Q6CQN7 (DUT_KLULA) 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:	KLLA0D15697g

Organism

Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica) [Complete proteome]

Taxonomic identifier

284590 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Kluyveromyces › Kluyveromyces lactis

Protein attributes

Sequence length	148 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 – 148	148	Deoxyuridine 5'-triphosphate nucleotidohydrolase		PRO_0000182933
Regions
	Region	68 – 70	3	Substrate binding By similarity
	Region	82 – 85	4	Substrate binding By similarity
	Region	142 – 143	2	Substrate binding By similarity
Sites
	Binding site	93	1	Substrate; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	137	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6CQN7 [UniParc]. Last modified August 16, 2004. Version 1. Checksum: E835B04A810A3DD3	FASTA	148	15,534
	10 20 30 40 50 60 MTESLSNSLK VQLRSADAKV PTKGSTTAAG YDIYASQPGV IPARGQGIAK TDISFTVPVG 70 80 90 100 110 120 TYGRIAPRSG LAVKHGIQTG AGVVDRDYTG EVGIVLFNHS DKDFQINKGD RVAQLILEKI 130 140 VEDAEIVVVE SLEETQRGAG GFGSTGKN

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 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR382124 Genomic DNA. Translation: CAH00848.1.
RefSeq	XP_453752.1. XM_453752.1.
3D structure databases
ProteinModelPortal	Q6CQN7.
ModBase	Search...
Protein-protein interaction databases
STRING	28985.Q6CQN7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2893442.
KEGG	kla:KLLA0D15697g.
Phylogenomic databases
eggNOG	COG0756.
HOGENOM	HOG000028966.
KO	K01520.
OMA	KVCLINH.
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_KLULA

Accession

Primary (citable) accession number: Q6CQN7

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 7, 2004
Last sequence update:	August 16, 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

Fungal Protein Annotation Program