Q54BW5 (DUT_DICDI) 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
ORF Names:	DDB_G0293374

Organism

Dictyostelium discoideum (Slime mold) [Reference proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	179 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 Reference 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 pyrimidine deoxyribonucleoside triphosphate catabolic process Inferred from sequence or structural similarity. Source: dictyBase
Molecular_function	dUTP diphosphatase activity Inferred from sequence or structural similarity. Source: dictyBase 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 – 179	179	Deoxyuridine 5'-triphosphate nucleotidohydrolase		PRO_0000327582
Regions
	Region	97 – 99	3	Substrate binding By similarity
	Region	111 – 114	4	Substrate binding By similarity
	Region	170 – 171	2	Substrate binding By similarity
	Compositional bias	21 – 26	6	Poly-Asn
Sites
	Binding site	122	1	Substrate; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	165	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q54BW5 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: 46187E1F460A533F	FASTA	179	19,532
	10 20 30 40 50 60 MPIEQKYFSL FSNLFKRLTT NNNNNNYLKM APPNFETFKV KKLSDKAIIP QRGSKGAAGY 70 80 90 100 110 120 DLSSAHELVV PAHGKALAMT DLQIAIPDGT YGRIAPRSGL AWKNFIDCGA GVIDSDYRGN 130 140 150 160 170 VGVVLFNHSD VDFKVAVGDR VAQLIFERIV TPEPLEVDEI DETQRGAGGF GSTGVKVQN

References

[1]

"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.

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Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAFI02000204 Genomic DNA. Translation: EAL60754.1.
RefSeq	XP_629169.1. XM_629167.1.
3D structure databases
HSSP	HSSP built from PDB template 1Q5H based on UniProtKB P33316.
ProteinModelPortal	Q54BW5.
SMR	Q54BW5. Positions 38-162.
ModBase	Search...
Protein-protein interaction databases
STRING	44689.DDB_0230111.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblProtists	DDB0230111; DDB0230111; DDB_G0293374.
GeneID	8629190.
KEGG	ddi:DDB_G0293374.
Organism-specific databases
dictyBase	DDB_G0293374. dut.
Phylogenomic databases
eggNOG	COG0756.
KO	K01520.
OMA	KVCLINH.
ProtClustDB	CLSZ2429281.
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_DICDI

Accession

Primary (citable) accession number: Q54BW5

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	May 24, 2005
Last modified:	May 1, 2013
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)