ID   UNG_MYCPN               Reviewed;         240 AA.
AC   P75536;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Uracil-DNA glycosylase;
DE            Short=UDG;
DE            EC=3.2.2.27;
GN   Name=ung; OrderedLocusNames=MPN_235; ORFNames=MP596;
OS   Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS   pneumoniae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129;
RX   PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
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:0000250}.
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily.
CC       UNG family. {ECO:0000305}.
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DR   EMBL; U00089; AAB96244.1; -; Genomic_DNA.
DR   PIR; S73922; S73922.
DR   RefSeq; NP_109923.1; NC_000912.1.
DR   RefSeq; WP_010874592.1; NC_000912.1.
DR   AlphaFoldDB; P75536; -.
DR   SMR; P75536; -.
DR   IntAct; P75536; 2.
DR   STRING; 272634.MPN_235; -.
DR   EnsemblBacteria; AAB96244; AAB96244; MPN_235.
DR   GeneID; 66609119; -.
DR   KEGG; mpn:MPN_235; -.
DR   PATRIC; fig|272634.6.peg.254; -.
DR   HOGENOM; CLU_032162_3_2_14; -.
DR   OMA; PDNGYLM; -.
DR   BioCyc; MPNE272634:G1GJ3-375-MON; -.
DR   Proteomes; UP000000808; 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..240
FT                   /note="Uracil-DNA glycosylase"
FT                   /id="PRO_0000176116"
FT   ACT_SITE        70
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   240 AA;  27819 MW;  8CF2B492009F4A2C CRC64;
     MEQLLDQFLS GVLSEWKAFI LQEAKQTYFQ ELLAKLKNVE QELTPKASQV FRPFSFFAPN
     NTKLIIYGQD PYPNPQHACG LSFASNAPKL PQSLKRMILR LQQEYPELAG QNHWTKQLLE
     GWAQQGILLL NGVFTTNAFQ TNAHRNWGWE QFNCHLLDFL LSQKLYVLLV FLGKQTENFV
     LKKIGGASQF ASLSYPHPSP LTGRKFFDHP DALFKQINQW LKHHNHTPID WTNGQVQYQF