Reviewed, UniProtKB/Swiss-Prot P06968 (DUT_ECOLI)

Names and origin

Protein names

Recommended name:
    Deoxyuridine 5'-triphosphate nucleotidohydrolase
      Short name=dUTPase
    EC=3.6.1.23
Alternative name(s):
    dUTP pyrophosphatase

Gene names

Name:	dut
Synonyms:	dnaS, sof
Ordered Locus Names:	b3640, JW3615

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	151 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.
Catalytic activity	dUTP + H(2)O = dUMP + diphosphate.
Pathway	Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2.
Subunit structure	Homotrimer.
Sequence similarities	Belongs to the dUTPase family.

Ontologies

Keywords
Biological process	Nucleotide metabolism
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Cellular component	cytosol Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 151

151

Deoxyuridine 5'-triphosphate nucleotidohydrolase

PRO_0000182858

Secondary structure

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151

Helix Strand Turn

Details...

Beta strand

1 – 8

8

Turn

14 – 16

3

Beta strand

30 – 33

4

Beta strand

40 – 42

3

Beta strand

47 – 57

11

Beta strand

63 – 68

6

Helix

71 – 77

7

Beta strand

79 – 81

3

Beta strand

84 – 88

5

Beta strand

94 – 102

9

Beta strand

104 – 106

3

Beta strand

108 – 110

3

Beta strand

115 – 123

9

Beta strand

125 – 133

9

Sequences

	Sequence		Length	Mass (Da)
	P06968-1 [UniParc]. Last modified April 1, 1988. Version 1. Checksum: 98FA3DE0BC70FFB2	FASTA	151	16,155
	10 20 30 40 50 60 MKKIDVKILD PRVGKEFPLP TYATSGSAGL DLRACLNDAV ELAPGDTTLV PTGLAIHIAD 70 80 90 100 110 120 PSLAAMMLPR SGLGHKHGIV LGNLVGLIDS DYQGQLMISV WNRGQDSFTI QPGERIAQMI 130 140 150 FVPVVQAEFN LVEDFDATDR GEGGFGHSGR Q

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the structural gene for dUTPase of Escherichia coli K-12." Lundberg L.G., Thoresson H.-O., Karlstroem O.H., Nyman P.O. EMBO J. 2:967-971(1983) [PubMed: 6139280] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication." Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R. Genomics 16:551-561(1993) [PubMed: 7686882] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"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.
[4]	"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.
[5]	"Crystal structure of a dUTPase." Cedergren-Zeppezauer E.S., Larsson G., Nyman P.O., Dauter Z., Wilson K.S. Nature 355:740-743(1992) [PubMed: 1311056] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[6]	"Crystal structure of the Escherichia coli dUTPase in complex with a substrate analogue (dUDP)." Larsson G., Svensson L.A., Nyman P.O. Nat. Struct. Biol. 3:532-538(1996) [PubMed: 8646539] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
[7]	"The refined structure of dUTPase from Escherichia coli." Dauter Z., Wilson K.S., Larsson G., Nyman P.O., Cedergren-Zeppezauer E.S. Acta Crystallogr. D 54:735-749(1998) [PubMed: 9757088] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[8]	"Atomic resolution structure of Escherichia coli dUTPase determined ab initio." Gonzalez A., Larsson G., Persson R., Cedergren-Zeppezauer E.S. Acta Crystallogr. D 57:767-774(2001) [PubMed: 11375495] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X01714 Genomic DNA. Translation: CAA25859.1.
V01578 Genomic DNA. Translation: CAA24897.1.
L10328 Genomic DNA. Translation: AAA61993.1.
U00096 Genomic DNA. Translation: AAC76664.1.
AP009048 Genomic DNA. Translation: BAE77652.1.

PIR

WPECDU. A30388.

RefSeq

AP_004151.1.
NP_418097.1.

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DUD	X-ray	2.30	A	1-151	[»]
1DUP	X-ray	1.90	A	1-151	[»]
1EU5	X-ray	1.45	A	1-151	[»]
1EUW	X-ray	1.05	A	1-151	[»]
1RN8	X-ray	1.93	A	1-151	[»]
1RNJ	X-ray	1.70	A	1-151	[»]
1SEH	X-ray	1.47	A	1-151	[»]
1SYL	X-ray	1.95	A	1-151	[»]
2HR6	X-ray	1.84	A	1-151	[»]
2HRM	X-ray	1.70	A	1-151	[»]

DisProt

DP00337.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:9483N.

2-D gel databases

SWISS-2DPAGE

P06968.

ECO2DBASE

C017.2. 6TH EDITION.

Genome annotation databases

GeneID

948607.

GenomeReviews

Gene locus b3640 in contig U00096_GR.
Gene locus JW3615 in contig AP009048_GR.

KEGG

ecj:JW3615.
eco:b3640.

Organism-specific databases

EchoBASE

EB0247.

EcoGene

EG10251. dut.

CMR

Search...

Phylogenomic databases

HOGENOM

P06968.

Enzyme and pathway databases

BioCyc

EcoCyc:DUTP-PYROP-MON.
MetaCyc:DUTP-PYROP-MON.

Family and domain databases

HAMAP

MF_00116.
[Tree]

InterPro

IPR008180. DeoxyUTPase.
IPR008181. dUTP_pyrophosphatase_subfam_1.
[Graphical view]

Pfam

PF00692. dUTPase. 1 hit.
[Graphical view]

ProDom

PD004900. dCTP_deaminase. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR00576. dut. 1 hit.

BLOCKS

Search...

ProtoNet

Search...

Other Resources

LinkHub

P06968.

Entry information

Entry name

DUT_ECOLI

Accession

Primary (citable) accession number: P06968
Secondary accession number(s): Q2M7V4

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	April 1, 1988
Last modified:	November 4, 2008
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)