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P12295

- UNG_ECOLI

UniProt

P12295 - UNG_ECOLI

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Protein

Uracil-DNA glycosylase

Gene

ung

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

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. uracil DNA N-glycosylase activity Source: EcoCyc

GO - Biological processi

  1. base-excision repair Source: UniProtKB-HAMAP
Complete GO annotation...

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-HAMAP
Complete GO annotation...

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 – 115Combined sources
Helixi14 – 163Combined sources
Helixi18 – 3316Combined sources
Beta strandi37 – 393Combined sources
Helixi41 – 433Combined sources
Helixi46 – 505Combined sources
Helixi53 – 553Combined sources
Beta strandi58 – 647Combined sources
Turni69 – 713Combined sources
Beta strandi74 – 774Combined sources
Beta strandi81 – 833Combined sources
Helixi87 – 9913Combined sources
Helixi112 – 1154Combined sources
Turni116 – 1183Combined sources
Beta strandi119 – 1257Combined sources
Turni133 – 1386Combined sources
Helixi141 – 15515Combined sources
Beta strandi160 – 1656Combined sources
Helixi166 – 1716Combined sources
Turni172 – 1743Combined sources
Turni177 – 1793Combined sources
Beta strandi180 – 1856Combined sources
Turni190 – 19910Combined sources
Helixi202 – 21211Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiP12295.
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

        10         20         30         40         50
MANELTWHDV LAEEKQQPYF LNTLQTVASE RQSGVTIYPP QKDVFNAFRF
60 70 80 90 100
TELGDVKVVI LGQDPYHGPG QAHGLAFSVR PGIAIPPSLL NMYKELENTI
110 120 130 140 150
PGFTRPNHGY LESWARQGVL LLNTVLTVRA GQAHSHASLG WETFTDKVIS
160 170 180 190 200
LINQHREGVV FLLWGSHAQK KGAIIDKQRH HVLKAPHPSP LSAHRGFFGC
210 220
NHFVLANQWL EQRGETPIDW MPVLPAESE
Length:229
Mass (Da):25,693
Last modified:January 23, 2007 - v2
Checksum:iCD44F1E214FE74ED
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
InParanoidi P12295.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 142 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