P61909 (DUT_LEPIC) Reviewed, UniProtKB/Swiss-Prot

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:	LIC_12560

Organism

Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni (strain Fiocruz L1-130) [Complete proteome] [HAMAP]

Taxonomic identifier

267671 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Spirochaetes › Spirochaetia › Spirochaetales › Leptospiraceae › Leptospira › Leptospira interrogans › Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni

Protein attributes

Sequence length	145 AA.
Sequence status	Complete.
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. HAMAP-Rule MF_00116
Catalytic activity	dUTP + H2O = dUMP + diphosphate. HAMAP-Rule MF_00116
Cofactor	Magnesium By similarity.
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 process	Nucleotide metabolism
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	dUMP biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway dUTP metabolic process Inferred from electronic annotation. Source: InterPro
Molecular_function	dUTP diphosphatase activity Inferred from electronic annotation. Source: HAMAP magnesium ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 145	145	Deoxyuridine 5'-triphosphate nucleotidohydrolase HAMAP-Rule MF_00116		PRO_0000182877
Regions
	Region	64 – 66	3	Substrate binding By similarity
	Region	81 – 83	3	Substrate binding By similarity
Sites
	Binding site	77	1	Substrate By similarity
	Binding site	91	1	Substrate; via amide nitrogen and carbonyl oxygen By similarity

Sequences

	Sequence		Length	Mass (Da)
	P61909 [UniParc]. Last modified June 7, 2004. Version 1. Checksum: 70B4A6C3309BED20	FASTA	145	16,182
	10 20 30 40 50 60 MKIFVQKLRP NAELPLLQTK QAAGYDIHAC LDSKLVLEPG NVGLVPTGLS FAIPQEFHFE 70 80 90 100 110 120 IRPRSGFSTK NRILIPNSPG TIDSDYRGEL MIPLLNLGDS SFIIEHGMRI AQLLIRKTWY 130 140 ADWELVSEFA DRTERGANGF GSTGH

References

[1]

"Comparative genomics of two Leptospira interrogans serovars reveals novel insights into physiology and pathogenesis." Nascimento A.L.T.O., Ko A.I., Martins E.A.L., Monteiro-Vitorello C.B., Ho P.L., Haake D.A., Verjovski-Almeida S., Hartskeerl R.A., Marques M.V., Oliveira M.C., Menck C.F.M., Leite L.C.C., Carrer H., Coutinho L.L., Degrave W.M., Dellagostin O.A., El-Dorry H., Ferro E.S. , Ferro M.I.T., Furlan L.R., Gamberini M., Giglioti E.A., Goes-Neto A., Goldman G.H., Goldman M.H.S., Harakava R., Jeronimo S.M.B., Junqueira-de-Azevedo I.L.M., Kimura E.T., Kuramae E.E., Lemos E.G.M., Lemos M.V.F., Marino C.L., Nunes L.R., de Oliveira R.C., Pereira G.G., Reis M.S., Schriefer A., Siqueira W.J., Sommer P., Tsai S.M., Simpson A.J.G., Ferro J.A., Camargo L.E.A., Kitajima J.P., Setubal J.C., Van Sluys M.A. J. Bacteriol. 186:2164-2172(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Fiocruz L1-130.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016823 Genomic DNA. Translation: AAS71124.1.
RefSeq	YP_002487.1. NC_005823.1.
3D structure databases
ProteinModelPortal	P61909.
ModBase	Search...
Protein-protein interaction databases
STRING	267671.LIC12560.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAS71124; AAS71124; LIC_12560.
GeneID	2771885.
KEGG	lic:LIC12560.
PATRIC	22377825. VBILepInt6257_3069.
Organism-specific databases
CMR	Search...
Phylogenomic databases
KO	K01520.
OMA	ILPRSGM.
ProtClustDB	CLSK573773.
Enzyme and pathway databases
BioCyc	LINT267671:GHQI-2821-MONOMER.
UniPathway	UPA00610; UER00666.
Family and domain databases
HAMAP	MF_00116. dUTPase_bact.
InterPro	IPR008180. dUTP_pyroPase. IPR008181. dUTP_pyroPase_sf. [Graphical view]
PANTHER	PTHR11241. PTHR11241. 1 hit.
Pfam	PF00692. dUTPase. 1 hit. [Graphical view]
TIGRFAMs	TIGR00576. dut. 1 hit.
ProtoNet	Search...

Entry information

Entry name

DUT_LEPIC

Accession

Primary (citable) accession number: P61909

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2004
Last sequence update:	June 7, 2004
Last modified:	May 1, 2013
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program