DUT_NITMU
ID DUT_NITMU Reviewed; 149 AA.
AC Q2Y742;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Deoxyuridine 5'-triphosphate nucleotidohydrolase {ECO:0000255|HAMAP-Rule:MF_00116};
DE Short=dUTPase {ECO:0000255|HAMAP-Rule:MF_00116};
DE EC=3.6.1.23 {ECO:0000255|HAMAP-Rule:MF_00116};
DE AltName: Full=dUTP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_00116};
GN Name=dut {ECO:0000255|HAMAP-Rule:MF_00116}; OrderedLocusNames=Nmul_A2136;
OS Nitrosospira multiformis (strain ATCC 25196 / NCIMB 11849 / C 71).
OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosospira.
OX NCBI_TaxID=323848;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25196 / NCIMB 11849 / C 71;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Nitrosospira multiformis ATCC
RT 25196.";
RL Submitted (AUG-2005) 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:0000255|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:0000255|HAMAP-Rule:MF_00116};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00116};
CC -!- PATHWAY: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP
CC route): step 2/2. {ECO:0000255|HAMAP-Rule:MF_00116}.
CC -!- SIMILARITY: Belongs to the dUTPase family. {ECO:0000255|HAMAP-
CC Rule:MF_00116}.
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DR EMBL; CP000103; ABB75429.1; -; Genomic_DNA.
DR RefSeq; WP_011381438.1; NZ_FNVK01000012.1.
DR AlphaFoldDB; Q2Y742; -.
DR SMR; Q2Y742; -.
DR STRING; 323848.Nmul_A2136; -.
DR EnsemblBacteria; ABB75429; ABB75429; Nmul_A2136.
DR KEGG; nmu:Nmul_A2136; -.
DR eggNOG; COG0756; Bacteria.
DR HOGENOM; CLU_068508_1_1_4; -.
DR OMA; YAAFVHP; -.
DR OrthoDB; 1669228at2; -.
DR UniPathway; UPA00610; UER00666.
DR Proteomes; UP000002718; 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 PANTHER; PTHR11241; PTHR11241; 1.
DR Pfam; PF00692; dUTPase; 1.
DR SUPFAM; SSF51283; SSF51283; 1.
DR TIGRFAMs; TIGR00576; dut; 1.
PE 3: Inferred from homology;
KW Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism;
KW Reference proteome.
FT CHAIN 1..149
FT /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase"
FT /id="PRO_0000231416"
FT BINDING 68..70
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00116"
FT BINDING 81
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00116"
FT BINDING 85..87
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00116"
SQ SEQUENCE 149 AA; 15973 MW; C8C680569B825AA3 CRC64;
MKKIDIKILD SRLKDQLPAY ATSGSAGLDL RACIEHVMTI QPGEAHLIPT GIAIHLSDPG
LAALVLPRSG LGHKHGIVMG NLVGLIDSDY QGQIFVSCWN RGQAPFLLNP LERIAQLVVV
PVVQVGFKVV DDFEQSERGA NGFGSTGKH