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Q58502 (DUT_METJA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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):
MjDUT
dUTP pyrophosphatase
Gene names
Name:dut
Ordered Locus Names:MJ1102
OrganismMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) [Reference proteome] [HAMAP]
Taxonomic identifier243232 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus

Protein attributes

Sequence length156 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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. HAMAP-Rule MF_00635

Catalytic activity

dUTP + H2O = dUMP + diphosphate. HAMAP-Rule MF_00635

Pathway

Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2. HAMAP-Rule MF_00635

Subunit structure

Homotrimer Probable.

Sequence similarities

Belongs to the dCTP deaminase family. Archaeal dUTPase subfamily.

Sequence caution

The sequence AAB99105.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processNucleotide metabolism
   Molecular functionHydrolase
   Technical termComplete proteome
Direct protein sequencing
Reference 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

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 156155Deoxyuridine 5'-triphosphate nucleotidohydrolase HAMAP-Rule MF_00635
PRO_0000153638

Sequences

Sequence LengthMass (Da)Tools
Q58502 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: AF6E28A4CF91FF3D

FASTA15618,070
        10         20         30         40         50         60 
MIIGANTSKN FFDNLEEEQI QQCGIDLRVW KIFKIEGEGV IDFSNEKRKL PNYIEIFNSE 

        70         80         90        100        110        120 
KDEHIKLDRG VYIVKVADYI KIPENVAGFA YPRSSLLRMG ATLYSAVHDP GYEGRPEYLM 

       130        140        150 
QVFNPITIYK YARIAQIVFV ECRDVKGVYE GIYKGR 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii."
Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R., Kirkness E.F., Weinstock K.G. expand/collapse author list , Merrick J.M., Glodek A., Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.
Science 273:1058-1073(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.
[2]"A bifunctional dCTP deaminase-dUTP nucleotidohydrolase from the hyperthermophilic archaeon Methanocaldococcus jannaschii."
Bjoernberg O., Neuhard J., Nyman P.O.
J. Biol. Chem. 278:20667-20672(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-10, CHARACTERIZATION.
[3]"The Methanococcus jannaschii dCTP deaminase is a bifunctional deaminase and diphosphatase."
Li H., Xu H., Graham D.E., White R.H.
J. Biol. Chem. 278:11100-11106(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L77117 Genomic DNA. Translation: AAB99105.1. Different initiation.
PIRE64437.
RefSeqNP_248095.1. NC_000909.1.

3D structure databases

ProteinModelPortalQ58502.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243232.MJ1102.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAB99105; AAB99105; MJ_1102.
GeneID1451999.
KEGGmja:MJ_1102.

Phylogenomic databases

eggNOGCOG0717.
KOK01520.
OMAQCGIDLR.
PhylomeDBQ58502.

Enzyme and pathway databases

SABIO-RKQ58502.
UniPathwayUPA00610; UER00666.

Family and domain databases

Gene3D2.70.40.10. 1 hit.
HAMAPMF_00635. dUTPase_arch.
InterProIPR029054. dUTPase-like.
IPR008180. dUTPase/dCTP_deaminase.
IPR023537. dUTPase_archaeal.
[Graphical view]
PfamPF00692. dUTPase. 1 hit.
[Graphical view]
SUPFAMSSF51283. SSF51283. 1 hit.
ProtoNetSearch...

Entry information

Entry nameDUT_METJA
AccessionPrimary (citable) accession number: Q58502
Entry history
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 84 of the entry and version 4 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

Methanococcus jannaschii

Methanococcus jannaschii: entries and gene names