B7GQI9 (DUT_BIFLS) 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:	Blon_0970, BLIJ_0987

Organism

Bifidobacterium longum subsp. infantis (strain ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12) [Complete proteome] [HAMAP]

Taxonomic identifier

391904 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Bifidobacteriales › Bifidobacteriaceae › Bifidobacterium › Bifidobacterium longum › Bifidobacterium longum subsp. infantis

Protein attributes

Sequence length	158 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 – 158	158	Deoxyuridine 5'-triphosphate nucleotidohydrolase HAMAP-Rule MF_00116		PRO_1000119226
Regions
	Region	75 – 77	3	Substrate binding By similarity
	Region	92 – 94	3	Substrate binding By similarity
Sites
	Binding site	88	1	Substrate By similarity
	Binding site	102	1	Substrate; via amide nitrogen and carbonyl oxygen By similarity

Sequences

	Sequence		Length	Mass (Da)
	B7GQI9 [UniParc]. Last modified February 10, 2009. Version 1. Checksum: 7B68EB219B10ECE1	FASTA	158	16,751
	10 20 30 40 50 60 MAFDETYNEP ESTEVLVKSL DPEHPALLRY AHAGDAGADL ITTVDVTLKP FERALVPTGV 70 80 90 100 110 120 AIALPAGYVA LVHPRSGLAA KQGVTVLNAP GTVDAGYRGE IKVPLINLDP KHTAVFHPGD 130 140 150 RIAQLVIQRY VEARFIPAET LPGSDRAERG FGSTGVAS

References

[1]

"The genome sequence of Bifidobacterium longum subsp. infantis reveals adaptations for milk utilization within the infant microbiome." Sela D.A., Chapman J., Adeuya A., Kim J.H., Chen F., Whitehead T.R., Lapidus A., Rokhsar D.S., Lebrilla C.B., German J.B., Price N.P., Richardson P.M., Mills D.A. Proc. Natl. Acad. Sci. U.S.A. 105:18964-18969(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12.

[2]

"Bifidobacteria can protect from enteropathogenic infection through production of acetate." Fukuda S., Toh H., Hase K., Oshima K., Nakanishi Y., Yoshimura K., Tobe T., Clarke J.M., Topping D.L., Suzuki T., Taylor T.D., Itoh K., Kikuchi J., Morita H., Hattori M., Ohno H. Nature 469:543-547(2011) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001095 Genomic DNA. Translation: ACJ52069.1. AP010889 Genomic DNA. Translation: BAJ68577.1.
RefSeq	YP_002322447.1. NC_011593.1. YP_005584747.1. NC_017219.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	391904.Blon_0970.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ACJ52069; ACJ52069; Blon_0970. BAJ68577; BAJ68577; BLIJ_0987.
GeneID	12166562. 7054288.
KEGG	bln:Blon_0970. blon:BLIJ_0987.
PATRIC	21122904. VBIBifLon71229_0974.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0756.
HOGENOM	HOG000028966.
KO	K01520.
ProtClustDB	CLSK573078.
Enzyme and pathway databases
BioCyc	BLON391904:GCDR-997-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_BIFLS

Accession

Primary (citable) accession number: B7GQI9
Secondary accession number(s): E8MRF2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 28, 2009
Last sequence update:	February 10, 2009
Last modified:	May 29, 2013
This is version 33 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program