ID A6LGR6_PARD8 Unreviewed; 144 AA.
AC A6LGR6;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 112.
DE RecName: Full=Deoxyuridine 5'-triphosphate nucleotidohydrolase {ECO:0000256|HAMAP-Rule:MF_00116};
DE Short=dUTPase {ECO:0000256|HAMAP-Rule:MF_00116};
DE EC=3.6.1.23 {ECO:0000256|HAMAP-Rule:MF_00116};
DE AltName: Full=dUTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_00116};
GN Name=dut {ECO:0000256|HAMAP-Rule:MF_00116};
GN OrderedLocusNames=BDI_3174 {ECO:0000313|EMBL:ABR44880.1};
OS Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 / JCM
OS 5825 / NCTC 11152).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC Parabacteroides.
OX NCBI_TaxID=435591 {ECO:0000313|EMBL:ABR44880.1, ECO:0000313|Proteomes:UP000000566};
RN [1] {ECO:0000313|EMBL:ABR44880.1, ECO:0000313|Proteomes:UP000000566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152
RC {ECO:0000313|Proteomes:UP000000566};
RX PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C.,
RA Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H.,
RA Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K.,
RA Knight R.D., Gordon J.I.;
RT "Evolution of symbiotic bacteria in the distal human intestine.";
RL PLoS Biol. 5:1574-1586(2007).
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:0000256|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:0000256|ARBA:ARBA00000878, ECO:0000256|HAMAP-
CC Rule:MF_00116};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00116};
CC -!- PATHWAY: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP
CC route): step 2/2. {ECO:0000256|HAMAP-Rule:MF_00116}.
CC -!- SIMILARITY: Belongs to the dUTPase family.
CC {ECO:0000256|ARBA:ARBA00006581, ECO:0000256|HAMAP-Rule:MF_00116}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00116}.
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DR EMBL; CP000140; ABR44880.1; -; Genomic_DNA.
DR RefSeq; WP_005860037.1; NZ_LR215978.1.
DR AlphaFoldDB; A6LGR6; -.
DR STRING; 435591.BDI_3174; -.
DR PaxDb; 435591-BDI_3174; -.
DR GeneID; 57236174; -.
DR KEGG; pdi:BDI_3174; -.
DR eggNOG; COG0756; Bacteria.
DR HOGENOM; CLU_068508_1_2_10; -.
DR BioCyc; PDIS435591:G1G5A-3254-MONOMER; -.
DR UniPathway; UPA00610; UER00666.
DR Proteomes; UP000000566; 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 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:0000256|HAMAP-Rule:MF_00116};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00116};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00116};
KW Nucleotide metabolism {ECO:0000256|ARBA:ARBA00023080, ECO:0000256|HAMAP-
KW Rule:MF_00116}; Reference proteome {ECO:0000313|Proteomes:UP000000566}.
FT DOMAIN 12..142
FT /note="dUTPase-like"
FT /evidence="ECO:0000259|Pfam:PF00692"
FT BINDING 63..65
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00116"
FT BINDING 76
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00116"
FT BINDING 80..82
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00116"
SQ SEQUENCE 144 AA; 15682 MW; 12FB89F347F71354 CRC64;
MKVRIINKSH HPLPGYATPL SAGMDIRANL SESVVLKPLE RKLIPTGLYI SLPEGYEAQM
RPRSGLALKH GITLLNTPGT IDADYRGEIG IILVNLSSEP FTVNDGERIC QMVIAAHSHV
DWEPVETLDD TERGAGGFGH TGKE
//
