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P12295

- UNG_ECOLI

UniProt

P12295 - UNG_ECOLI

Protein

Uracil-DNA glycosylase

Gene

ung

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    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.

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei64 – 641Proton acceptor

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. uracil DNA N-glycosylase activity Source: EcoCyc

    GO - Biological processi

    1. base-excision repair Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    DNA damage, DNA repair

    Enzyme and pathway databases

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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Uracil-DNA glycosylase (EC:3.2.2.27)
    Short name:
    UDG
    Gene namesi
    Name:ung
    Ordered Locus Names:b2580, JW2564
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG11058. ung.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 229228Uracil-DNA glycosylasePRO_0000176091Add
    BLAST

    Proteomic databases

    PaxDbiP12295.
    PRIDEiP12295.

    Expressioni

    Gene expression databases

    GenevestigatoriP12295.

    Interactioni

    Subunit structurei

    Monomer.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ndkP0A7633EBI-559403,EBI-370139
    UGIP147394EBI-559403,EBI-1025973From a different organism.

    Protein-protein interaction databases

    DIPiDIP-11092N.
    IntActiP12295. 10 interactions.
    MINTiMINT-194643.
    STRINGi511145.b2580.

    Structurei

    Secondary structure

    1
    229
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi7 – 115
    Helixi14 – 163
    Helixi18 – 3316
    Beta strandi37 – 393
    Helixi41 – 433
    Helixi46 – 505
    Helixi53 – 553
    Beta strandi58 – 647
    Turni69 – 713
    Beta strandi74 – 774
    Beta strandi81 – 833
    Helixi87 – 9913
    Helixi112 – 1154
    Turni116 – 1183
    Beta strandi119 – 1257
    Turni133 – 1386
    Helixi141 – 15515
    Beta strandi160 – 1656
    Helixi166 – 1716
    Turni172 – 1743
    Turni177 – 1793
    Beta strandi180 – 1856
    Turni190 – 19910
    Helixi202 – 21211

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EUGX-ray1.60A1-229[»]
    1EUIX-ray3.20A/B2-229[»]
    1FLZX-ray2.30A2-229[»]
    1LQGX-ray2.90A/B2-229[»]
    1LQJX-ray3.35A/B/C/D2-229[»]
    1LQMX-ray3.20A/C/E/G2-229[»]
    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[»]
    ProteinModelPortaliP12295.
    SMRiP12295. Positions 3-225.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP12295.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the uracil-DNA glycosylase family.Curated

    Phylogenomic databases

    eggNOGiCOG0692.
    HOGENOMiHOG000229528.
    KOiK03648.
    OMAiWARQGVM.
    OrthoDBiEOG6MSS63.
    PhylomeDBiP12295.

    Family and domain databases

    Gene3Di3.40.470.10. 1 hit.
    HAMAPiMF_00148. UDG.
    InterProiIPR018085. Ura-DNA_Glyclase_AS.
    IPR002043. Ura_DNA_glycsylse.
    IPR005122. Uracil-DNA_glycosylase-like.
    [Graphical view]
    PANTHERiPTHR11264. PTHR11264. 1 hit.
    PfamiPF03167. UDG. 1 hit.
    [Graphical view]
    SMARTiSM00986. UDG. 1 hit.
    [Graphical view]
    SUPFAMiSSF52141. SSF52141. 1 hit.
    TIGRFAMsiTIGR00628. ung. 1 hit.
    PROSITEiPS00130. U_DNA_GLYCOSYLASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P12295-1 [UniParc]FASTAAdd to Basket

    « Hide

    MANELTWHDV LAEEKQQPYF LNTLQTVASE RQSGVTIYPP QKDVFNAFRF    50
    TELGDVKVVI LGQDPYHGPG QAHGLAFSVR PGIAIPPSLL NMYKELENTI 100
    PGFTRPNHGY LESWARQGVL LLNTVLTVRA GQAHSHASLG WETFTDKVIS 150
    LINQHREGVV FLLWGSHAQK KGAIIDKQRH HVLKAPHPSP LSAHRGFFGC 200
    NHFVLANQWL EQRGETPIDW MPVLPAESE 229
    Length:229
    Mass (Da):25,693
    Last modified:January 23, 2007 - v2
    Checksum:iCD44F1E214FE74ED
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    PIRiA28175. DGECU.
    RefSeqiNP_417075.1. NC_000913.3.
    YP_490808.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75633; AAC75633; b2580.
    BAA16466; BAA16466; BAA16466.
    GeneIDi12934480.
    947067.
    KEGGiecj:Y75_p2533.
    eco:b2580.
    PATRICi32120561. VBIEscCol129921_2683.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    PIRi A28175. DGECU.
    RefSeqi NP_417075.1. NC_000913.3.
    YP_490808.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EUG X-ray 1.60 A 1-229 [» ]
    1EUI X-ray 3.20 A/B 2-229 [» ]
    1FLZ X-ray 2.30 A 2-229 [» ]
    1LQG X-ray 2.90 A/B 2-229 [» ]
    1LQJ X-ray 3.35 A/B/C/D 2-229 [» ]
    1LQM X-ray 3.20 A/C/E/G 2-229 [» ]
    1UUG X-ray 2.40 A/C 1-229 [» ]
    2EUG X-ray 1.50 A 1-229 [» ]
    2UUG X-ray 2.60 A/B 1-229 [» ]
    3EUG X-ray 1.43 A 1-229 [» ]
    3UF7 X-ray 1.20 A 1-229 [» ]
    4EUG X-ray 1.40 A 1-229 [» ]
    5EUG X-ray 1.60 A 1-229 [» ]
    ProteinModelPortali P12295.
    SMRi P12295. Positions 3-225.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-11092N.
    IntActi P12295. 10 interactions.
    MINTi MINT-194643.
    STRINGi 511145.b2580.

    Proteomic databases

    PaxDbi P12295.
    PRIDEi P12295.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC75633 ; AAC75633 ; b2580 .
    BAA16466 ; BAA16466 ; BAA16466 .
    GeneIDi 12934480.
    947067.
    KEGGi ecj:Y75_p2533.
    eco:b2580.
    PATRICi 32120561. VBIEscCol129921_2683.

    Organism-specific databases

    EchoBASEi EB1051.
    EcoGenei EG11058. ung.

    Phylogenomic databases

    eggNOGi COG0692.
    HOGENOMi HOG000229528.
    KOi K03648.
    OMAi WARQGVM.
    OrthoDBi EOG6MSS63.
    PhylomeDBi P12295.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG11058-MONOMER.
    ECOL316407:JW2564-MONOMER.
    MetaCyc:EG11058-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P12295.
    PROi P12295.

    Gene expression databases

    Genevestigatori P12295.

    Family and domain databases

    Gene3Di 3.40.470.10. 1 hit.
    HAMAPi MF_00148. UDG.
    InterProi IPR018085. Ura-DNA_Glyclase_AS.
    IPR002043. Ura_DNA_glycsylse.
    IPR005122. Uracil-DNA_glycosylase-like.
    [Graphical view ]
    PANTHERi PTHR11264. PTHR11264. 1 hit.
    Pfami PF03167. UDG. 1 hit.
    [Graphical view ]
    SMARTi SM00986. UDG. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52141. SSF52141. 1 hit.
    TIGRFAMsi TIGR00628. ung. 1 hit.
    PROSITEi PS00130. U_DNA_GLYCOSYLASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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).

    Entry informationi

    Entry nameiUNG_ECOLI
    AccessioniPrimary (citable) accession number: P12295
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 140 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3