UNG_BIFLO
ID UNG_BIFLO Reviewed; 213 AA.
AC Q8G3E9;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=BL1812;
OS Bifidobacterium longum (strain NCC 2705).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=206672;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCC 2705;
RX PubMed=12381787; DOI=10.1073/pnas.212527599;
RA Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT the human gastrointestinal tract.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(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: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; AE014295; AAN25596.1; -; Genomic_DNA.
DR RefSeq; NP_696959.1; NC_004307.2.
DR AlphaFoldDB; Q8G3E9; -.
DR SMR; Q8G3E9; -.
DR STRING; 206672.BL1812; -.
DR EnsemblBacteria; AAN25596; AAN25596; BL1812.
DR KEGG; blo:BL1812; -.
DR PATRIC; fig|206672.9.peg.1865; -.
DR HOGENOM; CLU_032162_3_1_11; -.
DR OMA; WEAVTEQ; -.
DR PhylomeDB; Q8G3E9; -.
DR Proteomes; UP000000439; 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 PROSITE; PS00130; U_DNA_GLYCOSYLASE; 1.
PE 3: Inferred from homology;
KW Cytoplasm; DNA damage; DNA repair; Hydrolase; Reference proteome.
FT CHAIN 1..213
FT /note="Uracil-DNA glycosylase"
FT /id="PRO_0000176069"
FT ACT_SITE 51
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00148"
SQ SEQUENCE 213 AA; 23105 MW; E9D40795369414EB CRC64;
MADVEPTIHH MGDFLRAENA AGRPWLPASH NILRAFTIPF DSIKVLIVGQ DPYPTPGHPV
GLSFCVAPNV HPLPKSLVNI YKELVDDLGV PMPTNGDLTP WTERGVMLLN RCLTVGVGRP
NSHQGKGWEE VTEAAIRALN ARTDADGKPQ PLVAILWGRN AQSLEPLLTN AFIIKSPHPS
PLSASRGFFG SKPFSRANQA LVTMGADPVD WTL