Skip Header

Contribute Send feedback
Read comments (?) or add your own

A3PYI9 (DUT_MYCSJ) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 36. 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 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

Subunit structure

Homotrimer By similarity. HAMAP 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. 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 – 154154Deoxyuridine 5'-triphosphate nucleotidohydrolase HAMAP 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...

Protein-protein interaction databases

STRINGA3PYI9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000051358; EBMYCP00000049639; EBMYCG00000051353.
GeneID4877900.
GenomeReviewsGene locus Mjls_2180 in contig CP000580_GR.
KEGGmjl:Mjls_2180.
PATRIC18090490. VBIMycSp51234_2185.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0756.
GeneTreeEBGT00050000017683.
HOGENOMHBG436079.
OMAKIAQMVI.
PhylomeDBA3PYI9.
ProtClustDBPRK00601.

Enzyme and pathway databases

BioCycMSP164757:MJLS_2180-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_MYCSJ
AccessionPrimary (citable) accession number: A3PYI9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: April 3, 2007
Last modified: January 25, 2012
This is version 36 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