ID   UNG_LACP7               Reviewed;         225 AA.
AC   A9KP29;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_00148};
DE            Short=UDG {ECO:0000255|HAMAP-Rule:MF_00148};
DE            EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_00148};
GN   Name=ung {ECO:0000255|HAMAP-Rule:MF_00148}; OrderedLocusNames=Cphy_2839;
OS   Lachnoclostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg)
OS   (Clostridium phytofermentans).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=357809;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700394 / DSM 18823 / ISDg;
RA   Leschine S.B., Warnick T.A., Blanchard J.L., Schnell D.J., Petit E.L.,
RA   LaTouf W.G., Copeland A., Lucas S., Lapidus A., Barry K.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T.,
RA   Bruce D., Detter J.C., Han C., Kuske C., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E.A., Richardson P.;
RT   "Complete genome sequence of Clostridium phytofermentans ISDg.";
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Excises uracil residues from the DNA which can arise as a
CC       result of misincorporation of dUMP residues by DNA polymerase or due to
CC       deamination of cytosine. {ECO:0000255|HAMAP-Rule:MF_00148}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolyzes single-stranded DNA or mismatched double-stranded
CC         DNA and polynucleotides, releasing free uracil.; EC=3.2.2.27;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00148};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00148}.
CC   -!- SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily.
CC       UNG family. {ECO:0000255|HAMAP-Rule:MF_00148}.
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DR   EMBL; CP000885; ABX43199.1; -; Genomic_DNA.
DR   RefSeq; WP_012200850.1; NC_010001.1.
DR   AlphaFoldDB; A9KP29; -.
DR   SMR; A9KP29; -.
DR   STRING; 357809.Cphy_2839; -.
DR   EnsemblBacteria; ABX43199; ABX43199; Cphy_2839.
DR   KEGG; cpy:Cphy_2839; -.
DR   eggNOG; COG0692; Bacteria.
DR   HOGENOM; CLU_032162_3_0_9; -.
DR   OMA; PDNGYLM; -.
DR   OrthoDB; 1260295at2; -.
DR   Proteomes; UP000000370; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004844; F:uracil DNA N-glycosylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006284; P:base-excision repair; IEA:UniProtKB-UniRule.
DR   CDD; cd10027; UDG-F1-like; 1.
DR   Gene3D; 3.40.470.10; -; 1.
DR   HAMAP; MF_00148; UDG; 1.
DR   InterPro; IPR002043; UDG_fam1.
DR   InterPro; IPR018085; Ura-DNA_Glyclase_AS.
DR   InterPro; IPR005122; Uracil-DNA_glycosylase-like.
DR   InterPro; IPR036895; Uracil-DNA_glycosylase-like_sf.
DR   PANTHER; PTHR11264; PTHR11264; 1.
DR   Pfam; PF03167; UDG; 1.
DR   SMART; SM00986; UDG; 1.
DR   SUPFAM; SSF52141; SSF52141; 1.
DR   TIGRFAMs; TIGR00628; ung; 1.
DR   PROSITE; PS00130; U_DNA_GLYCOSYLASE; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; DNA damage; DNA repair; Hydrolase; Reference proteome.
FT   CHAIN           1..225
FT                   /note="Uracil-DNA glycosylase"
FT                   /id="PRO_1000076670"
FT   ACT_SITE        64
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00148"
SQ   SEQUENCE   225 AA;  25886 MW;  943D6836D004BB7D CRC64;
     MSMIQNDWLD SIGEEFHKPY YKQLYDFVKE EYSQTTIYPL AENIFNAFHF TPLSKVKVLI
     LGQDPYHNVN QAHGLSFSVL PEQKDIPPSL QNIYKELQSD LGCFIPNNGY LKKWADQGVL
     LLNTVLTVRA HQANSHQGRG WEQFTNAIIQ AVNQQDRPIV YLLWGKPAQS KIPMLTNPKH
     LILKAPHPSP LSSYRGFFGS KHFSQTNEFF NANGLEPIDW QIENI