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Reviewed, UniProtKB/Swiss-Prot Q6E4Q0 (DUT_ANTLO)

Last modified September 22, 2009. Version 21. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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: DUT1
OrganismAntonospora locustae (Microsporidian parasite) (Nosema locustae)
Taxonomic identifier278021 [NCBI]
Taxonomic lineageEukaryotaFungiMicrosporidiaAntonospora

Protein attributes

Sequence length143 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Catalytic activity

dUTP + H2O = dUMP + diphosphate.

Cofactor

Magnesium By similarity.

Pathway

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

Subunit structure

Homotrimer By similarity.

Sequence similarities

Belongs to the dUTPase family.

Ontologies

Keywords
   Biological processNucleotide metabolism
   LigandMagnesium
Metal-binding
   Molecular functionHydrolase
Gene Ontology (GO)
   Biological processdUTP metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functiondUTP diphosphatase activity

Inferred from electronic annotation. Source: EC

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 143143Deoxyuridine 5'-triphosphate nucleotidohydrolase
PRO_0000182927

Regions

Region64 – 663Substrate binding By similarity
Region78 – 814Substrate binding By similarity
Region137 – 1382Substrate binding By similarity

Sites

Binding site1321Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6E4Q0-1 [UniParc].

Last modified August 16, 2004. Version 1.
Checksum: F8E434A8A47CBA8C

FASTA14315,526
        10         20         30         40         50         60 
MSEIITVKRL FSDAKIPVRH SEGAAAYDLY AYEDTVVAPN ERKVIATGVR ITVPLSCQGT 

        70         80         90        100        110        120 
IYSRSGLALK YCIEIFGVNI GPGETKDIVV DIYNHGKMPF NVAKGDRIAQ IVFIKLFGGD 

       130        140 
LHEVSELSDT KRGSCGWGST GIS 

« Hide

References

[1]"Genome compaction and stability in microsporidian intracellular parasites."
Slamovits C.H., Fast N.M., Law J.S., Keeling P.J.
Curr. Biol. 14:891-896(2004) [PubMed: 15186746] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

AY574349 Genomic DNA. Translation: AAT72741.1.

3D structure databases

ModBaseSearch...

Enzyme and pathway databases

BRENDA3.6.1.23. 288911.

Family and domain databases

InterProIPR008180. DeoxyUTP_pyroPase_dom.
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_ANTLO
AccessionPrimary (citable) accession number: Q6E4Q0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: August 16, 2004
Last modified: September 22, 2009
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

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