Q8PFR5 (DUT_XANAC) 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:	XAC3913

Organism

Xanthomonas axonopodis pv. citri (strain 306) [Complete proteome] [HAMAP]

Taxonomic identifier

190486 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Xanthomonas › Xanthomonas citri group › Xanthomonas campestris pv. citri › Xanthomonas citri pv. citri

Protein attributes

Sequence length	155 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. HAMAP-Rule MF_00116
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 – 155	155	Deoxyuridine 5'-triphosphate nucleotidohydrolase HAMAP-Rule MF_00116		PRO_0000182919
Regions
	Region	74 – 76	3	Substrate binding By similarity
	Region	91 – 93	3	Substrate binding By similarity
Sites
	Binding site	87	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8PFR5 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: D2CF200EBAFEEBDE	FASTA	155	16,354
	10 20 30 40 50 60 MSPPTQSLQV KLLDPRFGDL WPLPAYATES SAGMDLRAAL EAPMTLQPGD AALIPSGIAI 70 80 90 100 110 120 HLADPQLCAV ILPRSGLGHR HGIVLGNGTG LIDADYQGPL LISTWNRGRE AFTIEPGDRI 130 140 150 AQLVILPIVR MGLQVVDTFV DSARGAGGFG HTGVR

References

[1]

"Comparison of the genomes of two Xanthomonas pathogens with differing host specificities." da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., Ciapina L.P. , Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M., Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P. Nature 417:459-463(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 306.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE008923 Genomic DNA. Translation: AAM38750.1.
RefSeq	NP_644214.1. NC_003919.1.
3D structure databases
ProteinModelPortal	Q8PFR5.
SMR	Q8PFR5. Positions 6-139.
ModBase	Search...
Protein-protein interaction databases
STRING	190486.XAC3913.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAM38750; AAM38750; XAC3913.
GeneID	1157984.
KEGG	xac:XAC3913.
PATRIC	24059990. VBIXanAxo33670_4040.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0756.
HOGENOM	HOG000028968.
KO	K01520.
OMA	ILPRSGM.
ProtClustDB	PRK00601.
Enzyme and pathway databases
BioCyc	XAXO190486:GH55-3913-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_XANAC

Accession

Primary (citable) accession number: Q8PFR5

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 28, 2003
Last sequence update:	October 1, 2002
Last modified:	May 29, 2013
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program