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Q9X3X5 (DUT_ZYMMO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 87. 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:ZMO1191
OrganismZymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4) [Complete proteome] [HAMAP]
Taxonomic identifier264203 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesSphingomonadaceaeZymomonas

Protein attributes

Sequence length146 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.

Sequence caution

The sequence AAD21551.1 differs from that shown. Reason: Erroneous termination at position 119. Translated as Ser.

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 – 146146Deoxyuridine 5'-triphosphate nucleotidohydrolase HAMAP-Rule MF_00116
PRO_0000182925

Regions

Region66 – 683Substrate binding By similarity
Region83 – 853Substrate binding By similarity

Sites

Binding site791Substrate By similarity
Binding site931Substrate; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9X3X5 [UniParc].

Last modified February 15, 2005. Version 3.
Checksum: D703C965AA4E8BD6

FASTA14615,680
        10         20         30         40         50         60 
MKIKLEIKRL PHGANLPFPS YASEGAAGMD VVSAEDVILQ PMQRYPVKTG FAVAIPNGYE 

        70         80         90        100        110        120 
IQVRARSGLA LKHGIACPNA PGTIDSDYRG EVKILLINLG SEAFEIKRGD RIAQLILASV 

       130        140 
TQAVFCEVTD LDDTQRGHNG FGSTGI 

« Hide

References

« Hide 'large scale' references
[1]Lee H.J., Kang H.S.
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 31821 / ZM4 / CP4.
[2]"The genome sequence of the ethanologenic bacterium Zymomonas mobilis ZM4."
Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H., Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J., Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y. expand/collapse author list , Kang H.L., Lee S.Y., Lee K.J., Kang H.S.
Nat. Biotechnol. 23:63-68(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 31821 / ZM4 / CP4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF088896 Genomic DNA. Translation: AAD21551.1. Sequence problems.
AE008692 Genomic DNA. Translation: AAV89815.1.
RefSeqYP_162926.1. NC_006526.2.

3D structure databases

ProteinModelPortalQ9X3X5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING264203.ZMO1191.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV89815; AAV89815; ZMO1191.
GeneID3189276.
KEGGzmo:ZMO1191.
PATRIC32567674. VBIZymMob102260_1128.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0756.
HOGENOMHOG000028966.
KOK01520.
OMAINHDPRT.
OrthoDBEOG689HXK.
ProtClustDBCLSK2524803.

Enzyme and pathway databases

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_ZYMMO
AccessionPrimary (citable) accession number: Q9X3X5
Secondary accession number(s): Q5NN95
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: February 15, 2005
Last modified: February 19, 2014
This is version 87 of the entry and version 3 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