P12295 (UNG_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Uracil-DNA glycosylase
Short name=UDG
EC=3.2.2.27

Gene names

Name:	ung
Ordered Locus Names:	b2580, JW2564

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	229 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. HAMAP MF_00148
Catalytic activity	Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil. HAMAP MF_00148
Subunit structure	Monomer.
Subcellular location	Cytoplasm HAMAP MF_00148.
Sequence similarities	Belongs to the uracil-DNA glycosylase family.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Cellular component	Cytoplasm
Molecular function	Glycosidase Hydrolase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	base-excision repair Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein binding Inferred from physical interaction. Source: IntAct uracil DNA N-glycosylase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ndk	P0A763	3	EBI-559403,EBI-370139
UGI	P14739	4	EBI-559403,EBI-1025973	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.1

Chain

2 – 229

228

Uracil-DNA glycosylase HAMAP MF_00148

PRO_0000176091

Sites

Active site

64

1

Proton acceptor

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

229

Helix Strand Turn

Details...

Helix

7 – 11

5

Helix

14 – 16

3

Helix

18 – 32

15

Beta strand

37 – 39

3

Helix

41 – 43

3

Helix

46 – 50

5

Helix

53 – 55

3

Beta strand

58 – 62

5

Turn

69 – 71

3

Beta strand

74 – 77

4

Helix

87 – 97

11

Helix

112 – 115

4

Turn

116 – 118

3

Beta strand

119 – 125

7

Turn

133 – 138

6

Helix

141 – 155

15

Beta strand

160 – 165

6

Helix

166 – 171

6

Turn

177 – 179

3

Beta strand

180 – 185

6

Turn

190 – 192

3

Helix

193 – 195

3

Turn

196 – 199

4

Helix

202 – 212

11

Sequences

	Sequence		Length	Mass (Da)
	P12295 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: CD44F1E214FE74ED	FASTA	229	25,693
	10 20 30 40 50 60 MANELTWHDV LAEEKQQPYF LNTLQTVASE RQSGVTIYPP QKDVFNAFRF TELGDVKVVI 70 80 90 100 110 120 LGQDPYHGPG QAHGLAFSVR PGIAIPPSLL NMYKELENTI PGFTRPNHGY LESWARQGVL 130 140 150 160 170 180 LLNTVLTVRA GQAHSHASLG WETFTDKVIS LINQHREGVV FLLWGSHAQK KGAIIDKQRH 190 200 210 220 HVLKAPHPSP LSAHRGFFGC NHFVLANQWL EQRGETPIDW MPVLPAESE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 2836397] [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: 9205837] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"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: 9278503] [Abstract] 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: 16738553] [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: 9261156] [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: 9776748] [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: 10080896] [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: 10090282] [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: 11027138] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

PIR

DGECU. A28175.

RefSeq

NP_417075.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

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	2-228	[»]
1LQJ	X-ray	3.35	A/B/C/D	2-228	[»]
1LQM	X-ray	3.20	A/C/E/G	2-228	[»]
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	[»]
4EUG	X-ray	1.40	A	1-229	[»]
5EUG	X-ray	1.60	A	1-229	[»]

ProteinModelPortal

P12295.

SMR

P12295. Positions 5-229.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-11092N.

IntAct

P12295. 8 interactions.

MINT

MINT-194643.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000003215; EBESCP00000003215; EBESCG00000002640.
EBESCT00000017800; EBESCP00000017091; EBESCG00000016856.

GeneID

947067.

GenomeReviews

Gene locus JW2564 in contig AP009048_GR.
Gene locus b2580 in contig U00096_GR.

KEGG

ecj:JW2564.
eco:b2580.

PATRIC

32120561. VBIEscCol129921_2683.

Organism-specific databases

EchoBASE

EB1051.

EcoGene

EG11058. ung.

Phylogenomic databases

eggNOG

COG0692.

GeneTree

EBGT00050000009819.

HOGENOM

HBG605450.

OMA

GAHAQKK.

PhylomeDB

P12295.

ProtClustDB

PRK05254.

Enzyme and pathway databases

BioCyc

EcoCyc:EG11058-MONOMER.
MetaCyc:EG11058-MONOMER.

Gene expression databases

Genevestigator

P12295.

Family and domain databases

HAMAP

MF_00148. UDG.
[Tree]

InterPro

IPR002043. UDNA_glycsylse.
IPR018085. Ura-DNA_Glyclase_AS.
IPR005122. Uracil-DNA_glycosylase-like.
[Graphical view]

Gene3D

G3DSA:3.40.470.10. Uracil-DNA_glycosylase-like. 1 hit.

KO

K03648.

PANTHER

PTHR11264. UDNA_glycsylse. 1 hit.

Pfam

PF03167. UDG. 1 hit.
[Graphical view]

SMART

SM00986. UDG. 1 hit.
[Graphical view]

SUPFAM

SSF52141. UDNA_glycsylseSF. 1 hit.

TIGRFAMs

TIGR00628. Ung. 1 hit.

PROSITE

PS00130. U_DNA_GLYCOSYLASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

UNG_ECOLI

Accession

Primary (citable) accession number: P12295

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 117 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program