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P0A9H1

- MUG_ECOLI

UniProt

P0A9H1 - MUG_ECOLI

Protein

G/U mismatch-specific DNA glycosylase

Gene

mug

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 76 (01 Oct 2014)
      Sequence version 1 (19 Jul 2005)
      Previous versions | rss
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    Functioni

    Excises ethenocytosine and uracil, which can arise by alkylation or deamination of cytosine, respectively, from the corresponding mispairs with guanine in ds-DNA. It is capable of hydrolyzing the carbon-nitrogen bond between the sugar-phosphate backbone of the DNA and the mispaired base. The complementary strand guanine functions in substrate recognition. Required for DNA damage lesion repair in stationary-phase cells.2 Publications

    Catalytic activityi

    Specifically hydrolyzes mismatched double-stranded DNA and polynucleotides, releasing free uracil.

    Enzyme regulationi

    Subject to strong product inhibition. N-glycosyl hydrolysis proceeds 100-fold faster than product release.

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. pyrimidine-specific mismatch base pair DNA N-glycosylase activity Source: EcoCyc

    GO - Biological processi

    1. base-excision repair, AP site formation Source: EcoCyc

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    DNA damage, DNA excision, DNA repair

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:EG12717-MONOMER.
    ECOL316407:JW3040-MONOMER.
    MetaCyc:EG12717-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    G/U mismatch-specific DNA glycosylase (EC:3.2.2.28)
    Alternative name(s):
    Double-strand-specific uracil glycosylase
    Mismatch-specific uracil DNA-glycosylase
    Short name:
    MUG
    Gene namesi
    Name:mug
    Synonyms:ygjF
    Ordered Locus Names:b3068, JW3040
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG12717. mug.

    Subcellular locationi

    Cytoplasm Curated

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 168168G/U mismatch-specific DNA glycosylasePRO_0000185774Add
    BLAST

    Proteomic databases

    PaxDbiP0A9H1.
    PRIDEiP0A9H1.

    Expressioni

    Inductioni

    Induced in stationary phase.1 Publication

    Gene expression databases

    GenevestigatoriP0A9H1.

    Interactioni

    Subunit structurei

    Binds DNA as a monomer.3 Publications

    Protein-protein interaction databases

    IntActiP0A9H1. 21 interactions.
    STRINGi511145.b3068.

    Structurei

    Secondary structure

    1
    168
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi11 – 188
    Helixi21 – 266
    Helixi37 – 437
    Beta strandi46 – 494
    Helixi53 – 6210
    Beta strandi64 – 696
    Beta strandi74 – 763
    Helixi77 – 793
    Helixi82 – 9918
    Beta strandi102 – 1076
    Helixi109 – 1168
    Beta strandi123 – 1308
    Beta strandi133 – 1386
    Helixi149 – 16214

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1MTLX-ray2.80A/B1-168[»]
    1MUGX-ray1.80A1-168[»]
    1MWIX-ray2.35A1-168[»]
    1MWJX-ray2.85A1-168[»]
    ProteinModelPortaliP0A9H1.
    SMRiP0A9H1. Positions 1-165.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A9H1.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the TDG/mug DNA glycosylase family.Curated

    Phylogenomic databases

    eggNOGiCOG3663.
    HOGENOMiHOG000264684.
    KOiK03649.
    OMAiETGCGIT.
    OrthoDBiEOG68H872.
    PhylomeDBiP0A9H1.

    Family and domain databases

    Gene3Di3.40.470.10. 1 hit.
    HAMAPiMF_01956. MUG.
    InterProiIPR023502. DNA_glyclase_G/T-mismatch_bac.
    IPR015637. DNA_glycosylase_G/T-mismatch.
    IPR005122. Uracil-DNA_glycosylase-like.
    [Graphical view]
    PANTHERiPTHR12159. PTHR12159. 1 hit.
    PfamiPF03167. UDG. 1 hit.
    [Graphical view]
    SMARTiSM00986. UDG. 1 hit.
    [Graphical view]
    SUPFAMiSSF52141. SSF52141. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P0A9H1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVEDILAPGL RVVFCGINPG LSSAGTGFPF AHPANRFWKV IYQAGFTDRQ    50
    LKPQEAQHLL DYRCGVTKLV DRPTVQANEV SKQELHAGGR KLIEKIEDYQ 100
    PQALAILGKQ AYEQGFSQRG AQWGKQTLTI GSTQIWVLPN PSGLSRVSLE 150
    KLVEAYRELD QALVVRGR 168
    Length:168
    Mass (Da):18,673
    Last modified:July 19, 2005 - v1
    Checksum:iF1CD9B2E2030D6A7
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U28379 Genomic DNA. Translation: AAA89148.1.
    U00096 Genomic DNA. Translation: AAC76104.1.
    AP009048 Genomic DNA. Translation: BAE77119.1.
    J01687 Genomic DNA. No translation available.
    PIRiB65095.
    RefSeqiNP_417540.1. NC_000913.3.
    YP_491260.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76104; AAC76104; b3068.
    BAE77119; BAE77119; BAE77119.
    GeneIDi12933393.
    947560.
    KEGGiecj:Y75_p2994.
    eco:b3068.
    PATRICi32121552. VBIEscCol129921_3163.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U28379 Genomic DNA. Translation: AAA89148.1 .
    U00096 Genomic DNA. Translation: AAC76104.1 .
    AP009048 Genomic DNA. Translation: BAE77119.1 .
    J01687 Genomic DNA. No translation available.
    PIRi B65095.
    RefSeqi NP_417540.1. NC_000913.3.
    YP_491260.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1MTL X-ray 2.80 A/B 1-168 [» ]
    1MUG X-ray 1.80 A 1-168 [» ]
    1MWI X-ray 2.35 A 1-168 [» ]
    1MWJ X-ray 2.85 A 1-168 [» ]
    ProteinModelPortali P0A9H1.
    SMRi P0A9H1. Positions 1-165.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P0A9H1. 21 interactions.
    STRINGi 511145.b3068.

