C4YFC7 (DUT_CANAW) 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:	DUT1
ORF Names:	CAWG_01243

Organism

Candida albicans (strain WO-1) (Yeast) [Complete proteome]

Taxonomic identifier

294748 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida › Candida albicans

Protein attributes

Sequence length	159 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.
Catalytic activity	dUTP + H2O = dUMP + diphosphate.
Cofactor	Magnesium By similarity.
Pathway	Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2.
Subunit structure	Homotrimer By similarity.
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: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 159	159	Deoxyuridine 5'-triphosphate nucleotidohydrolase		PRO_0000413036
Regions
	Region	78 – 80	3	Substrate binding By similarity
	Region	92 – 95	4	Substrate binding By similarity
	Region	153 – 154	2	Substrate binding By similarity
Sites
	Binding site	103	1	Substrate; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	148	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	C4YFC7 [UniParc]. Last modified July 28, 2009. Version 1. Checksum: 982C016F1D31013A	FASTA	159	16,945
	10 20 30 40 50 60 MTSEDQSLKK QKLESTQSLK VYLRSPKGKV PTKGSALAAG YDLYSAEAAT IPAHGQGLVS 70 80 90 100 110 120 TDISIIVPIG TYGRVAPRSG LAVKHGISTG AGVIDADYRG EVKVVLFNHS EKDFEIKEGD 130 140 150 RIAQLVLEQI VNADIKEISL EELDNTERGE GGFGSTGKN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"MluI site-dependent transcriptional regulation of the Candida albicans dUTPase gene." McIntosh E., Looser J., Haynes R.H., Pearlman R.E. Curr. Genet. 26:415-421(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: WO-1.
[2]	"Evolution of pathogenicity and sexual reproduction in eight Candida genomes." Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S., Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I., Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C., Fitzpatrick D.A., de Groot P.W.J. , Harris D., Hoyer L.L., Hube B., Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D., Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T., Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C., Birren B.W., Kellis M., Cuomo C.A. Nature 459:657-662(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: WO-1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X77925 Genomic DNA. Translation: CAA54897.1. CH672346 Genomic DNA. Translation: EEQ43013.1.
3D structure databases
ProteinModelPortal	C4YFC7.
SMR	C4YFC7. Positions 25-159.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
HOGENOM	HOG000028966.
OMA	KVCLINH.
Enzyme and pathway databases
UniPathway	UPA00610; UER00666.
Family and domain databases
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_CANAW

Accession

Primary (citable) accession number: C4YFC7
Secondary accession number(s): P43058, Q5A912

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 19, 2011
Last sequence update:	July 28, 2009
Last modified:	April 3, 2013
This is version 22 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program