ID A0A443SYS7_XYLFS Unreviewed; 155 AA. AC A0A443SYS7; DT 08-MAY-2019, integrated into UniProtKB/TrEMBL. DT 08-MAY-2019, sequence version 1. DT 07-OCT-2020, entry version 11. DE RecName: Full=Deoxyuridine 5'-triphosphate nucleotidohydrolase {ECO:0000256|HAMAP-Rule:MF_00116}; DE Short=dUTPase {ECO:0000256|HAMAP-Rule:MF_00116}; DE EC=3.6.1.23 {ECO:0000256|HAMAP-Rule:MF_00116}; DE AltName: Full=dUTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_00116}; GN Name=dut {ECO:0000256|HAMAP-Rule:MF_00116}; GN ORFNames=FGX01_15630 {ECO:0000313|EMBL:MRT35016.1}, FGX02_10875 GN {ECO:0000313|EMBL:MRU34103.1}; OS Xylella fastidiosa subsp. multiplex. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xylella. OX NCBI_TaxID=644357 {ECO:0000313|EMBL:MRU34103.1, ECO:0000313|Proteomes:UP000429209}; RN [1] {ECO:0000313|EMBL:MRU34103.1, ECO:0000313|Proteomes:UP000429209, ECO:0000313|Proteomes:UP000469171} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IVIA6902 {ECO:0000313|EMBL:MRT35016.1, RC ECO:0000313|Proteomes:UP000469171}, and IVIA6903 RC {ECO:0000313|EMBL:MRU34103.1, ECO:0000313|Proteomes:UP000429209}; RX PubMed=31704683; RA Landa B.B., Castillo A.I., Giampetruzzi A., Kahn A., Roman-Ecija M., RA Velasco-Amo M.P., Navas-Cortes J.A., Marco-Noales E., Barbe S., RA Moralejo E., Coletta-Filho H.D., Saldarelli P., Saponari M., RA Almeida R.P.P.; RT "Multiple intercontinental introductions associated with the emergence of a RT plant pathogen in Europe."; RL Appl. Environ. Microbiol. 0:0-0(2019). RN [2] {ECO:0000313|EMBL:MRT35016.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=IVIA6902 {ECO:0000313|EMBL:MRT35016.1}; RA Castillo A., Giampetruzzi A., Landa B., Saponari M., Almeida R.P.P., RA Moralejo E., Marco-Noales E., Velasco-Amo M.P., Roman-Ecija M., Navarro I., RA Monterde A., Barbe S.; RL Submitted (MAY-2019) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:MRU34103.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=IVIA6903 {ECO:0000313|EMBL:MRU34103.1}; RA Castillo A., Giampetruzzi A., Landa B., Saponari M., Almeida R., RA Moralejo E., Marco-Noales E., Velasco-Amo M.P., Roman-Ecija M., Navarro I., RA Monterde A., Barbe S.; RL Submitted (MAY-2019) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: This enzyme is involved in nucleotide metabolism: it produces CC dUMP, the immediate precursor of thymidine nucleotides and it decreases CC the intracellular concentration of dUTP so that uracil cannot be CC incorporated into DNA. {ECO:0000256|HAMAP-Rule:MF_00116}. CC -!- CATALYTIC ACTIVITY: CC Reaction=dUTP + H2O = diphosphate + dUMP + H(+); Xref=Rhea:RHEA:10248, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:61555, ChEBI:CHEBI:246422; EC=3.6.1.23; CC Evidence={ECO:0000256|ARBA:ARBA00000878, ECO:0000256|HAMAP- CC Rule:MF_00116}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00116}; CC -!- PATHWAY: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP CC route): step 2/2. {ECO:0000256|HAMAP-Rule:MF_00116}. CC -!- SIMILARITY: Belongs to the dUTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00116}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00116}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:MRU34103.1}. 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; VCPO01001582; MRT35016.1; -; Genomic_DNA. DR EMBL; VCPP01000532; MRU34103.1; -; Genomic_DNA. DR RefSeq; WP_004085509.1; NZ_VDDF01000186.1. DR SMR; A0A443SYS7; -. DR UniPathway; UPA00610; UER00666. DR Proteomes; UP000429209; Unassembled WGS sequence. DR Proteomes; UP000469171; 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:0046081; P:dUTP catabolic 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00116, KW ECO:0000313|EMBL:MRU34103.1}; Magnesium {ECO:0000256|HAMAP-Rule:MF_00116}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00116}; KW Nucleotide metabolism {ECO:0000256|ARBA:ARBA00023080, ECO:0000256|HAMAP- KW Rule:MF_00116}. FT DOMAIN 21..153 FT /note="dUTPase" FT /evidence="ECO:0000259|Pfam:PF00692" FT REGION 74..76 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00116" FT REGION 91..93 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00116" FT BINDING 87 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule: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 //