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Formamidopyrimidine-DNA glycosylase (Fapy-DNA glycosylase) (EC 3.2.2.23) (DNA-(apurinic or apyrimidinic site) lyase MutM) (AP lyase MutM) (EC 4.2.99.18)

 FPG_PARXL               Reviewed;         276 AA.
Q145W8;
15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
22-AUG-2006, sequence version 1.
12-SEP-2018, entry version 82.
RecName: Full=Formamidopyrimidine-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_00103};
Short=Fapy-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_00103};
EC=3.2.2.23 {ECO:0000255|HAMAP-Rule:MF_00103};
AltName: Full=DNA-(apurinic or apyrimidinic site) lyase MutM {ECO:0000255|HAMAP-Rule:MF_00103};
Short=AP lyase MutM {ECO:0000255|HAMAP-Rule:MF_00103};
EC=4.2.99.18 {ECO:0000255|HAMAP-Rule:MF_00103};
Name=mutM {ECO:0000255|HAMAP-Rule:MF_00103};
Synonyms=fpg {ECO:0000255|HAMAP-Rule:MF_00103};
OrderedLocusNames=Bxeno_A0333; ORFNames=Bxe_A4129;
Paraburkholderia xenovorans (strain LB400).
Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
Burkholderiaceae; Paraburkholderia.
NCBI_TaxID=266265;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=LB400;
PubMed=17030797; DOI=10.1073/pnas.0606924103;
Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
Tiedje J.M.;
"Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
genome shaped for versatility.";
Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
-!- FUNCTION: Involved in base excision repair of DNA damaged by
oxidation or by mutagenic agents. Acts as DNA glycosylase that
recognizes and removes damaged bases. Has a preference for
oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has
AP (apurinic/apyrimidinic) lyase activity and introduces nicks in
the DNA strand. Cleaves the DNA backbone by beta-delta elimination
to generate a single-strand break at the site of the removed base
with both 3'- and 5'-phosphates. {ECO:0000255|HAMAP-
Rule:MF_00103}.
-!- CATALYTIC ACTIVITY: Hydrolysis of DNA containing ring-opened 7-
methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-
methyl)formamidopyrimidine. {ECO:0000255|HAMAP-Rule:MF_00103}.
-!- CATALYTIC ACTIVITY: The C-O-P bond 3' to the apurinic or
apyrimidinic site in DNA is broken by a beta-elimination reaction,
leaving a 3'-terminal unsaturated sugar and a product with a
terminal 5'-phosphate. {ECO:0000255|HAMAP-Rule:MF_00103}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000255|HAMAP-Rule:MF_00103};
Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-
Rule:MF_00103};
-!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00103}.
-!- SIMILARITY: Belongs to the FPG family. {ECO:0000255|HAMAP-
Rule:MF_00103}.
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EMBL; CP000270; ABE28871.1; -; Genomic_DNA.
RefSeq; WP_011486702.1; NZ_CP008760.1.
ProteinModelPortal; Q145W8; -.
SMR; Q145W8; -.
STRING; 266265.Bxe_A4129; -.
EnsemblBacteria; ABE28871; ABE28871; Bxe_A4129.
GeneID; 4003433; -.
KEGG; bxb:DR64_1805; -.
KEGG; bxe:Bxe_A4129; -.
PATRIC; fig|266265.5.peg.353; -.
eggNOG; ENOG4105ERD; Bacteria.
eggNOG; COG0266; LUCA.
HOGENOM; HOG000020881; -.
KO; K10563; -.
OMA; GVHLRMT; -.
OrthoDB; POG091H01RH; -.
BioCyc; BXEN266265:BXE_RS01670-MONOMER; -.
Proteomes; UP000001817; Chromosome 1.
GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:UniProtKB-EC.
GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
GO; GO:0008534; F:oxidized purine nucleobase lesion DNA N-glycosylase activity; IEA:UniProtKB-EC.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0006284; P:base-excision repair; IEA:InterPro.
GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
Gene3D; 3.20.190.10; -; 1.
HAMAP; MF_00103; Fapy_DNA_glycosyl; 1.
InterPro; IPR015886; DNA_glyclase/AP_lyase_DNA-bd.
InterPro; IPR015887; DNA_glyclase_Znf_dom_DNA_BS.
InterPro; IPR020629; Formamido-pyr_DNA_Glyclase.
InterPro; IPR012319; FPG_cat.
InterPro; IPR035937; MutM-like_N-ter.
InterPro; IPR010979; Ribosomal_S13-like_H2TH.
InterPro; IPR000214; Znf_DNA_glyclase/AP_lyase.
InterPro; IPR010663; Znf_FPG/IleRS.
Pfam; PF01149; Fapy_DNA_glyco; 1.
Pfam; PF06831; H2TH; 1.
Pfam; PF06827; zf-FPG_IleRS; 1.
SMART; SM00898; Fapy_DNA_glyco; 1.
SMART; SM01232; H2TH; 1.
SUPFAM; SSF46946; SSF46946; 1.
SUPFAM; SSF81624; SSF81624; 1.
TIGRFAMs; TIGR00577; fpg; 1.
PROSITE; PS51068; FPG_CAT; 1.
PROSITE; PS01242; ZF_FPG_1; 1.
PROSITE; PS51066; ZF_FPG_2; 1.
3: Inferred from homology;
Complete proteome; DNA damage; DNA repair; DNA-binding; Glycosidase;
Hydrolase; Lyase; Metal-binding; Multifunctional enzyme; Zinc;
Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000250}.
CHAIN 2 276 Formamidopyrimidine-DNA glycosylase.
/FTId=PRO_1000008689.
ZN_FING 242 276 FPG-type. {ECO:0000255|HAMAP-
Rule:MF_00103}.
ACT_SITE 2 2 Schiff-base intermediate with DNA.
{ECO:0000255|HAMAP-Rule:MF_00103}.
ACT_SITE 3 3 Proton donor. {ECO:0000255|HAMAP-
Rule:MF_00103}.
ACT_SITE 58 58 Proton donor; for beta-elimination
activity. {ECO:0000255|HAMAP-
Rule:MF_00103}.
ACT_SITE 266 266 Proton donor; for delta-elimination
activity. {ECO:0000255|HAMAP-
Rule:MF_00103}.
BINDING 94 94 DNA. {ECO:0000255|HAMAP-Rule:MF_00103}.
BINDING 112 112 DNA. {ECO:0000255|HAMAP-Rule:MF_00103}.
BINDING 157 157 DNA. {ECO:0000255|HAMAP-Rule:MF_00103}.
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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