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A2SIY4 (DUT_METPP) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 50. 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:Mpe_A2570
OrganismMethylibium petroleiphilum (strain PM1) [Complete proteome] [HAMAP]
Taxonomic identifier420662 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesMethylibium

Protein attributes

Sequence length149 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 – 149149Deoxyuridine 5'-triphosphate nucleotidohydrolase HAMAP-Rule MF_00116
PRO_1000015482

Regions

Region68 – 703Substrate binding By similarity
Region85 – 873Substrate binding By similarity

Sites

Binding site811Substrate By similarity
Binding site951Substrate; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
A2SIY4 [UniParc].

Last modified March 6, 2007. Version 1.
Checksum: DD5BBA4220C78CDD

FASTA14915,608
        10         20         30         40         50         60 
MTTIDVKVLD PRMADQLPAY ATPGSAGLDL RACLDAPLLL EPGQTQLIPT GLSIHIGDPG 

        70         80         90        100        110        120 
LAAVILPRSG LGHKHGIVLG NLVGLIDSDY QGPLMVSCWN RGLAAFTVQP LERIAQLVIV 

       130        140 
PVVQASFRVV DDFGASERGE GGFGSTGQR 

« Hide

References

[1]"Whole-genome analysis of the methyl tert-butyl ether-degrading beta-proteobacterium Methylibium petroleiphilum PM1."
Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W., Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M., Hristova K.R.
J. Bacteriol. 189:1931-1945(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PM1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000555 Genomic DNA. Translation: ABM95523.1.
RefSeqYP_001021758.1. NC_008825.1.

3D structure databases

ProteinModelPortalA2SIY4.
SMRA2SIY4. Positions 1-136.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING420662.Mpe_A2570.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM95523; ABM95523; Mpe_A2570.
GeneID4785232.
KEGGmpt:Mpe_A2570.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0756.
HOGENOMHOG000028968.
KOK01520.
OMAMVSAWNR.
OrthoDBEOG689HXK.

Enzyme and pathway databases

BioCycMPET420662:GHBE-2601-MONOMER.
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_METPP
AccessionPrimary (citable) accession number: A2SIY4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 6, 2007
Last modified: February 19, 2014
This is version 50 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