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Q1LTS1 (DUT_BAUCH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:BCI_0182
OrganismBaumannia cicadellinicola subsp. Homalodisca coagulata [Complete proteome] [HAMAP]
Taxonomic identifier374463 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaCandidatus Baumannia

Protein attributes

Sequence length150 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 – 150150Deoxyuridine 5'-triphosphate nucleotidohydrolase HAMAP MF_00116
PRO_1000057765

Regions

Region70 – 723Substrate binding By similarity
Region86 – 883Substrate binding By similarity

Sites

Binding site821Substrate By similarity
Binding site961Substrate; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1LTS1 [UniParc].

Last modified May 30, 2006. Version 1.
Checksum: 5B21FE87D916778F

FASTA15016,331
        10         20         30         40         50         60 
MKKIDIKILD SRIGDCFKLP KYATPGSAGI DLRACIDNTI SLEPGETNLI STGLAVHIAD 

        70         80         90        100        110        120 
TGLAGIIIPR SGLGHHGIVL GNLVGLIDSD YQGSIMVSLW NRGKEIFTIQ PNERIAQIVF 

       130        140        150 
VQIVQVYFNI VDNFQKSKRG ERGFGHSGRV 

« Hide

References

[1]"Metabolic complementarity and genomics of the dual bacterial symbiosis of sharpshooters."
Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A.
PLoS Biol. 4:1079-1092(2006) [PubMed: 16729848] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000238 Genomic DNA. Translation: ABF14111.1.
RefSeqYP_588643.1. NC_007984.1.

3D structure databases

ProteinModelPortalQ1LTS1.
SMRQ1LTS1. Positions 1-138.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ1LTS1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4056526.
GenomeReviewsGene locus BCI_0182 in contig CP000238_GR.
KEGGbci:BCI_0182.
PATRIC21073863. VBIBauCic75062_0176.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0756.
HOGENOMHBG436079.
OMALDLRACI.
PhylomeDBQ1LTS1.

Enzyme and pathway databases

BioCycBCIC186490:BCI_0182-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_BAUCH
AccessionPrimary (citable) accession number: Q1LTS1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: May 30, 2006
Last modified: January 25, 2012
This is version 41 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