(data stored in ACNUC7421 zone)

SWISSPROT: DUT_RHOPS

ID   DUT_RHOPS               Reviewed;         152 AA.
AC   Q13EP1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 80.
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};
GN   OrderedLocusNames=RPD_0208;
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA   Lykidis A., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This enzyme is involved in nucleotide metabolism: it
CC       produces dUMP, the immediate precursor of thymidine nucleotides
CC       and it decreases the intracellular concentration of dUTP so that
CC       uracil cannot be incorporated into DNA. {ECO:0000255|HAMAP-
CC       Rule:MF_00116}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dUTP + H2O = diphosphate + dUMP + H(+);
CC         Xref=Rhea:RHEA:10248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:61555, ChEBI:CHEBI:246422;
CC         EC=3.6.1.23; 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
CC       (dUTP route): step 2/2. {ECO:0000255|HAMAP-Rule:MF_00116}.
CC   -!- SIMILARITY: Belongs to the dUTPase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00116}.
DR   EMBL; CP000283; ABE37448.1; -; Genomic_DNA.
DR   RefSeq; WP_011500640.1; NC_007958.1.
DR   SMR; Q13EP1; -.
DR   STRING; 316057.RPD_0208; -.
DR   EnsemblBacteria; ABE37448; ABE37448; RPD_0208.
DR   KEGG; rpd:RPD_0208; -.
DR   eggNOG; ENOG4108Z1K; Bacteria.
DR   eggNOG; COG0756; LUCA.
DR   HOGENOM; HOG000028966; -.
DR   KO; K01520; -.
DR   OMA; GVILINH; -.
DR   OrthoDB; 1669228at2; -.
DR   BioCyc; RPAL316057:RPD_RS01055-MONOMER; -.
DR   UniPathway; UPA00610; UER00666.
DR   Proteomes; UP000001818; 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:0046080; P:dUTP metabolic 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; IPR029054; dUTPase-like.
DR   InterPro; IPR036157; dUTPase-like_sf.
DR   InterPro; IPR008181; dUTPase_1.
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   3: Inferred from homology;
DR   PRODOM; Q13EP1.
DR   SWISS-2DPAGE; Q13EP1.
KW   Complete proteome; Hydrolase; Magnesium; Metal-binding;
KW   Nucleotide metabolism.
FT   CHAIN         1    152       Deoxyuridine 5'-triphosphate
FT                                nucleotidohydrolase.
FT                                /FTId=PRO_1000015505.
FT   REGION       72     74       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00116}.
FT   REGION       89     91       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00116}.
FT   BINDING      85     85       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00116}.
SQ   SEQUENCE   152 AA;  15729 MW;  8A37F2A2E903DFE4 CRC64;
     MSDTIAVEIK QLPHAEGLPL PAYQSAHAAG LDLCAANSAD APLLLAPGSY VLVPTGLTIA
     LPENYEAQVR PRSGLAAKHG VTVLNAPGTI DADYRGEIGV LLINHGDAPF TIRRGERIAQ
     MVIAPVVRAE LIGVETLSET ARGVGGFGST GR
//

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