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O52597 (DUT_BRADU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 88. 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:bll0758
OrganismBradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110) [Reference proteome] [HAMAP]
Taxonomic identifier224911 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeBradyrhizobium

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
Reference 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_0000182834

Regions

Region72 – 743Substrate binding By similarity
Region89 – 913Substrate binding By similarity

Sites

Binding site851Substrate By similarity
Binding site991Substrate; via amide nitrogen and carbonyl oxygen By similarity

Experimental info

Sequence conflict601A → V in AAB97415. Ref.1
Sequence conflict109 – 12012AFVIK…ERIAQ → VLRDQARRADRAK Ref.1

Sequences

Sequence LengthMass (Da)Tools
O52597 [UniParc].

Last modified February 28, 2003. Version 2.
Checksum: 0270434059D7B3CE

FASTA15215,574
        10         20         30         40         50         60 
MSTKVTVELQ RLPHAEGLPL PAYQTAEAAG LDLMAAVPED APLTLASGRY ALVPTGLAIA 

        70         80         90        100        110        120 
LPPGHEAQVR PRSGLAAKHG VTVLNSPGTI DADYRGEIKV ILINHGAAAF VIKRGERIAQ 

       130        140        150 
MVIAPVVQAA LVPVATLSAT DRGAGGFGST GR 

« Hide

References

« Hide 'large scale' references
[1]"BdfA, a novel sensor protein of Bradyrhizobium japonicum, is required for normal bacteroid differentiation in soybean (Glycine max)."
Mueller P., Unnewehr A.
Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: USDA 110spc4.
[2]"Complete genomic sequence of nitrogen-fixing symbiotic bacterium Bradyrhizobium japonicum USDA110."
Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.
DNA Res. 9:189-197(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF042096 Genomic DNA. Translation: AAB97415.1.
BA000040 Genomic DNA. Translation: BAC46023.1.
RefSeqNP_767398.1. NC_004463.1.

3D structure databases

ProteinModelPortalO52597.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224911.bll0758.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC46023; BAC46023; BAC46023.
GeneID1049768.
KEGGbja:bll0758.
PATRIC21185020. VBIBraJap65052_0782.

Phylogenomic databases

eggNOGCOG0756.
HOGENOMHOG000028966.
KOK01520.
OMAINHDPRT.
OrthoDBEOG689HXK.
ProtClustDBPRK00601.

Enzyme and pathway databases

BioCycBJAP224911:GJEJ-766-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_BRADU
AccessionPrimary (citable) accession number: O52597
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: February 28, 2003
Last modified: February 19, 2014
This is version 88 of the entry and version 2 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