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A3PYI9 (DUT_MYCSJ) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 52. 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:Mjls_2180
OrganismMycobacterium sp. (strain JLS) [Complete proteome] [HAMAP]
Taxonomic identifier164757 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length154 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

Subunit structure

Homotrimer By similarity. HAMAP-Rule MF_00116

Miscellaneous

Each trimer binds three substrate molecules. The ligands are bound between subunits, and for each substrate molecule, residues from adjacent subunits contribute to the binding interactions By similarity.

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 – 154154Deoxyuridine 5'-triphosphate nucleotidohydrolase HAMAP-Rule MF_00116
PRO_1000015486

Regions

Region64 – 663Substrate binding By similarity
Region81 – 833Substrate binding By similarity

Sites

Binding site771Substrate By similarity
Binding site911Substrate; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
A3PYI9 [UniParc].

Last modified April 3, 2007. Version 1.
Checksum: 360D055C90FA8329

FASTA15416,089
        10         20         30         40         50         60 
MSTSLAVLRL DRELPMPARA HDGDAGVDLF SARDVELAPG QRELVPTGIA VAIPHGMVGL 

        70         80         90        100        110        120 
VHPRSGLAAR VGLSIVNSPG TIDAGYRGEI KVSLINLDPH APIVIRRGDR IAQLLVQRVE 

       130        140        150 
LPELVEVTSF DEAGLAETTR GEGGHGSSGG HASL 

« Hide

References

[1]"Complete sequence of Mycobacterium sp. JLS."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Mikhailova N., Miller C.D., Anderson A.J., Sims R.C., Richardson P.
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JLS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000580 Genomic DNA. Translation: ABN97966.1.
RefSeqYP_001070457.1. NC_009077.1.

3D structure databases

ProteinModelPortalA3PYI9.
SMRA3PYI9. Positions 1-144.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING164757.Mjls_2180.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABN97966; ABN97966; Mjls_2180.
GeneID4877900.
KEGGmjl:Mjls_2180.
PATRIC18090490. VBIMycSp51234_2185.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0756.
HOGENOMHOG000028966.
KOK01520.
OMAPKNTEAQ.
OrthoDBEOG689HXK.

Enzyme and pathway databases

BioCycMSP164757:GHV3-2191-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_MYCSJ
AccessionPrimary (citable) accession number: A3PYI9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: April 3, 2007
Last modified: June 11, 2014
This is version 52 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