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A5J8H0 (A5J8H0_BURMA) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Deoxyuridine 5'-triphosphate nucleotidohydrolase HAMAP MF_00116
Short name=dUTPase HAMAP MF_00116
EC=3.6.1.23 HAMAP MF_00116
Alternative name(s):
dUTP pyrophosphatase HAMAP MF_00116
Gene names
Name:dut HAMAP MF_00116 EMBL EDK53836.1
ORF Names:BMAFMH_0477 EMBL EDK53836.1
OrganismBurkholderia mallei FMH EMBL EDK53836.1
Taxonomic identifier334802 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group

Protein attributes

Sequence length148 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 SAAS SAAS008181

Catalytic activity

dUTP + H2O = dUMP + diphosphate. HAMAP MF_00116 SAAS SAAS008181

Cofactor

Magnesium By similarity. HAMAP MF_00116 SAAS SAAS008181

Pathway

Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2. HAMAP MF_00116

Sequence similarities

Belongs to the dUTPase family. HAMAP MF_00116

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region67 – 693Substrate binding By similarity HAMAP MF_00116
Region84 – 863Substrate binding By similarity HAMAP MF_00116

Sites

Binding site801Substrate By similarity HAMAP MF_00116
Binding site941Substrate; via amide nitrogen and carbonyl oxygen By similarity HAMAP MF_00116

Sequences

Sequence LengthMass (Da)Tools
A5J8H0 [UniParc].

Last modified June 26, 2007. Version 1.
Checksum: 7701824C804B54A0

FASTA14815,802
        10         20         30         40         50         60 
MKLDLKILDA RMRDYLPKYA TTGSAGLDLR ACLDAPVTLK PGDTALVPTG LAIHLADPGY 

        70         80         90        100        110        120 
AALILPRSGL GHKHGIVLGN LVGLIDSDYQ GELMISTWNR GQTEFALNPF ERLAQLVIVP 

       130        140 
VVQARFNLVD DFAQSERGAG GFGSTGRG

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References

[1]DeShazer D., Woods D.E., Nierman W.C.
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: FMH EMBL EDK53836.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		DS264097 Genomic DNA. Translation: EDK53836.1.

3D structure databases

ProteinModelPortalA5J8H0.
SMRA5J8H0. Positions 2-132.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

PATRIC26917306. VBIBurMal45758_3731.

Phylogenomic databases

OMALDLRACI.

Family and domain databases

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

Entry information

Entry nameA5J8H0_BURMA
AccessionPrimary (citable) accession number: A5J8H0
Entry history
Integrated into UniProtKB/TrEMBL: June 26, 2007
Last sequence update: June 26, 2007
Last modified: December 14, 2011
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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