Reviewed, UniProtKB/Swiss-Prot Q45920 (DUT_COXBU)

Names and origin

Protein names

Recommended 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:	CBU_0293

Organism

Coxiella burnetii [Complete proteome] [HAMAP]

Taxonomic identifier

777 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Legionellales › Coxiellaceae › Coxiella

Protein attributes

Sequence length	152 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred 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.
Catalytic activity	dUTP + H(2)O = dUMP + diphosphate.
Pathway	Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2.
Sequence similarities	Belongs to the dUTPase family.

Ontologies

Keywords
Biological process	Nucleotide metabolism
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Molecular function	dUTP diphosphatase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Chain	1 – 152	152	Deoxyuridine 5'-triphosphate nucleotidohydrolase

Sequences

	Sequence		Length	Mass (Da)
	Q45920-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 00041727C1882C57	FASTA	152	16,214
	10 20 30 40 50 60 MTHSVQLKIL DKRLGSEFPL PAYATTGSAG LDLRACLDEP LKIEPDETCL ISTGLAIYLG 70 80 90 100 110 120 HSNVAATILP RSGLGHKHGI VLGNLVGLID SDYQGPLMVS CWNRGKEPYT INPGDRIAQL 130 140 150 VVLPILKAQF AVVEEFELTE RGAGGFGSSG QN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Thiele D., Willems H., Oswald W., Krauss H. Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Nine Mile phase I.
[2]	"Complete genome sequence of the Q-fever pathogen, Coxiella burnetii." Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C., Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M., Lee K.H., Carty H.A. , Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E., Fraser C.M., Heidelberg J.F. Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003) [PubMed: 12704232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Nine Mile phase I / RSA 493.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X79075 Genomic DNA. Translation: CAA55678.1. AE016828 Genomic DNA. Translation: AAO89850.1.
PIR	S44300.
RefSeq	NP_819336.1.
3D structure databases
HSSP	HSSP built from PDB template 1EUW based on UniProtKB P06968.
ModBase	Search...
Genome annotation databases
GeneID	1208175.
GenomeReviews	Gene locus CBU_0293 in contig AE016828_GR.
KEGG	cbu:CBU_0293.
NMPDR	fig|227377.1.peg.280.
TIGR	CBU_0293.
Phylogenomic databases
HOGENOM	Q45920.
Enzyme and pathway databases
BioCyc	CBUR227377:CBU_0293-MON.
Family and domain databases
HAMAP	MF_00116. [Tree]
InterPro	IPR008180. DeoxyUTPase. IPR008181. dUTP_pyrophosphatase_subfam_1. [Graphical view]
Pfam	PF00692. dUTPase. 1 hit. [Graphical view]
TIGRFAMs	TIGR00576. dut. 1 hit.
ProDom	Q45920. [Graphical view] [Entries sharing at least one domain]
BLOCKS	Search...
Other Resources
ProtoNet	Search...

Entry information

Entry name

DUT_COXBU

Accession

Primary (citable) accession number: Q45920

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	November 1, 1996
Last modified:	July 22, 2008
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)