ID A0A2H6J849_9BACT Unreviewed; 152 AA. AC A0A2H6J849; DT 28-FEB-2018, integrated into UniProtKB/TrEMBL. DT 28-FEB-2018, sequence version 1. DT 28-MAR-2018, entry version 2. DE RecName: Full=Deoxyuridine 5'-triphosphate nucleotidohydrolase {ECO:0000256|HAMAP-Rule:MF_00116, ECO:0000256|SAAS:SAAS00759934}; DE Short=dUTPase {ECO:0000256|HAMAP-Rule:MF_00116}; DE EC=3.6.1.23 {ECO:0000256|HAMAP-Rule:MF_00116, ECO:0000256|SAAS:SAAS00759949}; DE AltName: Full=dUTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_00116}; GN Name=dut {ECO:0000256|HAMAP-Rule:MF_00116, GN ECO:0000313|EMBL:GBE46922.1}; GN ORFNames=BMS3Bbin12_00075 {ECO:0000313|EMBL:GBE46922.1}; OS bacterium BMS3Bbin12. OC Bacteria. OX NCBI_TaxID=2005735 {ECO:0000313|EMBL:GBE46922.1}; RN [1] {ECO:0000313|EMBL:GBE46922.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BMS3Bbin12 {ECO:0000313|EMBL:GBE46922.1}; RA Kato S., Shibuya T., Takaki Y., Hirai M., Nunoura T., Suzuki K.; RT "Genome-enabled metabolic reconstruction of dominant chemosynthetic RT colonizers in deep-sea massive sulfide deposits."; RL Environ. Microbiol. 0:0-0(2017). 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:SAAS00759945}. CC -!- CATALYTIC ACTIVITY: dUTP + H(2)O = dUMP + diphosphate. CC {ECO:0000256|HAMAP-Rule:MF_00116, ECO:0000256|SAAS:SAAS00759957}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00116, ECO:0000256|SAAS:SAAS00759926}; 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:SAAS00759922}. 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:GBE46922.1}. 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; BDTV01000006; GBE46922.1; -; Genomic_DNA. DR UniPathway; UPA00610; UER00666. 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 Pfam; PF00692; dUTPase; 1. DR SUPFAM; SSF51283; SSF51283; 1. DR TIGRFAMs; TIGR00576; dut; 1. PE 3: Inferred from homology; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00116, KW ECO:0000256|SAAS:SAAS00759968, ECO:0000313|EMBL:GBE46922.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00116, KW ECO:0000256|SAAS:SAAS00759937}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00116, KW ECO:0000256|SAAS:SAAS00759930}; KW Nucleotide metabolism {ECO:0000256|HAMAP-Rule:MF_00116, KW ECO:0000256|SAAS:SAAS00759928}. FT DOMAIN 19 150 dUTPase. {ECO:0000259|Pfam:PF00692}. FT REGION 71 73 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00116}. FT REGION 88 90 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00116}. FT BINDING 84 84 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00116}. SQ SEQUENCE 152 AA; 16066 MW; F1106FC66EB3A9CF CRC64; MPRTVQLKVL DPRIGREIPP PDYATAGAAG LDLRACLDAP ITLAAGETTL IPTGIAIHID DPGLAAVLLP RSGLGHKHGI VLGNLVGLID SDYQGQVFVS CWNRGGAPFT IEIGERIAQM VFMPVVQARF ERVEEFEASA RGAGGFGHSG RL //