ID   UNG_MYCTO               Reviewed;         227 AA.
AC   P9WFQ8; L0TBF3; P67071; P95119;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 33.
DE   RecName: Full=Uracil-DNA glycosylase;
DE            Short=UDG;
DE            EC=3.2.2.27;
GN   Name=ung; OrderedLocusNames=MT3053;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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; AE000516; AAK47381.1; -; Genomic_DNA.
DR   PIR; E70672; E70672.
DR   RefSeq; WP_003899565.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WFQ8; -.
DR   SMR; P9WFQ8; -.
DR   PRIDE; P9WFQ8; -.
DR   EnsemblBacteria; AAK47381; AAK47381; MT3053.
DR   GeneID; 45426965; -.
DR   KEGG; mtc:MT3053; -.
DR   PATRIC; fig|83331.31.peg.3297; -.
DR   HOGENOM; CLU_032162_3_1_11; -.
DR   Proteomes; UP000001020; 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.
FT   CHAIN           1..227
FT                   /note="Uracil-DNA glycosylase"
FT                   /id="PRO_0000428494"
FT   ACT_SITE        68
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   227 AA;  24481 MW;  379B5DB72894A304 CRC64;
     MTARPLSELV ERGWAAALEP VADQVAHMGQ FLRAEIAAGR RYLPAGSNVL RAFTFPFDNV
     RVLIVGQDPY PTPGHAVGLS FSVAPDVRPW PRSLANIFDE YTADLGYPLP SNGDLTPWAQ
     RGVLLLNRVL TVRPSNPASH RGKGWEAVTE CAIRALAARA APLVAILWGR DASTLKPMLA
     AGNCVAIESP HPSPLSASRG FFGSRPFSRA NELLVGMGAE PIDWRLP