(data stored in SCRATCH zone)

SWISSPROT: C5B9D2_EDWI9

ID   C5B9D2_EDWI9            Unreviewed;       152 AA.
AC   C5B9D2;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   08-MAY-2019, entry version 73.
DE   RecName: Full=Deoxyuridine 5'-triphosphate nucleotidohydrolase {ECO:0000256|HAMAP-Rule:MF_00116, ECO:0000256|SAAS:SAAS01176036};
DE            Short=dUTPase {ECO:0000256|HAMAP-Rule:MF_00116};
DE            EC=3.6.1.23 {ECO:0000256|HAMAP-Rule:MF_00116, ECO:0000256|SAAS:SAAS01176044};
DE   AltName: Full=dUTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_00116};
GN   Name=dut {ECO:0000256|HAMAP-Rule:MF_00116};
GN   OrderedLocusNames=NT01EI_0052 {ECO:0000313|EMBL:ACR67312.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67312.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACR67312.1, ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|EMBL:ACR67312.1,
RC   ECO:0000313|Proteomes:UP000001485};
RX   PubMed=22247535; DOI=10.1128/JB.06522-11;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Banes M.M.,
RA   Lawrence M.L.;
RT   "Genome Sequence of Edwardsiella ictaluri 93-146, a Strain Associated
RT   with a Natural Channel Catfish Outbreak of Enteric Septicemia of
RT   Catfish.";
RL   J. Bacteriol. 194:740-741(2012).
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:0000256|HAMAP-
CC       Rule:MF_00116, ECO:0000256|SAAS:SAAS01176047}.
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:0000256|HAMAP-Rule:MF_00116,
CC         ECO:0000256|SAAS:SAAS01176050};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00116, ECO:0000256|SAAS:SAAS01176048};
CC   -!- PATHWAY: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP
CC       (dUTP route): step 2/2. {ECO:0000256|HAMAP-Rule:MF_00116}.
CC   -!- SIMILARITY: Belongs to the dUTPase family. {ECO:0000256|HAMAP-
CC       Rule:MF_00116, ECO:0000256|SAAS:SAAS01176039}.
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DR   EMBL; CP001600; ACR67312.1; -; Genomic_DNA.
DR   RefSeq; WP_015869536.1; NC_012779.2.
DR   EnsemblBacteria; ACR67312; ACR67312; NT01EI_0052.
DR   GeneID; 7959771; -.
DR   KEGG; eic:NT01EI_0052; -.
DR   PATRIC; fig|634503.3.peg.45; -.
DR   eggNOG; ENOG4108Z1K; Bacteria.
DR   eggNOG; COG0756; LUCA.
DR   HOGENOM; HOG000028968; -.
DR   KO; K01520; -.
DR   OMA; GVILINH; -.
DR   OrthoDB; 1669228at2; -.
DR   BioCyc; EICT634503:G1GVC-45-MONOMER; -.
DR   UniPathway; UPA00610; UER00666.
DR   Proteomes; UP000001485; 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; C5B9D2.
DR   SWISS-2DPAGE; C5B9D2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00116,
KW   ECO:0000256|SAAS:SAAS01176051, ECO:0000313|EMBL:ACR67312.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00116,
KW   ECO:0000256|SAAS:SAAS01176034};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00116,
KW   ECO:0000256|SAAS:SAAS01176043};
KW   Nucleotide metabolism {ECO:0000256|HAMAP-Rule:MF_00116,
KW   ECO:0000256|SAAS:SAAS01176045};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485}.
FT   DOMAIN       17    150       dUTPase. {ECO:0000259|Pfam:PF00692}.
FT   REGION       71     73       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00116}.
FT   REGION       88     90       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00116}.
FT   BINDING      84     84       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00116}.
FT   BINDING      98     98       Substrate; via amide nitrogen and
FT                                carbonyl oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00116}.
SQ   SEQUENCE   152 AA;  16057 MW;  3C5E811FA4E18D08 CRC64;
     MKKKIDVKIL DARIGQQFPL PTYATPGSAG LDLRACLDSA VVLAPGETTL LPTGLAIHIA
     DPSLAAVILP RSGLGHKHGI VLGNLVGLID SDYQGQLMIS AWNRGQTPFT IEPGERIAQL
     VLVPVVQADF NLVESFEDSA RGDGGFGHSG RH
//

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