ID A0A3A5I3X1_BACIU Unreviewed; 142 AA. AC A0A3A5I3X1; DT 05-DEC-2018, integrated into UniProtKB/TrEMBL. DT 05-DEC-2018, sequence version 1. DT 10-APR-2019, entry version 4. DE RecName: Full=Deoxyuridine 5'-triphosphate nucleotidohydrolase {ECO:0000256|SAAS:SAAS01088750}; DE EC=3.6.1.23 {ECO:0000256|SAAS:SAAS01088736}; GN ORFNames=CJ481_17295 {ECO:0000313|EMBL:RJS57486.1}; OS Bacillus subtilis. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1423 {ECO:0000313|EMBL:RJS57486.1, ECO:0000313|Proteomes:UP000279300}; RN [1] {ECO:0000313|EMBL:RJS57486.1, ECO:0000313|Proteomes:UP000279300} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PK3_2 {ECO:0000313|EMBL:RJS57486.1, RC ECO:0000313|Proteomes:UP000279300}; RA Bokhari A., Bougouffa S., Essack M., Andres-Barrao C., Saad M., RA Bajic V.B., Hirt H.; RT "Complete genomes of four Endophytic plant-growth promoting Bacillus RT that were isolated from a desert in Pakistan."; RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases. 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. CC {ECO:0000256|SAAS:SAAS01088743}. 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|SAAS:SAAS01123170}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|SAAS:SAAS01088733}; CC -!- SIMILARITY: Belongs to the dUTPase family. CC {ECO:0000256|SAAS:SAAS01088746}. 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:RJS57486.1}. 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; NQYD01000001; RJS57486.1; -; Genomic_DNA. DR Proteomes; UP000279300; Unassembled WGS sequence. DR GO; GO:0004170; F:dUTP diphosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0046080; P:dUTP metabolic process; IEA:InterPro. DR CDD; cd07557; trimeric_dUTPase; 1. DR Gene3D; 2.70.40.10; -; 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. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000279300}; KW Hydrolase {ECO:0000256|SAAS:SAAS01088744, KW ECO:0000313|EMBL:RJS57486.1}; KW Magnesium {ECO:0000256|SAAS:SAAS01088729}; KW Metal-binding {ECO:0000256|SAAS:SAAS01088734}; KW Nucleotide metabolism {ECO:0000256|SAAS:SAAS01088751}. FT DOMAIN 25 139 dUTPase. {ECO:0000259|Pfam:PF00692}. SQ SEQUENCE 142 AA; 16140 MW; 89C0C5B4D597DCF9 CRC64; MQIKIKYLDE TQTRISKIEQ GDWIDLRAAE DVAIKKDEFK LVPLGVAMEL PEGYEAHVVP RSSTYKNFGV IQTNSMGVID ESYKGDTDFW FFPAYALRDT EIKKGDRICQ FRIIKKMPAV ELVEVEHLGN EDRGGHGSTG TK //