ID A0A163UXC1_9BACT Unreviewed; 148 AA.
AC A0A163UXC1; A0A161SG81;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
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:NLI02391.1};
GN ORFNames=AO394_05290 {ECO:0000313|EMBL:KZD17612.1}, GX473_03540
GN {ECO:0000313|EMBL:NLI02391.1};
OS Candidatus Fermentibacter daniensis.
OC Bacteria; Candidatus Fermentibacteria; Candidatus Fermentibacteria (class);
OC Candidatus Fermentibacterales; Candidatus Fermentibacteraceae;
OC Fermentibacter.
OX NCBI_TaxID=1729713 {ECO:0000313|EMBL:KZD17612.1, ECO:0000313|Proteomes:UP000076793};
RN [1] {ECO:0000313|EMBL:KZD17612.1, ECO:0000313|Proteomes:UP000076793}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Dam_1 {ECO:0000313|EMBL:KZD17612.1};
RX PubMed=27058503;
RA Kirkegaard R.H., Dueholm M.S., McIlroy S.J., Nierychlo M., Karst S.M.,
RA Albertsen M., Nielsen P.H.;
RT "Genomic insights into members of the candidate phylum Hyd24-12 common in
RT mesophilic anaerobic digesters.";
RL ISME J. 0:0-0(2016).
RN [2] {ECO:0000313|EMBL:NLI02391.1, ECO:0000313|Proteomes:UP000567630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AS4DglBPLU_32 {ECO:0000313|EMBL:NLI02391.1};
RX PubMed=32123542;
RA Campanaro S., Treu L., Rodriguez-R L.M., Kovalovszki A., Ziels R.M.,
RA Maus I., Zhu X., Kougias P.G., Basile A., Luo G., Schluter A.,
RA Konstantinidis K.T., Angelidaki I.;
RT "New insights from the biogas microbiome by comprehensive genome-resolved
RT metagenomics of nearly 1600 species originating from multiple anaerobic
RT digesters.";
RL Biotechnol. Biofuels 13:25-20(2020).
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:KZD17612.1}.
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DR EMBL; LKHB01000189; KZD17612.1; -; Genomic_DNA.
DR EMBL; JAAYWI010000027; NLI02391.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A163UXC1; -.
DR STRING; 1729713.AO395_08115; -.
DR UniPathway; UPA00610; UER00666.
DR Proteomes; UP000076793; Unassembled WGS sequence.
DR Proteomes; UP000567630; 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}.
FT DOMAIN 17..145
FT /note="dUTPase-like"
FT /evidence="ECO:0000259|Pfam:PF00692"
FT BINDING 67..69
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00116"
FT BINDING 80
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00116"
FT BINDING 84..86
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00116"
SQ SEQUENCE 148 AA; 15437 MW; 6DA8C753F1F04291 CRC64;
MNRILVSVLP HGEGLPLPVR ATAGSSGFDL HAAIDGETTL SPGQRAVVPT GIRVAVPDGF
EWQVRPRSGN AARHGLTVLN SPGTVDSDYR GEVGVILINL GDGPVTIRRG DRIAQAVLCE
VPETEIVKVD SLPDTGRGDG GFGHSDRG
//
