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O68992 (DUT_CHLTE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 91. 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
Synonyms:dutA
Ordered Locus Names:CT1418
OrganismChlorobium tepidum (strain ATCC 49652 / DSM 12025 / TLS) [Reference proteome] [HAMAP]
Taxonomic identifier194439 [NCBI]
Taxonomic lineageBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobaculum

Protein attributes

Sequence length152 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
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

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 – 152152Deoxyuridine 5'-triphosphate nucleotidohydrolase HAMAP-Rule MF_00116
PRO_0000182848

Regions

Region65 – 673Substrate binding By similarity
Region82 – 843Substrate binding By similarity

Sites

Binding site781Substrate By similarity

Experimental info

Sequence conflict61 – 622QL → HV in AAC14879. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O68992 [UniParc].

Last modified August 30, 2002. Version 2.
Checksum: 5A95DA98FD41BEE1

FASTA15216,098
        10         20         30         40         50         60 
MIKVKIVRLN QKAILPVYAT AHAAGMDVSA CLDAPVTVPS SASALIPTGF AIELPEGYEA 

        70         80         90        100        110        120 
QLRPRSGLAL RHCISLPNSP ATIDADYRGE VGVILINHGR EPFTVSHGDR IAQMVVAKVD 

       130        140        150 
HVVFEEVESL SETARGEGGF GHTGVQAKAE CL 

« Hide

References

« Hide 'large scale' references
[1]Bryant D.A., Jakobs C., Stirewalt V.L.
Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Molecular evidence for the early evolution of photosynthesis."
Xiong J., Fischer W.M., Inoue K., Nakahara M., Bauer C.E.
Science 289:1724-1730(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic, anaerobic, green-sulfur bacterium."
Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J., DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D., Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M. expand/collapse author list , Brenner M., Shea T.P., Parksey D.S., Nierman W.C., Feldblyum T.V., Hansen C.L., Craven M.B., Radune D., Vamathevan J.J., Khouri H.M., White O., Gruber T.M., Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A., Fraser C.M.
Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 49652 / DSM 12025 / TLS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF060080 Genomic DNA. Translation: AAC14879.1.
AY005138 Genomic DNA. Translation: AAG12427.1.
AE006470 Genomic DNA. Translation: AAM72646.1.
RefSeqNP_662304.1. NC_002932.3.

3D structure databases

ProteinModelPortalO68992.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING194439.CT1418.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM72646; AAM72646; CT1418.
GeneID1006834.
KEGGcte:CT1418.
PATRIC21400763. VBIChlTep116050_1286.

Phylogenomic databases

eggNOGCOG0756.
HOGENOMHOG000028966.
KOK01520.
OMAPKNTEAQ.
OrthoDBEOG689HXK.
ProtClustDBCLSK637750.

Enzyme and pathway databases

BioCycCTEP194439:GHN0-1457-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_CHLTE
AccessionPrimary (citable) accession number: O68992
Secondary accession number(s): Q93ST9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: August 30, 2002
Last modified: February 19, 2014
This is version 91 of the entry and version 2 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