ID D3NY72_AZOS1 Unreviewed; 151 AA.
AC D3NY72;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 24-JAN-2024, entry version 80.
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 ECO:0000313|EMBL:BAI73351.1};
GN OrderedLocusNames=AZL_027130 {ECO:0000313|EMBL:BAI73351.1};
OS Azospirillum sp. (strain B510).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=137722 {ECO:0000313|EMBL:BAI73351.1, ECO:0000313|Proteomes:UP000002040};
RN [1] {ECO:0000313|EMBL:BAI73351.1, ECO:0000313|Proteomes:UP000002040}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B510 {ECO:0000313|EMBL:BAI73351.1,
RC ECO:0000313|Proteomes:UP000002040};
RX PubMed=20047946; DOI=10.1093/dnares/dsp026;
RA Kaneko T., Minamisawa K., Isawa T., Nakatsukasa H., Mitsui H.,
RA Kawaharada Y., Nakamura Y., Watanabe A., Kawashima K., Ono A., Shimizu Y.,
RA Takahashi C., Minami C., Fujishiro T., Kohara M., Katoh M., Nakazaki N.,
RA Nakayama S., Yamada M., Tabata S., Sato S.;
RT "Complete genomic structure of the cultivated rice endophyte Azospirillum
RT sp. B510.";
RL DNA Res. 17:37-50(2010).
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; AP010946; BAI73351.1; -; Genomic_DNA.
DR RefSeq; WP_012975267.1; NC_013854.1.
DR AlphaFoldDB; D3NY72; -.
DR STRING; 137722.AZL_027130; -.
DR KEGG; azl:AZL_027130; -.
DR HOGENOM; CLU_068508_1_2_5; -.
DR OrthoDB; 9809956at2; -.
DR UniPathway; UPA00610; UER00666.
DR Proteomes; UP000002040; 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:UP000002040}.
FT DOMAIN 17..149
FT /note="dUTPase-like"
FT /evidence="ECO:0000259|Pfam:PF00692"
FT BINDING 70..72
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00116"
FT BINDING 83
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00116"
FT BINDING 87..89
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00116"
SQ SEQUENCE 151 AA; 15447 MW; FFB7446ACE2C3F4E CRC64;
MSPTVAFLRL PGNDDLPLPA YATEGAAGFD LRAAVPADAP VTLAPGRRVL VPTGFAVGLP
PGWEMQIRPR SGLAVKNGVT VLNTPGTVDC DYRGPVGVCL INLGEEPFTI ARGDRIAQAV
IAQAPQALLV EVATLDDTAR GTGGFGSTGI A
//
