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Protein

G/U mismatch-specific DNA glycosylase

Gene

mug

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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

GO - Biological processi

  • base-excision repair, AP site formation Source: EcoCyc
Complete GO annotation...

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.
BRENDAi3.2.2.28. 2026.

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 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12717. mug.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

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

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 – 188Combined sources
Helixi21 – 266Combined sources
Helixi37 – 437Combined sources
Beta strandi46 – 494Combined sources
Helixi53 – 6210Combined sources
Beta strandi64 – 696Combined sources
Beta strandi74 – 763Combined sources
Helixi77 – 793Combined sources
Helixi82 – 9918Combined sources
Beta strandi102 – 1076Combined sources
Helixi109 – 1168Combined sources
Beta strandi123 – 1308Combined sources
Beta strandi133 – 1386Combined sources
Helixi149 – 16214Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiP0A9H1.
KOiK03649.
OMAiRPGNRFW.
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

        10         20         30         40         50
MVEDILAPGL RVVFCGINPG LSSAGTGFPF AHPANRFWKV IYQAGFTDRQ
60 70 80 90 100
LKPQEAQHLL DYRCGVTKLV DRPTVQANEV SKQELHAGGR KLIEKIEDYQ
110 120 130 140 150
PQALAILGKQ AYEQGFSQRG AQWGKQTLTI GSTQIWVLPN PSGLSRVSLE
160
KLVEAYRELD QALVVRGR
Length:168
Mass (Da):18,673
Last modified:July 19, 2005 - v1
Checksum:iF1CD9B2E2030D6A7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
WP_000228937.1. NZ_CP010445.1.

Genome annotation databases

EnsemblBacteriaiAAC76104; AAC76104; b3068.
BAE77119; BAE77119; BAE77119.
GeneIDi947560.
KEGGieco:b3068.
PATRICi32121552. VBIEscCol129921_3163.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
WP_000228937.1. NZ_CP010445.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

IntActiP0A9H1. 21 interactions.
STRINGi511145.b3068.

Proteomic databases

PaxDbiP0A9H1.
PRIDEiP0A9H1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76104; AAC76104; b3068.
BAE77119; BAE77119; BAE77119.
GeneIDi947560.
KEGGieco:b3068.
PATRICi32121552. VBIEscCol129921_3163.

Organism-specific databases

EchoBASEiEB2576.
EcoGeneiEG12717. mug.

Phylogenomic databases

eggNOGiCOG3663.
HOGENOMiHOG000264684.
InParanoidiP0A9H1.
KOiK03649.
OMAiRPGNRFW.
OrthoDBiEOG68H872.
PhylomeDBiP0A9H1.

Enzyme and pathway databases

BioCyciEcoCyc:EG12717-MONOMER.
ECOL316407:JW3040-MONOMER.
MetaCyc:EG12717-MONOMER.
BRENDAi3.2.2.28. 2026.

Miscellaneous databases

EvolutionaryTraceiP0A9H1.
PROiP0A9H1.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: July 22, 2015
This is version 83 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.