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Database: UniProt
Entry: C5BLG1
LinkDB: C5BLG1
Original site: C5BLG1 
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   01-OCT-2014, entry version 38.
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=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. {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; CP001614; ACR12438.1; -; Genomic_DNA.
DR   RefSeq; WP_015818550.1; NC_012997.1.
DR   RefSeq; YP_003071862.1; NC_012997.1.
DR   STRING; 377629.TERTU_0178; -.
DR   EnsemblBacteria; ACR12438; ACR12438; 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; AKIHPEK; -.
DR   OrthoDB; EOG6QP131; -.
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: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;
KW   Reference proteome; Zinc; Zinc-finger.
FT   INIT_MET      1      1       Removed. {ECO:0000250}.
FT   CHAIN         2    272       Formamidopyrimidine-DNA glycosylase.
FT                                /FTId=PRO_1000202831.
FT   ZN_FING     238    272       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     58     58       Proton donor; for beta-elimination
FT                                activity. {ECO:0000255|HAMAP-
FT                                Rule:MF_00103}.
FT   ACT_SITE    262    262       Proton donor; for delta-elimination
FT                                activity. {ECO:0000255|HAMAP-
FT                                Rule:MF_00103}.
FT   BINDING      92     92       DNA. {ECO:0000255|HAMAP-Rule:MF_00103}.
FT   BINDING     111    111       DNA. {ECO:0000255|HAMAP-Rule:MF_00103}.
FT   BINDING     153    153       DNA. {ECO:0000255|HAMAP-Rule:MF_00103}.
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
//
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