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Q5QZB6 (DUT_IDILO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 59. 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:IL0238
OrganismIdiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR) [Complete proteome] [HAMAP]
Taxonomic identifier283942 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesIdiomarinaceaeIdiomarina

Protein attributes

Sequence length151 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 – 151151Deoxyuridine 5'-triphosphate nucleotidohydrolase HAMAP-Rule MF_00116
PRO_0000182871

Regions

Region70 – 723Substrate binding By similarity
Region87 – 893Substrate binding By similarity

Sites

Binding site831Substrate By similarity
Binding site971Substrate; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5QZB6 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: FCF70404FA5C17EE

FASTA15116,289
        10         20         30         40         50         60 
MTQVEVKILD DRIGQSIPLP EYATQGSAGM DLRACLDQPL TIEPGQTQLI GTGIAMYIGD 

        70         80         90        100        110        120 
PNYAATILPR SGLGHKHGLV LGNLVGLIDS DYQGELKVSC WNRSNQAYTI EPGDRIAQLV 

       130        140        150 
ILPVVQAQMS IVEEFHETDR GEGGFGHSGR S 

« Hide

References

[1]"Genome sequence of the deep-sea gamma-proteobacterium Idiomarina loihiensis reveals amino acid fermentation as a source of carbon and energy."
Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y., Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S., Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S., Denery J. expand/collapse author list , Aizawa S., Shibata S., Malahoff A., Alam M.
Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-735 / DSM 15497 / L2-TR.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017340 Genomic DNA. Translation: AAV81081.1.
RefSeqYP_154630.1. NC_006512.1.

3D structure databases

ProteinModelPortalQ5QZB6.
SMRQ5QZB6. Positions 1-138.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING283942.IL0238.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV81081; AAV81081; IL0238.
GeneID3172949.
KEGGilo:IL0238.
PATRIC22138483. VBIIdiLoi21852_0238.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0756.
HOGENOMHOG000028968.
KOK01520.
OMAINHDPRT.
OrthoDBEOG689HXK.
ProtClustDBPRK00601.

Enzyme and pathway databases

BioCycILOI283942:GI0U-239-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_IDILO
AccessionPrimary (citable) accession number: Q5QZB6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: January 4, 2005
Last modified: February 19, 2014
This is version 59 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