    Proteomic databases

    PaxDbi P0A9H1.
    PRIDEi P0A9H1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76104 ; AAC76104 ; b3068 .
    BAE77119 ; BAE77119 ; BAE77119 .
    GeneIDi 12933393.
    947560.
    KEGGi ecj:Y75_p2994.
    eco:b3068.
    PATRICi 32121552. VBIEscCol129921_3163.

    Organism-specific databases

    EchoBASEi EB2576.
    EcoGenei EG12717. mug.

    Phylogenomic databases

    eggNOGi COG3663.
    HOGENOMi HOG000264684.
    KOi K03649.
    OMAi ETGCGIT.
    OrthoDBi EOG68H872.
    PhylomeDBi P0A9H1.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG12717-MONOMER.
    ECOL316407:JW3040-MONOMER.
    MetaCyc:EG12717-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0A9H1.
    PROi P0A9H1.

    Gene expression databases

    Genevestigatori P0A9H1.

    Family and domain databases

    Gene3Di 3.40.470.10. 1 hit.
    HAMAPi MF_01956. MUG.
    InterProi IPR023502. DNA_glyclase_G/T-mismatch_bac.
    IPR015637. DNA_glycosylase_G/T-mismatch.
    IPR005122. Uracil-DNA_glycosylase-like.
    [Graphical view ]
    PANTHERi PTHR12159. PTHR12159. 1 hit.
    Pfami PF03167. UDG. 1 hit.
    [Graphical view ]
    SMARTi SM00986. UDG. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52141. SSF52141. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    2. "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.
    3. "The nucleotide sequence of the cloned rpoD gene for the RNA polymerase sigma subunit from E coli K12."
      Burton Z.F., Burgess R.R., Lin J., Moore D., Holder S., Gross C.A.
      Nucleic Acids Res. 9:2889-2903(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 118-168.
      Strain: K12.
    4. "Detection of new genes in a bacterial genome using Markov models for three gene classes."
      Borodovsky M., McIninch J., Koonin E.V., Rudd K.E., Medigue C., Danchin A.
      Nucleic Acids Res. 23:3554-3562(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION.
    5. "A new class of uracil-DNA glycosylases related to human thymine-DNA glycosylase."
      Gallinari P., Jiricny J.
      Nature 383:735-738(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "Escherichia coli DNA glycosylase Mug: a growth-regulated enzyme required for mutation avoidance in stationary-phase cells."
      Mokkapati S.K., Fernandez de Henestrosa A.R., Bhagwat A.S.
      Mol. Microbiol. 41:1101-1111(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    7. "Mismatch uracil glycosylase from Escherichia coli: a general mismatch or a specific DNA glycosylase?"
      O'Neill R.J., Vorob'eva O.V., Shahbakhti H., Zmuda E., Bhagwat A.S., Baldwin G.S.
      J. Biol. Chem. 278:20526-20532(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "Crystal structure of a G:T/U mismatch-specific DNA glycosylase: mismatch recognition by complementary-strand interactions."
      Barrett T.E., Savva R., Panayotou G., Brown T., Barlow T., Jiricny J., Pearl L.H.
      Cell 92:117-129(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH DNA.
    9. "Structure of a DNA base-excision product resembling a cisplatin inter-strand adduct."
      Barrett T.E., Savva R., Barlow T., Brown T., Jiricny J., Pearl L.H.
      Nat. Struct. Biol. 5:697-701(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH DNA.
    10. "Crystal structure of a thwarted mismatch glycosylase DNA repair complex."
      Barrett T.E., Schaerer O.D., Savva R., Brown T., Jiricny J., Verdine G.L., Pearl L.H.
      EMBO J. 18:6599-6609(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) IN COMPLEX WITH DNA.

    Entry informationi

    Entry nameiMUG_ECOLI
    AccessioniPrimary (citable) accession number: P0A9H1
    Secondary accession number(s): P43342, Q2M9D7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2005
    Last sequence update: July 19, 2005
    Last modified: October 1, 2014
    This is version 76 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, 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