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Q82KK4 (DUT_STRAW) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 48. 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:SAV_2399
OrganismStreptomyces avermitilis [Complete proteome] [HAMAP]
Taxonomic identifier33903 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length175 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 MF_00116

Catalytic activity

dUTP + H2O = dUMP + diphosphate. HAMAP MF_00116

Cofactor

Magnesium By similarity. HAMAP MF_00116

Pathway

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

Inferred from electronic annotation. Source: InterPro

   Molecular functiondUTP diphosphatase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 175175Deoxyuridine 5'-triphosphate nucleotidohydrolase HAMAP MF_00116
PRO_0000182909

Regions

Region67 – 693Substrate binding By similarity
Region84 – 863Substrate binding By similarity

Sites

Binding site801Substrate By similarity
Binding site941Substrate; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q82KK4 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 792E3551799CB7B0

FASTA17518,558
        10         20         30         40         50         60 
MTRAPLNVLL RRVDPDVPLP AYEHPGDAGA DLRTTESCEL KPGERAVLPT GVSVALPEGY 

        70         80         90        100        110        120 
AAFVHPRSGL AARCGVALVN APGTVDAGYR GEIKVIVVNL DPRESVRFER FDRIAQLVVQ 

       130        140        150        160        170 
QVERVRFQEV AELPDSARAE GGFGSTGGHA AVGADTNGQQ GGNRYASVVS DRKGQ 

« Hide

References

[1]"Genome sequence of an industrial microorganism Streptomyces avermitilis: deducing the ability of producing secondary metabolites."
Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M., Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T., Sakaki Y., Hattori M.
Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001) [PubMed: 11572948] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165.
[2]"Complete genome sequence and comparative analysis of the industrial microorganism Streptomyces avermitilis."
Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T., Sakaki Y., Hattori M., Omura S.
Nat. Biotechnol. 21:526-531(2003) [PubMed: 12692562] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000030 Genomic DNA. Translation: BAC70110.1.
RefSeqNP_823575.1. NC_003155.4.

3D structure databases

ProteinModelPortalQ82KK4.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1210420.
GenomeReviewsGene locus SAV_2399 in contig BA000030_GR.
KEGGsma:SAV_2399.
NMPDRfig|227882.1.peg.2401.
PATRIC23718289. VBIStrAve112782_2562.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG436079.
OMAKIAQMVI.
ProtClustDBPRK00601.

Enzyme and pathway databases

BioCycSAVE227882:SAV2399-MONOMER.

Family and domain databases

HAMAPMF_00116. dUTPase_bact.
[Tree]
InterProIPR008180. dUTP_pyroPase.
IPR008181. dUTP_pyroPase_sf.
[Graphical view]
KOK01520.
PANTHERPTHR11241. PTHR11241. 1 hit.
PfamPF00692. dUTPase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00576. Dut. 1 hit.
ProtoNetSearch...

Entry information

Entry nameDUT_STRAW
AccessionPrimary (citable) accession number: Q82KK4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: June 1, 2003
Last modified: January 25, 2012
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families