ID   DUT_CHLMU               Reviewed;         145 AA.
AC   Q9PKA2;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 2.
DT   28-JAN-2026, entry version 127.
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=TC_0565;
OS   Chlamydia muridarum (strain MoPn / Nigg).
OC   Bacteria; Pseudomonadati; Chlamydiota; Chlamydiia; Chlamydiales;
OC   Chlamydiaceae; Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=243161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MoPn / Nigg;
RX   PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA   Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA   Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA   Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA   Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA   Salzberg S.L., Eisen J.A., Fraser C.M.;
RT   "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT   AR39.";
RL   Nucleic Acids Res. 28:1397-1406(2000).
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 = dUMP + diphosphate + 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; Evidence={ECO:0000255|HAMAP-
CC         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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF39402.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE002160; AAF39402.1; ALT_INIT; Genomic_DNA.
DR   PIR; G81687; G81687.
DR   RefSeq; WP_010230843.1; NC_002620.2.
DR   AlphaFoldDB; Q9PKA2; -.
DR   SMR; Q9PKA2; -.
DR   GeneID; 1245924; -.
DR   KEGG; cmu:TC_0565; -.
DR   eggNOG; COG0756; Bacteria.
DR   HOGENOM; CLU_068508_1_2_0; -.
DR   OrthoDB; 9809956at2; -.
DR   UniPathway; UPA00610; UER00666.
DR   Proteomes; UP000000800; 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-UniRule.
DR   GO; GO:0046081; P:dUTP catabolic process; IEA:InterPro.
DR   CDD; cd07557; trimeric_dUTPase; 1.
DR   FunFam; 2.70.40.10:FF:000008; Deoxyuridine 5'-triphosphate nucleotidohydrolase; 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   NCBIfam; NF001862; PRK00601.1; 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; Magnesium; Metal-binding; Nucleotide metabolism;
KW   Reference proteome.
FT   CHAIN           1..145
FT                   /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase"
FT                   /id="PRO_0000182845"
FT   BINDING         63..65
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00116"
FT   BINDING         76
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00116"
FT   BINDING         80..82
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00116"
SQ   SEQUENCE   145 AA;  15324 MW;  2E79B2A45BBDF0B5 CRC64;
     MKFFCKLESG SSLPEYATSG ASGADVRANI SEPIAILPGQ RALIPTGISV DIPHGYEIQV
     RSRSGLAVKY GVIVLQSPGT VDADYRGEIR VILANLGEST FIVEPGMRIA QLVVAKVEQV
     SFVETQEELT ATARGTGGFG HTGEC
//