UniProt Accession

 DUT_ECOLI; P06968; Q2M7V4 

Genbank Protein ID

 X01714; V01578; L10328; U00096; AP009048 

Genbank Nucleotide ID

 CAA25859.1; CAA24897.1; AAA61993.1; AAC76664.1; BAE77652.1 

Protein Name

 Deoxyuridine 5'-triphosphate nucleotidohydrolase 

Protein Synonyms/Alias

 dUTPase; dUTP pyrophosphatase 

Gene Name

 dut 

Gene Synonyms/Alias

 dnaS; sof; b3640; JW3615 

Created Date

 July 27, 2013 

Organism

 Escherichia coli (strain K12) 

NCBI Taxa ID

 83333 

Lysine Modification

Position	Peptide	Type	References
3	*****MKKIDVKILD	acetylation	[1]
7	*MKKIDVKILDPRVG	acetylation	[1]
15	ILDPRVGKEFPLPTY	acetylation	[1]
15	ILDPRVGKEFPLPTY	pupylation	[2]

Reference

 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618]
 [2] Reconstitution of the Mycobacterium tuberculosis pupylation pathway in Escherichia coli.
 Cerda-Maira FA, McAllister F, Bode NJ, Burns KE, Gygi SP, Darwin KH.
 EMBO Rep. 2011 Jul 8;12(8):863-70. [PMID: 21738222] 

Functional Description

 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. 

Sequence Annotation

 REGION 70 72 Substrate binding (By similarity).
 REGION 87 89 Substrate binding (Probable).
 BINDING 83 83 Substrate.
 BINDING 97 97 Substrate; via amide nitrogen and  

Keyword

 3D-structure; Complete proteome; Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 151 AA 

Protein Sequence

Gene Ontology

 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0004170; F:dUTP diphosphatase activity; IDA:EcoCyc.
 GO:0000287; F:magnesium ion binding; IEA:HAMAP.
 GO:0006226; P:dUMP biosynthetic process; IEA:UniProtKB-UniPathway.
 GO:0046080; P:dUTP metabolic process; IEA:InterPro. 

Interpro

 IPR008180; dUTP_pyroPase.
 IPR008181; dUTP_pyroPase_sf. 

Pfam

 PF00692; dUTPase 

SMART

  

PROSITE

  

PRINTS