Deoxyuridine 5'-triphosphate nucleotidohydrolase

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Reviewed, UniProtKB/Swiss-Prot P06968 (DUT_ECOLI)

Last modified June 16, 2009. Version 92. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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

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Protein attributes

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

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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. HAMAP MF_00116
Catalytic activity	dUTP + H₂O = dUMP + diphosphate. HAMAP MF_00116
Pathway	Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2. HAMAP MF_00116
Subunit structure	Homotrimer. HAMAP MF_00116
Sequence similarities	Belongs to the dUTPase family.

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Ontologies

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

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 151

151

Deoxyuridine 5'-triphosphate nucleotidohydrolase HAMAP MF_00116

PRO_0000182858

Secondary structure

151

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P06968-1 [UniParc].

Last modified April 1, 1988. Version 1.
Checksum: 98FA3DE0BC70FFB2
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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

« Hide

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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.

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Cross-references

Sequence databases

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

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

KEGG

ecj:JW3615.
eco:b3640.

Organism-specific databases

EchoBASE

EB0247.

EcoGene

EG10251. dut.

CMR

Search...

Phylogenomic databases

HOGENOM

P06968.

OMA

P06968. LDLRACI.

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.

ProtoNet

Search...

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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:	June 16, 2009
This is version 92 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)

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