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Database: UniProt
Entry: A0A023D5G7_ACIMT
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ID   A0A023D5G7_ACIMT        Unreviewed;       163 AA.
AC   A0A023D5G7;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 49.
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   ORFNames=Amme_060_039 {ECO:0000313|EMBL:GAJ29403.1};
OS   Acidomonas methanolica NBRC 104435.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acidomonas.
OX   NCBI_TaxID=1231351 {ECO:0000313|EMBL:GAJ29403.1, ECO:0000313|Proteomes:UP000019760};
RN   [1] {ECO:0000313|Proteomes:UP000019760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MB58 {ECO:0000313|Proteomes:UP000019760};
RX   PubMed=24330138; DOI=10.1111/1574-6968.12357;
RA   Higashiura N., Hadano H., Hirakawa H., Matsutani M., Takabe S.,
RA   Matsushita K., Azuma Y.;
RT   "Draft Genomic DNA Sequence of the Facultatively Methylotrophic Bacterium
RT   Acidomonas methanolica type strain MB58.";
RL   FEMS Microbiol. Lett. 351:9-13(2014).
RN   [2] {ECO:0000313|EMBL:GAJ29403.1, ECO:0000313|Proteomes:UP000019760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MB58 {ECO:0000313|EMBL:GAJ29403.1,
RC   ECO:0000313|Proteomes:UP000019760};
RA   Higashiura N., Hadano H., Hirakawa H., Matsutani M., Takabe S.,
RA   Matsushita K., Azuma Y.;
RT   "Draft genomic DNA sequence of the facultatively methylotrophic bacterium
RT   Acidomonas methanolica type strain MB58.";
RL   FEMS Microbiol. Lett. 351:9-13(2014).
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}.
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:GAJ29403.1}.
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DR   EMBL; BAND01000060; GAJ29403.1; -; Genomic_DNA.
DR   RefSeq; WP_042059213.1; NZ_BJVB01000001.1.
DR   AlphaFoldDB; A0A023D5G7; -.
DR   OrthoDB; 9809956at2; -.
DR   UniPathway; UPA00610; UER00666.
DR   Proteomes; UP000019760; Unassembled WGS sequence.
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:UP000019760}.
FT   DOMAIN          25..154
FT                   /note="dUTPase-like"
FT                   /evidence="ECO:0000259|Pfam:PF00692"
FT   BINDING         75..77
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00116"
FT   BINDING         88
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00116"
FT   BINDING         92..94
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00116"
SQ   SEQUENCE   163 AA;  17016 MW;  28784A062C37E887 CRC64;
     MTVHDSPDSI PVEVVRLPHA EGLDLPAYAT DGAAGLDLLA AITEDVVLAP GGRALIPTGL
     KLALPQGYEV QVRPRSGLAL RHGIMLPNAP GTIDEDYRGE LGVIVLNGGS DSFTITRGMR
     IAQAVLAPVV RLRWVEVEML DATTRGEGGF GSTGFHRGAS GKG
//
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