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Reviewed, UniProtKB/Swiss-Prot P06968 (DUT_ECOLI)

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

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
OrganismEscherichia coli (strain K12) [Complete proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length151 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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. 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.

Ontologies

Keywords
   Biological processNucleotide metabolism
   Molecular functionHydrolase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processdUTP metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytosol

Inferred from direct assay. Source: UniProtKB

   Molecular functiondUTP diphosphatase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 151151Deoxyuridine 5'-triphosphate nucleotidohydrolase HAMAP MF_00116
PRO_0000182858

Secondary structure

............................ 151
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P06968-1 [UniParc].

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

FASTA15116,155
        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

References

« Hide '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

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.
PIRWPECDU. A30388.
RefSeqAP_004151.1.
NP_418097.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1DUDX-ray2.30A1-151[»]
1DUPX-ray1.90A1-151[»]
1EU5X-ray1.45A1-151[»]
1EUWX-ray1.05A1-151[»]
1RN8X-ray1.93A1-151[»]
1RNJX-ray1.70A1-151[»]
1SEHX-ray1.47A1-151[»]
1SYLX-ray1.95A1-151[»]
2HR6X-ray1.84A1-151[»]
2HRMX-ray1.70A1-151[»]
DisProtDP00337.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:9483N.

2-D gel databases

SWISS-2DPAGEP06968.
ECO2DBASEC017.2. 6TH EDITION.

Genome annotation databases

GeneID948607.
GenomeReviewsGene locus JW3615 in contig AP009048_GR.
Gene locus b3640 in contig U00096_GR.
KEGGecj:JW3615.
eco:b3640.

Organism-specific databases

EchoBASEEB0247.
EcoGeneEG10251. dut.
CMRSearch...

Phylogenomic databases

HOGENOMP06968.
OMAP06968. LDLRACI.

Enzyme and pathway databases

BioCycEcoCyc:DUTP-PYROP-MON.
MetaCyc:DUTP-PYROP-MON.

Family and domain databases

HAMAPMF_00116.
[Tree]
InterProIPR008180. DeoxyUTPase.
IPR008181. dUTP_pyrophosphatase_subfam_1.
[Graphical view]
PfamPF00692. dUTPase. 1 hit.
[Graphical view]
ProDomPD004900. dCTP_deaminase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR00576. dut. 1 hit.
ProtoNetSearch...

Entry information

Entry nameDUT_ECOLI
AccessionPrimary (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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Escherichia coli

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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