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Database: UniProt
Entry: A0A133Z9G7_9CORY
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Original site: A0A133Z9G7_9CORY 
ID   A0A133Z9G7_9CORY        Unreviewed;       154 AA.
AC   A0A133Z9G7;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
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=HMPREF0307_02412 {ECO:0000313|EMBL:KXB52064.1};
OS   Corynebacterium sp. DNF00584.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1384076 {ECO:0000313|EMBL:KXB52064.1, ECO:0000313|Proteomes:UP000070591};
RN   [1] {ECO:0000313|EMBL:KXB52064.1, ECO:0000313|Proteomes:UP000070591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DNF00584 {ECO:0000313|EMBL:KXB52064.1,
RC   ECO:0000313|Proteomes:UP000070591};
RA   Oliw E.H.;
RL   Submitted (JAN-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}.
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:KXB52064.1}.
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DR   EMBL; LSCZ01000052; KXB52064.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A133Z9G7; -.
DR   PATRIC; fig|1384076.3.peg.2357; -.
DR   UniPathway; UPA00610; UER00666.
DR   Proteomes; UP000070591; 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:UP000070591}.
FT   DOMAIN          23..152
FT                   /note="dUTPase-like"
FT                   /evidence="ECO:0000259|Pfam:PF00692"
FT   BINDING         72..74
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00116"
FT   BINDING         85
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00116"
FT   BINDING         89..91
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00116"
SQ   SEQUENCE   154 AA;  16449 MW;  DCBC384AB3D6E2FF CRC64;
     MTFTTSQEPI ADIRVKRLDP ELPLPQRAHR GDAGADLYAA ETVTLEPEER ALIGTGIAIA
     LPLGTVGLIH PRSGLAAKHG LSIVNTPGTV DADYRGELKV CLINHDPREA FTVERGMRIA
     QLVVQRVELP GFVEVEDLDA TERGAGGYGS TGVN
//
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