DUT_LEGPH
ID DUT_LEGPH Reviewed; 152 AA.
AC Q5ZSN0;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 103.
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=lpg2487;
OS Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC
OS 33152 / DSM 7513).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=272624;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
RX PubMed=15448271; DOI=10.1126/science.1099776;
RA Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G.,
RA Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V.,
RA Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S., Georghiou A.,
RA Chou I.-C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A.,
RA Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A.,
RA Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A.,
RA Russo J.J.;
RT "The genomic sequence of the accidental pathogen Legionella pneumophila.";
RL Science 305:1966-1968(2004).
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 = 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:0000255|HAMAP-Rule:MF_00116};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-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=AAU28547.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE017354; AAU28547.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_014842515.1; NC_002942.5.
DR RefSeq; YP_096494.1; NC_002942.5.
DR PDB; 6MAI; X-ray; 1.80 A; A=1-152.
DR PDB; 6MAO; X-ray; 1.95 A; A=1-152.
DR PDBsum; 6MAI; -.
DR PDBsum; 6MAO; -.
DR AlphaFoldDB; Q5ZSN0; -.
DR SMR; Q5ZSN0; -.
DR STRING; 272624.lpg2487; -.
DR PaxDb; Q5ZSN0; -.
DR PRIDE; Q5ZSN0; -.
DR EnsemblBacteria; AAU28547; AAU28547; lpg2487.
DR KEGG; lpn:lpg2487; -.
DR PATRIC; fig|272624.6.peg.2636; -.
DR eggNOG; COG0756; Bacteria.
DR HOGENOM; CLU_068508_1_1_6; -.
DR UniPathway; UPA00610; UER00666.
DR Proteomes; UP000000609; 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 PANTHER; PTHR11241; PTHR11241; 1.
DR Pfam; PF00692; dUTPase; 1.
DR SUPFAM; SSF51283; SSF51283; 1.
DR TIGRFAMs; TIGR00576; dut; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism;
KW Reference proteome.
FT CHAIN 1..152
FT /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase"
FT /id="PRO_0000182874"
FT BINDING 71..73
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00116"
FT BINDING 84
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00116"
FT BINDING 88..90
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00116"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00116"
FT STRAND 6..9
FT /evidence="ECO:0007829|PDB:6MAI"
FT TURN 15..17
FT /evidence="ECO:0007829|PDB:6MAI"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:6MAI"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:6MAI"
FT STRAND 48..58
FT /evidence="ECO:0007829|PDB:6MAI"
FT STRAND 64..70
FT /evidence="ECO:0007829|PDB:6MAI"
FT HELIX 72..78
FT /evidence="ECO:0007829|PDB:6MAI"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:6MAI"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:6MAI"
FT STRAND 95..103
FT /evidence="ECO:0007829|PDB:6MAI"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:6MAI"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:6MAI"
FT STRAND 116..124
FT /evidence="ECO:0007829|PDB:6MAI"
SQ SEQUENCE 152 AA; 16347 MW; 37E05FB3A74BAE5D CRC64;
MHQVIQLKIL DSRIGDTIPL PAYATDGSAG LDLRVCISEP MQVAPQQTVL LPTGIAIYIA
DPKLAAVILP RSGLGHKNGI VLGNLVGLID SDYQGELKIS CWNRSQEHFT VNPGDRIAQL
VFIPVVQASF EVVNEFTESS RGEGGFGSSG RY
