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P12295 (UNG_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Uracil-DNA glycosylase

Short name=UDG
EC=3.2.2.27
Gene names
Name:ung
Ordered Locus Names:b2580, JW2564
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length229 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. HAMAP-Rule MF_00148

Catalytic activity

Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil. HAMAP-Rule MF_00148

Subunit structure

Monomer.

Subcellular location

Cytoplasm HAMAP-Rule MF_00148.

Sequence similarities

Belongs to the uracil-DNA glycosylase family.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
   Cellular componentCytoplasm
   Molecular functionGlycosidase
Hydrolase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processbase-excision repair

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionuracil DNA N-glycosylase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ndkP0A7633EBI-559403,EBI-370139
UGIP147394EBI-559403,EBI-1025973From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 229228Uracil-DNA glycosylase HAMAP-Rule MF_00148
PRO_0000176091

Sites

Active site641Proton acceptor

Secondary structure

............................................ 229
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P12295 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: CD44F1E214FE74ED

FASTA22925,693
        10         20         30         40         50         60 
MANELTWHDV LAEEKQQPYF LNTLQTVASE RQSGVTIYPP QKDVFNAFRF TELGDVKVVI 

        70         80         90        100        110        120 
LGQDPYHGPG QAHGLAFSVR PGIAIPPSLL NMYKELENTI PGFTRPNHGY LESWARQGVL 

       130        140        150        160        170        180 
LLNTVLTVRA GQAHSHASLG WETFTDKVIS LINQHREGVV FLLWGSHAQK KGAIIDKQRH 

       190        200        210        220 
HVLKAPHPSP LSAHRGFFGC NHFVLANQWL EQRGETPIDW MPVLPAESE 

« Hide

References

« Hide 'large scale' references
[1]"Sequence analysis, expression, and conservation of Escherichia coli uracil DNA glycosylase and its gene (ung)."
Varshney U., Hutcheon T., de Sande J.H.
J. Biol. Chem. 263:7776-7784(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-32.
[2]"Non-ribosomal proteins affecting the assembly of ribosomes in Escherichia coli."
Nashimoto H.
(In) Nierhaus K.H. (eds.); The translational apparatus, pp.185-195, Plenum Press, New York (1993)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[3]Nashimoto H., Saito N.
Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[4]"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. expand/collapse author list , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[6]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]"Site-directed mutagenesis and characterization of uracil-DNA glycosylase inhibitor protein. Role of specific carboxylic amino acids in complex formation with Escherichia coli uracil-DNA glycosylase."
Lundquist A.J., Beger R.D., Bennett S.E., Bolton P.H., Mosbaugh D.W.
J. Biol. Chem. 272:21408-21419(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[8]"X-ray analysis of a complex of Escherichia coli uracil DNA glycosylase (EcUDG) with a proteinaceous inhibitor. The structure elucidation of a prokaryotic UDG."
Ravishankar R., Sagar M.B., Roy S., Purnapatre K., Handa P., Varshney U., Vijayan M.
Nucleic Acids Res. 26:4880-4887(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS).
[9]"Protein mimicry of DNA from crystal structures of the uracil-DNA glycosylase inhibitor protein and its complex with Escherichia coli uracil-DNA glycosylase."
Putnam C.D., Shroyer M.J.N., Lundquist A.J., Mol C.D., Arvai A.S., Mosbaugh D.W., Tainer J.A.
J. Mol. Biol. 287:331-346(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS).
[10]"Crystal structure of Escherichia coli uracil DNA glycosylase and its complexes with uracil and glycerol: structure and glycosylase mechanism revisited."
Xiao G., Tordova M., Jagadeesh J., Drohat A.C., Stivers J.T., Gilliland G.L.
Proteins 35:13-24(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
[11]"Stressing-out DNA? The contribution of serine-phosphodiester interactions in catalysis by uracil DNA glycosylase."
Werner R.M., Jiang Y.L., Gordley R.G., Jagadeesh G.J., Ladner J.E., Xiao G., Tordova M., Gilliland G.L., Stivers J.T.
Biochemistry 39:12585-12594(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J03725 Genomic DNA. Translation: AAA24743.1.
D13169 Genomic DNA. Translation: BAA02448.1.
D64044 Genomic DNA. Translation: BAA10923.1.
U00096 Genomic DNA. Translation: AAC75633.1.
AP009048 Genomic DNA. Translation: BAA16466.1.
PIRDGECU. A28175.
RefSeqNP_417075.1. NC_000913.3.
YP_490808.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EUGX-ray1.60A1-229[»]
1EUIX-ray3.20A/B2-229[»]
1FLZX-ray2.30A2-229[»]
1LQGX-ray2.90A/B2-228[»]
1LQJX-ray3.35A/B/C/D2-228[»]
1LQMX-ray3.20A/C/E/G2-228[»]
1UUGX-ray2.40A/C1-229[»]
2EUGX-ray1.50A1-229[»]
2UUGX-ray2.60A/B1-229[»]
3EUGX-ray1.43A1-229[»]
3UF7X-ray1.20A1-229[»]
4EUGX-ray1.40A1-229[»]
5EUGX-ray1.60A1-229[»]
ProteinModelPortalP12295.
SMRP12295. Positions 3-225.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-11092N.
IntActP12295. 10 interactions.
MINTMINT-194643.
STRING511145.b2580.

Proteomic databases

PaxDbP12295.
PRIDEP12295.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75633; AAC75633; b2580.
BAA16466; BAA16466; BAA16466.
GeneID12934480.
947067.
KEGGecj:Y75_p2533.
eco:b2580.
PATRIC32120561. VBIEscCol129921_2683.

Organism-specific databases

EchoBASEEB1051.
EcoGeneEG11058. ung.

Phylogenomic databases

eggNOGCOG0692.
HOGENOMHOG000229528.
KOK03648.
OMAAGKEIYP.
OrthoDBEOG6MSS63.
PhylomeDBP12295.
ProtClustDBPRK05254.

Enzyme and pathway databases

BioCycEcoCyc:EG11058-MONOMER.
ECOL316407:JW2564-MONOMER.
MetaCyc:EG11058-MONOMER.

Gene expression databases

GenevestigatorP12295.

Family and domain databases

Gene3D3.40.470.10. 1 hit.
HAMAPMF_00148. UDG.
InterProIPR018085. Ura-DNA_Glyclase_AS.
IPR002043. Ura_DNA_glycsylse.
IPR005122. Uracil-DNA_glycosylase-like.
[Graphical view]
PANTHERPTHR11264. PTHR11264. 1 hit.
PfamPF03167. UDG. 1 hit.
[Graphical view]
SMARTSM00986. UDG. 1 hit.
[Graphical view]
SUPFAMSSF52141. SSF52141. 1 hit.
TIGRFAMsTIGR00628. ung. 1 hit.
PROSITEPS00130. U_DNA_GLYCOSYLASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP12295.
PROP12295.

Entry information

Entry nameUNG_ECOLI
AccessionPrimary (citable) accession number: P12295
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 136 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene