ID   Q1MS81_LAWIP            Unreviewed;       160 AA.
AC   Q1MS81;
DT   30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   30-MAY-2006, sequence version 1.
DT   04-NOV-2026, entry version 113.
DE   RecName: Full=dUTP diphosphatase {ECO:0000256|ARBA:ARBA00012379};
DE            EC=3.6.1.23 {ECO:0000256|ARBA:ARBA00012379};
GN   Name=dut {ECO:0000313|EMBL:CAJ54144.1};
GN   OrderedLocusNames=LI0088 {ECO:0000313|EMBL:CAJ54144.1};
OS   Lawsonia intracellularis (strain PHE/MN1-00).
OC   Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfovibrionia;
OC   Desulfovibrionales; Desulfovibrionaceae; Lawsonia.
OX   NCBI_TaxID=363253 {ECO:0000313|EMBL:CAJ54144.1, ECO:0000313|Proteomes:UP000002430};
RN   [1] {ECO:0000313|EMBL:CAJ54144.1, ECO:0000313|Proteomes:UP000002430}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHE/MN1-00 {ECO:0000313|EMBL:CAJ54144.1,
RC   ECO:0000313|Proteomes:UP000002430};
RA   Kaur K., Zhang Q., Beckler D., Munir S., Li L., Kinsley K., Herron L.,
RA   Peterson A., May B., Singh S., Gebhart C., Kapur V.;
RT   "The complete genome sequence of Lawsonia intracellularis: the causative
RT   agent of proliferative enteropathy.";
RL   Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00047686};
CC   -!- SIMILARITY: Belongs to the dUTPase family.
CC       {ECO:0000256|ARBA:ARBA00006581}.
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DR   EMBL; AM180252; CAJ54144.1; -; Genomic_DNA.
DR   RefSeq; WP_011526171.1; NC_008011.1.
DR   AlphaFoldDB; Q1MS81; -.
DR   STRING; 363253.LI0088; -.
DR   GeneID; 310556149; -.
DR   KEGG; lip:LI0088; -.
DR   eggNOG; COG0756; Bacteria.
DR   HOGENOM; CLU_068508_1_1_7; -.
DR   OMA; AACFDLH; -.
DR   OrthoDB; 9809956at2; -.
DR   Proteomes; UP000002430; Chromosome.
DR   GO; GO:0004170; F:dUTP diphosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0006226; P:dUMP biosynthetic process; IEA:InterPro.
DR   GO; GO:0046081; P:dUTP catabolic process; IEA:InterPro.
DR   CDD; cd07557; trimeric_dUTPase; 1.
DR   Gene3D; 2.70.40.10; -; 1.
DR   InterPro; IPR008181; dUTPase.
DR   InterPro; IPR029054; dUTPase-like.
DR   InterPro; IPR036157; dUTPase-like_sf.
DR   InterPro; IPR033704; dUTPase_trimeric.
DR   NCBIfam; NF001862; dut; 1.
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};
KW   Nucleotide metabolism {ECO:0000256|ARBA:ARBA00023080};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002430}.
FT   DOMAIN          28..158
FT                   /note="dUTPase-like"
FT                   /evidence="ECO:0000259|Pfam:PF00692"
SQ   SEQUENCE   160 AA;  17336 MW;  849F08B70E8445A1 CRC64;
     MSAFLHSEVS IRFMYLRDAK KIYTTSGIAY ETPASVGLDL RACIEETSLT ILPGERETIP
     CGIAIEPLEK NIAGFVYSRS GLGAIHGLTV AQGVGVIDPD YRGEIIVVLL NTAKNPVHVN
     RGDRIAQLVF QPAFQVSLVE TQQLDNTSRG SFGFGHTGKN
//