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Q5PC28 (DUT_SALPA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 58. 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:SPA3583
OrganismSalmonella paratyphi A (strain ATCC 9150 / SARB42) [Complete proteome] [HAMAP]
Taxonomic identifier295319 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length151 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 – 151151Deoxyuridine 5'-triphosphate nucleotidohydrolase HAMAP-Rule MF_00116
PRO_0000231427

Regions

Region70 – 723Substrate binding By similarity
Region87 – 893Substrate binding By similarity

Sites

Binding site831Substrate By similarity
Binding site971Substrate; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5PC28 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: FE8F6BE974C53558

FASTA15116,036
        10         20         30         40         50         60 
MKKIDVKILD PRVGQQFPLP TYATSGSAGL DLRACLDDAV ELAPGATTLV PTGLAIHIAD 

        70         80         90        100        110        120 
PSLAAVMLPR SGLGHKHGIV LGNLVGLIDS DYQGQLMVSI WNRGQDSFTI EPGERIAQMV 

       130        140        150 
FVPVVQAEFN LVEAFDATER GEGGFGHSGR K 

« Hide

References

[1]"Comparison of genome degradation in Paratyphi A and Typhi, human-restricted serovars of Salmonella enterica that cause typhoid."
McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S., Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R., Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F. expand/collapse author list , Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W., Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M., Warren W., Florea L., Spieth J., Wilson R.K.
Nat. Genet. 36:1268-1274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 9150 / SARB42.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000026 Genomic DNA. Translation: AAV79384.1.
RefSeqYP_152696.1. NC_006511.1.

3D structure databases

ProteinModelPortalQ5PC28.
SMRQ5PC28. Positions 1-138.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING295319.SPA3583.

Proteomic databases

PRIDEQ5PC28.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV79384; AAV79384; SPA3583.
PATRIC32356851. VBISalEnt134188_3808.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0756.
HOGENOMHOG000028968.
OMASIYIGDP.
OrthoDBEOG689HXK.

Enzyme and pathway databases

BioCycSENT295319:GJBZ-3581-MONOMER.
UniPathwayUPA00610; UER00666.

Family and domain databases

Gene3D2.70.40.10. 1 hit.
HAMAPMF_00116. dUTPase_bact.
InterProIPR029054. dUTPase-like.
IPR008180. dUTPase/dCTP_deaminase.
IPR008181. dUTPase_1.
[Graphical view]
PfamPF00692. dUTPase. 1 hit.
[Graphical view]
SUPFAMSSF51283. SSF51283. 1 hit.
TIGRFAMsTIGR00576. dut. 1 hit.
ProtoNetSearch...

Entry information

Entry nameDUT_SALPA
AccessionPrimary (citable) accession number: Q5PC28
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: January 4, 2005
Last modified: June 11, 2014
This is version 58 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