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Database: UniProt
Entry: A0A1H8VFJ9_9GAMM
LinkDB: A0A1H8VFJ9_9GAMM
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ID   A0A1H8VFJ9_9GAMM        Unreviewed;       151 AA.
AC   A0A1H8VFJ9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
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=SAMN04488052_11228 {ECO:0000313|EMBL:SEP14169.1};
OS   Aquisalimonas asiatica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Aquisalimonas.
OX   NCBI_TaxID=406100 {ECO:0000313|EMBL:SEP14169.1, ECO:0000313|Proteomes:UP000199657};
RN   [1] {ECO:0000313|EMBL:SEP14169.1, ECO:0000313|Proteomes:UP000199657}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.6291 {ECO:0000313|EMBL:SEP14169.1,
RC   ECO:0000313|Proteomes:UP000199657};
RA   de Groot N.N.;
RL   Submitted (OCT-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; FOEG01000012; SEP14169.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H8VFJ9; -.
DR   STRING; 406100.SAMN04488052_11228; -.
DR   OrthoDB; 9809956at2; -.
DR   UniPathway; UPA00610; UER00666.
DR   Proteomes; UP000199657; 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; 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:UP000199657}.
FT   DOMAIN          16..149
FT                   /note="dUTPase-like"
FT                   /evidence="ECO:0000259|Pfam:PF00692"
FT   BINDING         70..72
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00116"
FT   BINDING         83
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00116"
FT   BINDING         87..89
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00116"
SQ   SEQUENCE   151 AA;  16084 MW;  E59F87300B81D180 CRC64;
     MTTVDVRMLD ARLNNEWGLP GYATDGSAGV DLRACLEGET LLAPDATLLI PTGLAIHMGD
     PTLAAVILPR SGLGHKHGIV LGNLVGLIDS DYQGEVFVSC WNRSRDTYTV QPGDRIAQLV
     FVPVVRPELR VVDSFEASER GAGGFGHSGR S
//
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