G/U mismatch-specific DNA glycosylase - Escherichia coli (strain K12)

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P0A9H1 (MUG_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 68. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:	mug
Synonyms:	ygjF
Ordered Locus Names:	b3068, JW3040

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	168 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	DNA damage DNA excision DNA repair
Cellular component	Cytoplasm
Ligand	DNA-binding
Molecular function	Glycosidase Hydrolase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	base-excision repair, AP site formation Inferred from direct assay Ref.5. Source: EcoCyc
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	DNA 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 168

168

G/U mismatch-specific DNA glycosylase HAMAP-Rule MF_01956

PRO_0000185774

Secondary structure

168

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0A9H1 [UniParc].

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

168

18,673

        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' referencesShow '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 277:1453-1474(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.

PIR

B65095.

RefSeq

NP_417540.1. NC_000913.2.
YP_491260.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P0A9H1.

SMR

P0A9H1. Positions 1-165.

ModBase

Search...

Protein-protein interaction databases

IntAct

P0A9H1. 21 interactions.

STRING

511145.b3068.

Proteomic databases

PaxDb

P0A9H1.

PRIDE

P0A9H1.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76104; AAC76104; b3068.
BAE77119; BAE77119; BAE77119.

GeneID

12933393.
947560.

KEGG

ecj:Y75_p2994.
eco:b3068.

PATRIC

32121552. VBIEscCol129921_3163.

Organism-specific databases

EchoBASE

EB2576.

EcoGene

EG12717. mug.

Phylogenomic databases

eggNOG

COG3663.

HOGENOM

HOG000264684.

K03649.

OMA

FARPGNR.

ProtClustDB

PRK10201.

Enzyme and pathway databases

BioCyc

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

Gene expression databases

Genevestigator

P0A9H1.

Family and domain databases

Gene3D

3.40.470.10. 1 hit.

HAMAP

MF_01956. MUG.

InterPro

IPR023502. DNA_glyclase_G/T-mismatch_bac.
IPR015637. DNA_glycosylase_G/T-mismatch.
IPR005122. Uracil-DNA_glycosylase-like.
[Graphical view]

PANTHER

PTHR12159. PTHR12159. 1 hit.

Pfam

PF03167. UDG. 1 hit.
[Graphical view]

SMART

SM00986. UDG. 1 hit.
[Graphical view]

SUPFAM

SSF52141. UDNA_glycsylseSF. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P0A9H1.

Entry information

Entry name

MUG_ECOLI

Accession

Primary (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:	May 1, 2013
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents