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Database: UniProt
Entry: A0A087N6A7_9SPHN
LinkDB: A0A087N6A7_9SPHN
Original site: A0A087N6A7_9SPHN 
ID   A0A087N6A7_9SPHN        Unreviewed;       118 AA.
AC   A0A087N6A7;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=dUTP diphosphatase {ECO:0000256|ARBA:ARBA00012379};
DE            EC=3.6.1.23 {ECO:0000256|ARBA:ARBA00012379};
GN   ORFNames=IL54_0026 {ECO:0000313|EMBL:KFL44660.1};
OS   Sphingobium sp. ba1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=1522072 {ECO:0000313|EMBL:KFL44660.1, ECO:0000313|Proteomes:UP000029094};
RN   [1] {ECO:0000313|EMBL:KFL44660.1, ECO:0000313|Proteomes:UP000029094}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ba1 {ECO:0000313|Proteomes:UP000029094};
RA   Manzari C., Chiara M., Costanza A., Leoni C., Picardi E., Trotta M.,
RA   Volpicella M., D'Erchia A.M., Horner D.S., Pesole G., Ceci L.R.;
RT   "Draft genome sequence of a Kanamycin and Nickel resistant bacterium
RT   Sphingobium species.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KFL44660.1}.
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DR   EMBL; JPPQ01000083; KFL44660.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A087N6A7; -.
DR   PATRIC; fig|1522072.3.peg.4064; -.
DR   eggNOG; COG0756; Bacteria.
DR   Proteomes; UP000029094; Unassembled WGS sequence.
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};
KW   Nucleotide metabolism {ECO:0000256|ARBA:ARBA00023080}.
FT   DOMAIN          2..117
FT                   /note="dUTPase-like"
FT                   /evidence="ECO:0000259|Pfam:PF00692"
SQ   SEQUENCE   118 AA;  12561 MW;  1986D991802BA9FD CRC64;
     MDVVSAEELI LQPGGRHAVA TGFAMAIPQG YEVQVRPRSG LALKHGISLP NTPGTIDADY
     RGELKIILIN LGDVPFPIRR GDRIAQLVVA PVQLASFVEV DRLDDTERGQ GGFGSTGV
//
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