UNG_ECOLI
ID UNG_ECOLI Reviewed; 229 AA.
AC P12295;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Uracil-DNA glycosylase;
DE Short=UDG;
DE EC=3.2.2.27;
GN Name=ung; OrderedLocusNames=b2580, JW2564;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-32.
RX PubMed=2836397; DOI=10.1016/s0021-9258(18)68566-7;
RA Varshney U., Hutcheon T., de Sande J.H.;
RT "Sequence analysis, expression, and conservation of Escherichia coli uracil
RT DNA glycosylase and its gene (ung).";
RL J. Biol. Chem. 263:7776-7784(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RA Nashimoto H.;
RT "Non-ribosomal proteins affecting the assembly of ribosomes in Escherichia
RT coli.";
RL (In) Nierhaus K.H. (eds.);
RL The translational apparatus, pp.185-195, Plenum Press, New York (1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RA Nashimoto H., Saito N.;
RL Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [7]
RP STRUCTURE BY NMR.
RX PubMed=9261156; DOI=10.1074/jbc.272.34.21408;
RA Lundquist A.J., Beger R.D., Bennett S.E., Bolton P.H., Mosbaugh D.W.;
RT "Site-directed mutagenesis and characterization of uracil-DNA glycosylase
RT inhibitor protein. Role of specific carboxylic amino acids in complex
RT formation with Escherichia coli uracil-DNA glycosylase.";
RL J. Biol. Chem. 272:21408-21419(1997).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS).
RX PubMed=9776748; DOI=10.1093/nar/26.21.4880;
RA Ravishankar R., Sagar M.B., Roy S., Purnapatre K., Handa P., Varshney U.,
RA Vijayan M.;
RT "X-ray analysis of a complex of Escherichia coli uracil DNA glycosylase
RT (EcUDG) with a proteinaceous inhibitor. The structure elucidation of a
RT prokaryotic UDG.";
RL Nucleic Acids Res. 26:4880-4887(1998).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS).
RX PubMed=10080896; DOI=10.1006/jmbi.1999.2605;
RA Putnam C.D., Shroyer M.J.N., Lundquist A.J., Mol C.D., Arvai A.S.,
RA Mosbaugh D.W., Tainer J.A.;
RT "Protein mimicry of DNA from crystal structures of the uracil-DNA
RT glycosylase inhibitor protein and its complex with Escherichia coli uracil-
RT DNA glycosylase.";
RL J. Mol. Biol. 287:331-346(1999).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
RX PubMed=10090282;
RX DOI=10.1002/(sici)1097-0134(19990401)35:1<13::aid-prot2>3.0.co;2-2;
RA Xiao G., Tordova M., Jagadeesh J., Drohat A.C., Stivers J.T.,
RA Gilliland G.L.;
RT "Crystal structure of Escherichia coli uracil DNA glycosylase and its
RT complexes with uracil and glycerol: structure and glycosylase mechanism
RT revisited.";
RL Proteins 35:13-24(1999).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=11027138; DOI=10.1021/bi001532v;
RA Werner R.M., Jiang Y.L., Gordley R.G., Jagadeesh G.J., Ladner J.E.,
RA Xiao G., Tordova M., Gilliland G.L., Stivers J.T.;
RT "Stressing-out DNA? The contribution of serine-phosphodiester interactions
RT in catalysis by uracil DNA glycosylase.";
RL Biochemistry 39:12585-12594(2000).
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.
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 -!- SUBUNIT: Monomer.
CC -!- INTERACTION:
CC P12295; P08957: hsdM; NbExp=3; IntAct=EBI-559403, EBI-878571;
CC P12295; P0A763: ndk; NbExp=3; IntAct=EBI-559403, EBI-370139;
CC P12295; P14739: UGI; Xeno; NbExp=4; IntAct=EBI-559403, EBI-1025973;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily.
CC UNG family. {ECO:0000305}.
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DR EMBL; J03725; AAA24743.1; -; Genomic_DNA.
DR EMBL; D13169; BAA02448.1; -; Genomic_DNA.
DR EMBL; D64044; BAA10923.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75633.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16466.1; -; Genomic_DNA.
DR PIR; A28175; DGECU.
DR RefSeq; NP_417075.1; NC_000913.3.
DR RefSeq; WP_001262716.1; NZ_STEB01000011.1.
DR PDB; 1EUG; X-ray; 1.60 A; A=1-229.
DR PDB; 1EUI; X-ray; 3.20 A; A/B=2-229.
DR PDB; 1FLZ; X-ray; 2.30 A; A=2-229.
DR PDB; 1LQG; X-ray; 2.90 A; A/B=2-229.
DR PDB; 1LQJ; X-ray; 3.35 A; A/B/C/D=2-229.
DR PDB; 1LQM; X-ray; 3.20 A; A/C/E/G=2-229.
DR PDB; 1UUG; X-ray; 2.40 A; A/C=1-229.
