ID A0A1B3MWR5_9SPHN Unreviewed; 151 AA.
AC A0A1B3MWR5;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 42.
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 ECO:0000313|EMBL:AOF97540.1};
GN ORFNames=BSY17_771 {ECO:0000313|EMBL:AOF97540.1};
OS Sphingobium sp. RAC03.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1843368 {ECO:0000313|EMBL:AOF97540.1, ECO:0000313|Proteomes:UP000094323};
RN [1] {ECO:0000313|EMBL:AOF97540.1, ECO:0000313|Proteomes:UP000094323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RAC03 {ECO:0000313|EMBL:AOF97540.1,
RC ECO:0000313|Proteomes:UP000094323};
RA Fixen K.R., Hovde B., Kunde Y.A., Davenport K.W., Johnson S.L., Li P.-E.,
RA Xu Y., Daligault H.E., Deodato C.R., Starkenburg S.R., Cattolico R.A.;
RL Submitted (JUL-2016) 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.
CC {ECO:0000256|ARBA:ARBA00006581, ECO:0000256|HAMAP-Rule:MF_00116}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00116}.
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DR EMBL; CP016456; AOF97540.1; -; Genomic_DNA.
DR RefSeq; WP_069065177.1; NZ_CP016456.1.
DR AlphaFoldDB; A0A1B3MWR5; -.
DR STRING; 1843368.BSY17_771; -.
DR KEGG; sphr:BSY17_771; -.
DR PATRIC; fig|1843368.3.peg.796; -.
DR UniPathway; UPA00610; UER00666.
DR Proteomes; UP000094323; Chromosome.
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; IPR008181; dUTPase.
DR InterPro; IPR029054; dUTPase-like.
DR InterPro; IPR036157; dUTPase-like_sf.
DR InterPro; IPR033704; dUTPase_trimeric.
DR NCBIfam; TIGR00576; dut; 1.
DR PANTHER; PTHR11241; DEOXYURIDINE 5'-TRIPHOSPHATE NUCLEOTIDOHYDROLASE; 1.
DR PANTHER; PTHR11241:SF0; DEOXYURIDINE 5'-TRIPHOSPHATE NUCLEOTIDOHYDROLASE; 1.
DR Pfam; PF00692; dUTPase; 1.
DR SUPFAM; SSF51283; dUTPase-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00116};
KW 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}; Reference proteome {ECO:0000313|Proteomes:UP000094323}.
FT DOMAIN 22..150
FT /note="dUTPase-like"
FT /evidence="ECO:0000259|Pfam:PF00692"
FT BINDING 71..73
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00116"
FT BINDING 84
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00116"
FT BINDING 88..90
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00116"
SQ SEQUENCE 151 AA; 15894 MW; EBFFFB61E154EE71 CRC64;
MPSPLTPIDI QLKRLPHGEG LPVPAYATAH AAGMDVVSAE ELTLQPGGRH AVATGFAMAI
PQGYEVQVRP RSGLALKHGI SLPNTPGTID ADYRGELKII LINLGNAPFP IQRGDRIAQL
VVAPVQLASF VEVDRLDDTE RGQGGFGSTG V
//
