DUT_RICPR
ID DUT_RICPR Reviewed; 148 AA.
AC Q9ZDD2;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 112.
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=RP399;
OS Rickettsia prowazekii (strain Madrid E).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=272947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Madrid E;
RX PubMed=9823893; DOI=10.1038/24094;
RA Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA Kurland C.G.;
RT "The genome sequence of Rickettsia prowazekii and the origin of
RT mitochondria.";
RL Nature 396:133-140(1998).
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; AJ235271; CAA14856.1; -; Genomic_DNA.
DR PIR; F71697; F71697.
DR RefSeq; NP_220780.1; NC_000963.1.
DR RefSeq; WP_004597580.1; NC_000963.1.
DR PDB; 7N56; X-ray; 2.15 A; A/B/C/D/E/F/G/H/I/J/K/L=1-148.
DR PDB; 7N6S; X-ray; 1.75 A; A/B/C/D/E/F=1-148.
DR PDBsum; 7N56; -.
DR PDBsum; 7N6S; -.
DR AlphaFoldDB; Q9ZDD2; -.
DR SMR; Q9ZDD2; -.
DR STRING; 272947.RP399; -.
DR EnsemblBacteria; CAA14856; CAA14856; CAA14856.
DR GeneID; 57569524; -.
DR KEGG; rpr:RP399; -.
DR PATRIC; fig|272947.5.peg.412; -.
DR eggNOG; COG0756; Bacteria.
DR HOGENOM; CLU_068508_1_2_5; -.
DR OMA; YAAFVHP; -.
DR UniPathway; UPA00610; UER00666.
DR Proteomes; UP000002480; 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 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism;
KW Reference proteome.
FT CHAIN 1..148
FT /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase"
FT /id="PRO_0000182903"
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"
FT BINDING 95
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00116"
FT STRAND 3..10
FT /evidence="ECO:0007829|PDB:7N6S"
FT STRAND 27..32
FT /evidence="ECO:0007829|PDB:7N6S"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:7N6S"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:7N6S"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:7N6S"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:7N6S"
FT HELIX 69..75
FT /evidence="ECO:0007829|PDB:7N6S"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:7N6S"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:7N6S"
FT STRAND 95..100
FT /evidence="ECO:0007829|PDB:7N6S"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:7N6S"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:7N6S"
FT STRAND 113..121
FT /evidence="ECO:0007829|PDB:7N6S"
FT STRAND 123..129
FT /evidence="ECO:0007829|PDB:7N6S"
FT TURN 138..141
FT /evidence="ECO:0007829|PDB:7N6S"
SQ SEQUENCE 148 AA; 16068 MW; 23A97A89A3702001 CRC64;
MTIIEVKIKK LENFLGNLPE YATEHSAGMD LVAANEQSIT IKVGSIQLIP TGIAIALPES
FEAQIRPRSG LAVKHGITVA NSPGTIDADY RGEIKVLLIN LGNKDFIIEK GMRIAQMIIA
KYERVLWAET SILTETMRGR GGFGSTGL
