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Database: UniProt
Entry: V9W9A2_9BACL
LinkDB: V9W9A2_9BACL
Original site: V9W9A2_9BACL 
ID   V9W9A2_9BACL            Unreviewed;       152 AA.
AC   V9W9A2;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   RecName: Full=dUTP diphosphatase {ECO:0000256|ARBA:ARBA00012379};
DE            EC=3.6.1.23 {ECO:0000256|ARBA:ARBA00012379};
GN   Name=dut2 {ECO:0000313|EMBL:AHD06474.1};
GN   ORFNames=ERIC2_c26870 {ECO:0000313|EMBL:AHD06474.1};
OS   Paenibacillus larvae subsp. larvae DSM 25430.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=697284 {ECO:0000313|EMBL:AHD06474.1, ECO:0000313|Proteomes:UP000029431};
RN   [1] {ECO:0000313|EMBL:AHD06474.1, ECO:0000313|Proteomes:UP000029431}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25430 {ECO:0000313|EMBL:AHD06474.1,
RC   ECO:0000313|Proteomes:UP000029431};
RX   PubMed=24599066;
RA   Djukic M., Brzuszkiewicz E., Funfhaus A., Voss J., Gollnow K., Poppinga L.,
RA   Liesegang H., Garcia-Gonzalez E., Genersch E., Daniel R.;
RT   "How to Kill the Honey Bee Larva: Genomic Potential and Virulence
RT   Mechanisms of Paenibacillus larvae.";
RL   PLoS ONE 9:E90914-E90914(2014).
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};
CC   -!- SIMILARITY: Belongs to the dUTPase family.
CC       {ECO:0000256|ARBA:ARBA00006581}.
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DR   EMBL; CP003355; AHD06474.1; -; Genomic_DNA.
DR   RefSeq; WP_024094662.1; NZ_CP019652.1.
DR   AlphaFoldDB; V9W9A2; -.
DR   KEGG; plv:ERIC2_c26870; -.
DR   PATRIC; fig|697284.3.peg.2545; -.
DR   eggNOG; COG0756; Bacteria.
DR   HOGENOM; CLU_068508_1_2_9; -.
DR   Proteomes; UP000029431; 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; 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:0000313|EMBL:AHD06474.1};
KW   Nucleotide metabolism {ECO:0000256|ARBA:ARBA00023080};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029431}.
FT   DOMAIN          12..150
FT                   /note="dUTPase-like"
FT                   /evidence="ECO:0000259|Pfam:PF00692"
SQ   SEQUENCE   152 AA;  16458 MW;  0FCFBBC6A21A3137 CRC64;
     MEIKIKKIHP DAVIPEYATA GAAGFDLVAL EDVIIEPGDV KTIRTGLAFE IPVGYELQIR
     PRSGVSLKTK LRQPNSVGTI DSDYRGEVQL MFENTLTKLA HLNVKLASYL IQKGDRLAQG
     IIAPVERAKF TVVDELSGTE RGAGGFGHTG VQ
//
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