(data stored in ACNUC7421 zone)

SWISSPROT: FPG_PARXL

ID   FPG_PARXL               Reviewed;         276 AA.
AC   Q145W8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 87.
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=Bxeno_A0333; ORFNames=Bxe_A4129;
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400;
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(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:
CC       Reaction=Hydrolysis of DNA containing ring-opened 7-methylguanine
CC         residues, releasing 2,6-diamino-4-hydroxy-5-(N-
CC         methyl)formamidopyrimidine.; EC=3.2.2.23;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00103};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=The C-O-P bond 3' to the apurinic or apyrimidinic site in
CC         DNA is broken by a beta-elimination reaction, leaving a 3'-
CC         terminal unsaturated sugar and a product with a terminal 5'-
CC         phosphate.; EC=4.2.99.18; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00103};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00103};
CC       Note=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}.
DR   EMBL; CP000270; ABE28871.1; -; Genomic_DNA.
DR   RefSeq; WP_011486702.1; NZ_CP008760.1.
DR   SMR; Q145W8; -.
DR   STRING; 266265.Bxe_A4129; -.
DR   EnsemblBacteria; ABE28871; ABE28871; Bxe_A4129.
DR   GeneID; 4003433; -.
DR   KEGG; bxb:DR64_1805; -.
DR   KEGG; bxe:Bxe_A4129; -.
DR   PATRIC; fig|266265.5.peg.353; -.
DR   eggNOG; ENOG4105ERD; Bacteria.
DR   eggNOG; COG0266; LUCA.
DR   HOGENOM; HOG000020881; -.
DR   KO; K10563; -.
DR   OMA; GVHLRMT; -.
DR   OrthoDB; 1162346at2; -.
DR   BioCyc; BXEN266265:BXE_RS01670-MONOMER; -.
DR   Proteomes; UP000001817; Chromosome 1.
DR   GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:UniProtKB-EC.
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-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR   GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR   Gene3D; 3.20.190.10; -; 1.
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; IPR020629; Formamido-pyr_DNA_Glyclase.
DR   InterPro; IPR012319; FPG_cat.
DR   InterPro; IPR035937; MutM-like_N-ter.
DR   InterPro; IPR010979; Ribosomal_S13-like_H2TH.
DR   InterPro; IPR000214; Znf_DNA_glyclase/AP_lyase.
DR   InterPro; IPR010663; Znf_FPG/IleRS.
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   SMART; SM01232; H2TH; 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;
DR   PRODOM; Q145W8.
DR   SWISS-2DPAGE; Q145W8.
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    276       Formamidopyrimidine-DNA glycosylase.
FT                                /FTId=PRO_1000008689.
FT   ZN_FING     242    276       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    266    266       Proton donor; for delta-elimination
FT                                activity. {ECO:0000255|HAMAP-
FT                                Rule:MF_00103}.
FT   BINDING      94     94       DNA. {ECO:0000255|HAMAP-Rule:MF_00103}.
FT   BINDING     112    112       DNA. {ECO:0000255|HAMAP-Rule:MF_00103}.
FT   BINDING     157    157       DNA. {ECO:0000255|HAMAP-Rule:MF_00103}.
SQ   SEQUENCE   276 AA;  30808 MW;  6051EEF13F678AFA CRC64;
     MPELPEVEVT RRGIEPYVSG RKVERVEVRT PALRWPIPAD LAKTLRGRVV RKVERRGKYL
     LFEIDAGWFI VHLGMTGTLR VLRHVPHPPA AAKHDHVDWI FDEFILRYRD PRRFGAVLWH
     PREAGDVLEH PLLAGLGVEP FSPAFSGALM HRLTRGRKVS VKQALLAGEI VVGVGNIYAS
     ESLFRAGIRP ATAAGRVSLV RYDLLADAVR VTLAAAIEKG GSTLRDFVGS NGESGYFQLD
     YFVYDRAGLP CRVCGTPIKQ IVQGQRSTYF CPTCQR
//

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