Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q5WTW6 (DUT_LEGPL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
Ordered Locus Names:lpl2407
OrganismLegionella pneumophila (strain Lens) [Complete proteome] [HAMAP]
Taxonomic identifier297245 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella

Protein attributes

Sequence length152 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity. HAMAP-Rule MF_00116

Catalytic activity

dUTP + H2O = dUMP + diphosphate. HAMAP-Rule MF_00116

Cofactor

Magnesium By similarity. HAMAP-Rule MF_00116

Pathway

Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2. HAMAP-Rule MF_00116

Sequence similarities

Belongs to the dUTPase family.

Ontologies

Keywords
   Biological processNucleotide metabolism
   LigandMagnesium
Metal-binding
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processdUMP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

dUTP metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular_functiondUTP diphosphatase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 152152Deoxyuridine 5'-triphosphate nucleotidohydrolase HAMAP-Rule MF_00116
PRO_0000182875

Regions

Region71 – 733Substrate binding By similarity
Region88 – 903Substrate binding By similarity

Sites

Binding site841Substrate By similarity
Binding site981Substrate; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5WTW6 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: 98E05FB0684AB15F

FASTA15216,337
        10         20         30         40         50         60 
MHQVIQLKIL DSRIGDTISL PAYATDGSAG LDLRVCISEP MQVAPQQTVL LPTGIAIYIA 

        70         80         90        100        110        120 
DPKLAAVILP RSGLGHKNGI VLGNLVGLID SDYQGELKIS CWNRSQEHFT VNPGDRIAQL 

       130        140        150 
VFIPVVQASF EVVNEFTESS RGEGGFGSSG RY 

« Hide

References

[1]"Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity."
Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L., Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J., Glaser P., Buchrieser C.
Nat. Genet. 36:1165-1173(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Lens.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR628337 Genomic DNA. Translation: CAH16647.1.
RefSeqYP_127737.1. NC_006369.1.

3D structure databases

ProteinModelPortalQ5WTW6.
SMRQ5WTW6. Positions 1-136.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING297245.lpl2407.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAH16647; CAH16647; lpl2407.
GeneID3113988.
KEGGlpf:lpl2407.
PATRIC22318663. VBILegPne33733_2641.

Organism-specific databases

LegioListlpl2407.
CMRSearch...

Phylogenomic databases

eggNOGCOG0756.
HOGENOMHOG000028968.
KOK01520.
OMAMVSAWNR.
OrthoDBEOG689HXK.
ProtClustDBPRK00601.

Enzyme and pathway databases

BioCycLPNE297245:GJD4-2611-MONOMER.
UniPathwayUPA00610; UER00666.

Family and domain databases

HAMAPMF_00116. dUTPase_bact.
InterProIPR008180. dUTP_pyroPase.
IPR008181. dUTP_pyroPase_sf.
[Graphical view]
PfamPF00692. dUTPase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00576. dut. 1 hit.
ProtoNetSearch...

Entry information

Entry nameDUT_LEGPL
AccessionPrimary (citable) accession number: Q5WTW6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: November 23, 2004
Last modified: February 19, 2014
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways