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P0A9H1 (MUG_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 74. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:mug
Synonyms:ygjF
Ordered Locus Names:b3068, JW3040
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length168 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5 Ref.7

Catalytic activity

Specifically hydrolyzes mismatched double-stranded DNA and polynucleotides, releasing free uracil. HAMAP-Rule MF_01956

Enzyme regulation

Subject to strong product inhibition. N-glycosyl hydrolysis proceeds 100-fold faster than product release. HAMAP-Rule MF_01956

Subunit structure

Binds DNA as a monomer.

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_01956.

Induction

Induced in stationary phase. Ref.6

Sequence similarities

Belongs to the TDG/mug DNA glycosylase family.

Ontologies

Keywords
   Biological processDNA damage
DNA excision
DNA repair
   Cellular componentCytoplasm
   LigandDNA-binding
   Molecular functionGlycosidase
Hydrolase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbase-excision repair, AP site formation

Inferred from direct assay Ref.5. Source: EcoCyc

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

pyrimidine-specific mismatch base pair DNA N-glycosylase activity

Inferred from direct assay Ref.5. Source: EcoCyc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 168168G/U mismatch-specific DNA glycosylase HAMAP-Rule MF_01956
PRO_0000185774

Secondary structure

............................ 168
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A9H1 [UniParc].

Last modified July 19, 2005. Version 1.
Checksum: F1CD9B2E2030D6A7

FASTA16818,673
        10         20         30         40         50         60 
MVEDILAPGL RVVFCGINPG LSSAGTGFPF AHPANRFWKV IYQAGFTDRQ LKPQEAQHLL 

        70         80         90        100        110        120 
DYRCGVTKLV DRPTVQANEV SKQELHAGGR KLIEKIEDYQ PQALAILGKQ AYEQGFSQRG 

       130        140        150        160 
AQWGKQTLTI GSTQIWVLPN PSGLSRVSLE KLVEAYRELD QALVVRGR 

« Hide

References

« Hide 'large scale' references
[1]"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.
[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U28379 Genomic DNA. Translation: AAA89148.1.
U00096 Genomic DNA. Translation: AAC76104.1.
AP009048 Genomic DNA. Translation: BAE77119.1.
J01687 Genomic DNA. No translation available.
PIRB65095.
RefSeqNP_417540.1. NC_000913.3.
YP_491260.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MTLX-ray2.80A/B1-168[»]
1MUGX-ray1.80A1-168[»]
1MWIX-ray2.35A1-168[»]
1MWJX-ray2.85A1-168[»]
ProteinModelPortalP0A9H1.
SMRP0A9H1. Positions 1-165.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP0A9H1. 21 interactions.
STRING511145.b3068.

Proteomic databases

PaxDbP0A9H1.
PRIDEP0A9H1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76104; AAC76104; b3068.
BAE77119; BAE77119; BAE77119.
GeneID12933393.
947560.
KEGGecj:Y75_p2994.
eco:b3068.
PATRIC32121552. VBIEscCol129921_3163.

Organism-specific databases

EchoBASEEB2576.
EcoGeneEG12717. mug.

Phylogenomic databases

eggNOGCOG3663.
HOGENOMHOG000264684.
KOK03649.
OMAFARPGNR.
OrthoDBEOG68H872.
PhylomeDBP0A9H1.
ProtClustDBPRK10201.

Enzyme and pathway databases

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

Gene expression databases

GenevestigatorP0A9H1.

Family and domain databases

Gene3D3.40.470.10. 1 hit.
HAMAPMF_01956. MUG.
InterProIPR023502. DNA_glyclase_G/T-mismatch_bac.
IPR015637. DNA_glycosylase_G/T-mismatch.
IPR005122. Uracil-DNA_glycosylase-like.
[Graphical view]
PANTHERPTHR12159. PTHR12159. 1 hit.
PfamPF03167. UDG. 1 hit.
[Graphical view]
SMARTSM00986. UDG. 1 hit.
[Graphical view]
SUPFAMSSF52141. SSF52141. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP0A9H1.
PROP0A9H1.

Entry information

Entry nameMUG_ECOLI
AccessionPrimary (citable) accession number: P0A9H1
Secondary accession number(s): P43342, Q2M9D7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: April 16, 2014
This is version 74 of the entry and version 1 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