSITQGGTTL RDFVGGDGKP GYFAQQLNVY
GRGGEPCPVC AKPLTEKPLS QRTTVYCTHC QN
//
