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Q8FPH9 (DUT_COREF) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 48. 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:CE1799
OrganismCorynebacterium efficiens [Complete proteome] [HAMAP]
Taxonomic identifier152794 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length181 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

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 – 181181Deoxyuridine 5'-triphosphate nucleotidohydrolase HAMAP MF_00116
PRO_0000182854

Regions

Region96 – 983Substrate binding By similarity
Region113 – 1153Substrate binding By similarity

Sites

Binding site1091Substrate By similarity
Binding site1231Substrate; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8FPH9 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 184F50AE22C6E56B

FASTA18119,462
        10         20         30         40         50         60 
MILSHRWQCT IVPVDSGRQR RAYPEGVTEN LNTIDSIRLL RLDPGLPMPR RAHRGDAGVD 

        70         80         90        100        110        120 
LHSTTDVVIA PGHRELVGTG VAIALPLGTV GLIHPRSGLA AREGLSIVNA PGTVDADYRG 

       130        140        150        160        170        180 
EIKVCLINLD PSTPITITRG DRIAQLIIQR VELVDFVEVD ELDETTRGDQ GHGSTGRGST 


A 

« Hide

References

[1]"Comparative complete genome sequence analysis of the amino acid replacements responsible for the thermostability of Corynebacterium efficiens."
Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.
Genome Res. 13:1572-1579(2003) [PubMed: 12840036] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000035 Genomic DNA. Translation: BAC18609.1.
RefSeqNP_738409.1. NC_004369.1.

3D structure databases

ProteinModelPortalQ8FPH9.
SMRQ8FPH9. Positions 36-171.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1034420.
GenomeReviewsGene locus CE1799 in contig BA000035_GR.
KEGGcef:CE1799.
NMPDRfig|196164.1.peg.1799.
PATRIC21489751. VBICorEff9312_1789.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG436079.
OMAKIAQMVI.
PhylomeDBQ8FPH9.
ProtClustDBPRK00601.

Enzyme and pathway databases

BioCycCEFF196164:CE1799-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_COREF
AccessionPrimary (citable) accession number: Q8FPH9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: March 1, 2003
Last modified: January 25, 2012
This is version 48 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