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B7GQI9 (DUT_BIFLS) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 36. 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:Blon_0970, BLIJ_0987
OrganismBifidobacterium longum subsp. infantis (strain ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12) [Complete proteome] [HAMAP]
Taxonomic identifier391904 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeBifidobacterialesBifidobacteriaceaeBifidobacterium

Protein attributes

Sequence length158 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 – 158158Deoxyuridine 5'-triphosphate nucleotidohydrolase HAMAP-Rule MF_00116
PRO_1000119226

Regions

Region75 – 773Substrate binding By similarity
Region92 – 943Substrate binding By similarity

Sites

Binding site881Substrate By similarity
Binding site1021Substrate; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
B7GQI9 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: 7B68EB219B10ECE1

FASTA15816,751
        10         20         30         40         50         60 
MAFDETYNEP ESTEVLVKSL DPEHPALLRY AHAGDAGADL ITTVDVTLKP FERALVPTGV 

        70         80         90        100        110        120 
AIALPAGYVA LVHPRSGLAA KQGVTVLNAP GTVDAGYRGE IKVPLINLDP KHTAVFHPGD 

       130        140        150 
RIAQLVIQRY VEARFIPAET LPGSDRAERG FGSTGVAS 

« Hide

References

[1]"The genome sequence of Bifidobacterium longum subsp. infantis reveals adaptations for milk utilization within the infant microbiome."
Sela D.A., Chapman J., Adeuya A., Kim J.H., Chen F., Whitehead T.R., Lapidus A., Rokhsar D.S., Lebrilla C.B., German J.B., Price N.P., Richardson P.M., Mills D.A.
Proc. Natl. Acad. Sci. U.S.A. 105:18964-18969(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12.
[2]"Bifidobacteria can protect from enteropathogenic infection through production of acetate."
Fukuda S., Toh H., Hase K., Oshima K., Nakanishi Y., Yoshimura K., Tobe T., Clarke J.M., Topping D.L., Suzuki T., Taylor T.D., Itoh K., Kikuchi J., Morita H., Hattori M., Ohno H.
Nature 469:543-547(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001095 Genomic DNA. Translation: ACJ52069.1.
AP010889 Genomic DNA. Translation: BAJ68577.1.
RefSeqYP_002322447.1. NC_011593.1.
YP_005584747.1. NC_017219.1.

3D structure databases

ProteinModelPortalB7GQI9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING391904.Blon_0970.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACJ52069; ACJ52069; Blon_0970.
BAJ68577; BAJ68577; BLIJ_0987.
GeneID12166562.
7054288.
KEGGbln:Blon_0970.
blon:BLIJ_0987.
PATRIC21122904. VBIBifLon71229_0974.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0756.
HOGENOMHOG000028966.
KOK01520.
OMAMDLRANI.
OrthoDBEOG689HXK.
ProtClustDBCLSK573078.

Enzyme and pathway databases

BioCycBLON391904:GCDR-997-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_BIFLS
AccessionPrimary (citable) accession number: B7GQI9
Secondary accession number(s): E8MRF2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: February 10, 2009
Last modified: February 19, 2014
This is version 36 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