DR PDB; 2EUG; X-ray; 1.50 A; A=1-229.
DR PDB; 2UUG; X-ray; 2.60 A; A/B=1-229.
DR PDB; 3EUG; X-ray; 1.43 A; A=1-229.
DR PDB; 3UF7; X-ray; 1.20 A; A=1-229.
DR PDB; 4EUG; X-ray; 1.40 A; A=1-229.
DR PDB; 5EUG; X-ray; 1.60 A; A=1-229.
DR PDBsum; 1EUG; -.
DR PDBsum; 1EUI; -.
DR PDBsum; 1FLZ; -.
DR PDBsum; 1LQG; -.
DR PDBsum; 1LQJ; -.
DR PDBsum; 1LQM; -.
DR PDBsum; 1UUG; -.
DR PDBsum; 2EUG; -.
DR PDBsum; 2UUG; -.
DR PDBsum; 3EUG; -.
DR PDBsum; 3UF7; -.
DR PDBsum; 4EUG; -.
DR PDBsum; 5EUG; -.
DR AlphaFoldDB; P12295; -.
DR SMR; P12295; -.
DR BioGRID; 4263474; 132.
DR BioGRID; 851404; 2.
DR DIP; DIP-11092N; -.
DR IntAct; P12295; 10.
DR STRING; 511145.b2580; -.
DR jPOST; P12295; -.
DR PaxDb; P12295; -.
DR PRIDE; P12295; -.
DR EnsemblBacteria; AAC75633; AAC75633; b2580.
DR EnsemblBacteria; BAA16466; BAA16466; BAA16466.
DR GeneID; 947067; -.
DR KEGG; ecj:JW2564; -.
DR KEGG; eco:b2580; -.
DR PATRIC; fig|1411691.4.peg.4154; -.
DR EchoBASE; EB1051; -.
DR eggNOG; COG0692; Bacteria.
DR HOGENOM; CLU_032162_3_1_6; -.
DR InParanoid; P12295; -.
DR OMA; PDNGYLM; -.
DR PhylomeDB; P12295; -.
DR BioCyc; EcoCyc:EG11058-MON; -.
DR BioCyc; MetaCyc:EG11058-MON; -.
DR BRENDA; 3.2.2.27; 2026.
DR SABIO-RK; P12295; -.
DR EvolutionaryTrace; P12295; -.
DR PRO; PR:P12295; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004844; F:uracil DNA N-glycosylase activity; IDA:EcoCyc.
DR GO; GO:0006284; P:base-excision repair; IMP:EcoCyc.
DR GO; GO:0097510; P:base-excision repair, AP site formation via deaminated base removal; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; DNA damage; DNA repair;
KW Hydrolase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2836397"
FT CHAIN 2..229
FT /note="Uracil-DNA glycosylase"
FT /id="PRO_0000176091"
FT ACT_SITE 64
FT /note="Proton acceptor"
FT HELIX 7..11
FT /evidence="ECO:0007829|PDB:3UF7"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:3UF7"
FT HELIX 18..33
FT /evidence="ECO:0007829|PDB:3UF7"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:3UF7"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:3UF7"
FT HELIX 46..50
FT /evidence="ECO:0007829|PDB:3UF7"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:3UF7"
FT STRAND 58..64
FT /evidence="ECO:0007829|PDB:3UF7"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:3UF7"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:3UF7"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:1LQJ"
FT HELIX 87..99
FT /evidence="ECO:0007829|PDB:3UF7"
FT HELIX 112..115
FT /evidence="ECO:0007829|PDB:3UF7"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:3UF7"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:3UF7"
FT TURN 133..138
FT /evidence="ECO:0007829|PDB:3UF7"
FT HELIX 141..155
FT /evidence="ECO:0007829|PDB:3UF7"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:3UF7"
FT HELIX 166..171
FT /evidence="ECO:0007829|PDB:3UF7"
FT TURN 172..174
FT /evidence="ECO:0007829|PDB:3UF7"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:3UF7"
FT STRAND 180..185
FT /evidence="ECO:0007829|PDB:3UF7"
FT TURN 190..199
FT /evidence="ECO:0007829|PDB:3UF7"
FT HELIX 202..212
FT /evidence="ECO:0007829|PDB:3UF7"
SQ SEQUENCE 229 AA; 25693 MW; CD44F1E214FE74ED CRC64;
MANELTWHDV LAEEKQQPYF LNTLQTVASE RQSGVTIYPP QKDVFNAFRF TELGDVKVVI
LGQDPYHGPG QAHGLAFSVR PGIAIPPSLL NMYKELENTI PGFTRPNHGY LESWARQGVL
LLNTVLTVRA GQAHSHASLG WETFTDKVIS LINQHREGVV FLLWGSHAQK KGAIIDKQRH
HVLKAPHPSP LSAHRGFFGC NHFVLANQWL EQRGETPIDW MPVLPAESE
