ID A0A443SYS7_XYLFS Unreviewed; 155 AA. AC A0A443SYS7; DT 08-MAY-2019, integrated into UniProtKB/TrEMBL. DT 08-MAY-2019, sequence version 1. DT 03-JUL-2019, entry version 3. DE RecName: Full=Deoxyuridine 5'-triphosphate nucleotidohydrolase {ECO:0000256|HAMAP-Rule:MF_00116, ECO:0000256|SAAS:SAAS01176036}; DE Short=dUTPase {ECO:0000256|HAMAP-Rule:MF_00116}; DE EC=3.6.1.23 {ECO:0000256|HAMAP-Rule:MF_00116, ECO:0000256|SAAS:SAAS01176044}; DE AltName: Full=dUTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_00116}; GN Name=dut {ECO:0000256|HAMAP-Rule:MF_00116}; GN ORFNames=DVS74_09065 {ECO:0000313|EMBL:RWS33852.1}, XfCFBP8078_07670 GN {ECO:0000313|EMBL:RWA37417.1}; OS Xylella fastidiosa subsp. multiplex. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xylella. OX NCBI_TaxID=644357 {ECO:0000313|EMBL:RWS33852.1, ECO:0000313|Proteomes:UP000288714}; RN [1] {ECO:0000313|EMBL:RWA37417.1, ECO:0000313|Proteomes:UP000288919} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CFBP8078 {ECO:0000313|EMBL:RWA37417.1, RC ECO:0000313|Proteomes:UP000288919}; RA Denance N., Briand M., Gaborieau R., Gaillard S., Jacques M.A.; RT "Identification of genetic relationships and subspecies signatures in RT Xylella fastidiosa."; RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:RWS33852.1, ECO:0000313|Proteomes:UP000288714} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ESVL {ECO:0000313|EMBL:RWS33852.1, RC ECO:0000313|Proteomes:UP000288714}; RX PubMed=30592693; RA Giampetruzzi A., Velasco-Amo M.P., Marco-Noales E., Montes-Borrego M., RA Roman-Ecija M., Navarro I., Monterde A., Barbe S., Almeida R.P.P., RA Saldarelli P., Saponari M., Montilon V., Savino V.N., Boscia D., RA Landa B.B.; RT "Draft Genome Resources of Two Strains ('ESVL' and 'IVIA5901') of RT Xylella fastidiosa Associated with Almond Leaf Scorch Disease in RT Alicante, Spain."; RL Phytopathology 0:PHYTO09180328A-PHYTO09180328A(2018). CC -!- FUNCTION: This enzyme is involved in nucleotide metabolism: it CC produces dUMP, the immediate precursor of thymidine nucleotides CC and it decreases the intracellular concentration of dUTP so that CC uracil cannot be incorporated into DNA. {ECO:0000256|HAMAP- CC Rule:MF_00116, ECO:0000256|SAAS:SAAS01176047}. CC -!- CATALYTIC ACTIVITY: CC Reaction=dUTP + H2O = diphosphate + dUMP + H(+); CC Xref=Rhea:RHEA:10248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:61555, ChEBI:CHEBI:246422; CC EC=3.6.1.23; Evidence={ECO:0000256|HAMAP-Rule:MF_00116, CC ECO:0000256|SAAS:SAAS01176050}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00116, ECO:0000256|SAAS:SAAS01176048}; CC -!- PATHWAY: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP CC (dUTP route): step 2/2. {ECO:0000256|HAMAP-Rule:MF_00116}. CC -!- SIMILARITY: Belongs to the dUTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00116, ECO:0000256|SAAS:SAAS01176039}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00116}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:RWS33852.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; PHFS01000016; RWA37417.1; -; Genomic_DNA. DR EMBL; QPQV01000129; RWS33852.1; -; Genomic_DNA. DR RefSeq; WP_004085509.1; NZ_QPQW01000139.1. DR SMR; A0A443SYS7; -. DR UniPathway; UPA00610; UER00666. DR Proteomes; UP000288714; Unassembled WGS sequence. DR Proteomes; UP000288919; Unassembled WGS sequence. DR GO; GO:0004170; F:dUTP diphosphatase activity; IEA:UniProtKB-UniRule. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0006226; P:dUMP biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0046080; P:dUTP metabolic process; IEA:InterPro. DR CDD; cd07557; trimeric_dUTPase; 1. DR Gene3D; 2.70.40.10; -; 1. DR HAMAP; MF_00116; dUTPase_bact; 1. DR InterPro; IPR029054; dUTPase-like. DR InterPro; IPR036157; dUTPase-like_sf. DR InterPro; IPR008181; dUTPase_1. DR InterPro; IPR033704; dUTPase_trimeric. DR PANTHER; PTHR11241; PTHR11241; 1. DR Pfam; PF00692; dUTPase; 1. DR SUPFAM; SSF51283; SSF51283; 1. DR TIGRFAMs; TIGR00576; dut; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000288714, KW ECO:0000313|Proteomes:UP000288919}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00116, KW ECO:0000256|SAAS:SAAS01176051, ECO:0000313|EMBL:RWS33852.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00116, KW ECO:0000256|SAAS:SAAS01176034}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00116, KW ECO:0000256|SAAS:SAAS01176043}; KW Nucleotide metabolism {ECO:0000256|HAMAP-Rule:MF_00116, KW ECO:0000256|SAAS:SAAS01176045}. FT DOMAIN 21 153 dUTPase. {ECO:0000259|Pfam:PF00692}. FT REGION 74 76 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00116}. FT REGION 91 93 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00116}. FT BINDING 87 87 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00116}. SQ SEQUENCE 155 AA; 16260 MW; 2E047246225348DF CRC64; MSAAVKPLQI KILDPRLGTV WPLPTYATEA SAGLDLRAAL DAPMTLVPGD AELLSTGIAI HLVDPSLCAV VLPRSGLGHR HGIVLGNGTG LIDSDYQGPL LVSLWNRGRE AFTIEPGDRI AQLVVLPIVR VVLQVVDTFV ESGRGAGGFG HTGVR //