Q6FKQ6 (DUT_CANGA) 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
Ordered Locus Names:	CAGL0L09581g

Organism

Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata) [Complete proteome]

Taxonomic identifier

284593 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Nakaseomyces › mitosporic Nakaseomyces › Candida glabrata

Protein attributes

Sequence length	144 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.
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 – 144	144	Deoxyuridine 5'-triphosphate nucleotidohydrolase		PRO_0000182931
Regions
	Region	65 – 67	3	Substrate binding By similarity
	Region	79 – 82	4	Substrate binding By similarity
	Region	139 – 140	2	Substrate binding By similarity
Sites
	Binding site	90	1	Substrate; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	134	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6FKQ6 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: 2F3A261209F0CA63	FASTA	144	15,314
	10 20 30 40 50 60 MSGNVLKVQL RSEHGIAPTK GSVYAAGYDI YASADYVIPA MGQGMVPTDI SFTVPEGTYG 70 80 90 100 110 120 RIAPRSGLAV KHGIQTGAGV VDRDYTGEVK IILFNHSQKD FEIKRGDRVA QLILEKIVDD 130 140 AEVVVVESLE DSQRGAGGFG STGK

References

[1]

"Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L. Nature 430:35-44(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR380958 Genomic DNA. Translation: CAG62158.1.
RefSeq	XP_449188.1. XM_449188.1.
3D structure databases
ProteinModelPortal	Q6FKQ6.
SMR	Q6FKQ6. Positions 6-118.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2891138.
KEGG	cgr:CAGL0L09581g.
Phylogenomic databases
KO	K01520.
OMA	YGTEFSA.
OrthoDB	EOG47M57F.
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_CANGA

Accession

Primary (citable) accession number: Q6FKQ6

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 7, 2004
Last sequence update:	July 19, 2004
Last modified:	May 1, 2013
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program