ID V2PX13_9BACT Unreviewed; 144 AA.
AC V2PX13;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
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:USF23020.1};
GN ORFNames=N508_000073 {ECO:0000313|EMBL:USF23020.1}, N508_01934
GN {ECO:0000313|EMBL:ESJ97132.1};
OS Mucispirillum schaedleri ASF457.
OC Bacteria; Deferribacterota; Deferribacteres; Deferribacterales;
OC Mucispirillaceae; Mucispirillum.
OX NCBI_TaxID=1379858 {ECO:0000313|EMBL:ESJ97132.1};
RN [1] {ECO:0000313|EMBL:ESJ97132.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ASF457 {ECO:0000313|EMBL:ESJ97132.1};
RX PubMed=24723722;
RA Wannemuehler M.J., Overstreet A.M., Ward D.V., Phillips G.J.;
RT "Draft genome sequences of the altered schaedler flora, a defined bacterial
RT community from gnotobiotic mice.";
RL Genome Announc. 2:e00287-e00214(2014).
RN [2] {ECO:0000313|EMBL:USF23020.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ASF457 {ECO:0000313|EMBL:USF23020.1};
RA Proctor A.L., Phillips G.J., Wannemuehler M.J.;
RL Submitted (MAY-2022) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:USF23020.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ASF457 {ECO:0000313|EMBL:USF23020.1};
RA Proctor A., Parvinroo S., Richie T., Jia X., Lee S.T.M., Karp P.D.,
RA Paley S., Kostic A.D., Pierre J.F., Wannemuehler M.J., Phillips G.J.;
RT "Resources to Facilitate Use of the Altered Schaedler Flora (ASF) Mouse
RT Model to Study Microbiome Function.";
RL Submitted (JUN-2022) to the EMBL/GenBank/DDBJ databases.
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; AYGZ01000022; ESJ97132.1; -; Genomic_DNA.
DR EMBL; CP097562; USF23020.1; -; Genomic_DNA.
DR RefSeq; WP_023276735.1; NZ_FTRD01000034.1.
DR AlphaFoldDB; V2PX13; -.
DR STRING; 1379858.N508_01934; -.
DR GeneID; 78586812; -.
DR PATRIC; fig|1379858.3.peg.1929; -.
DR eggNOG; COG0756; Bacteria.
DR HOGENOM; CLU_068508_1_2_0; -.
DR OrthoDB; 9809956at2; -.
DR UniPathway; UPA00610; UER00666.
DR Proteomes; UP000017429; 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:UP000017429}.
FT DOMAIN 16..143
FT /note="dUTPase-like"
FT /evidence="ECO:0000259|Pfam:PF00692"
FT BINDING 64..66
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00116"
FT BINDING 77
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00116"
FT BINDING 81..83
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00116"
SQ SEQUENCE 144 AA; 15569 MW; A27A8042FD3AB4B9 CRC64;
MDIININIIA EEDCLIPSYE TAGASGADLK SKEDGILKSG ERRLVKTGVF IELPAGYEAQ
VRPRSGLALK HGITMLNSPG TIDSDYRGEI GVIMINHGSE PFVYKKGDRI AQLVISKYSR
VEFKNTLSLT ETVRGAGGFG HTGK
//
