(data stored in ACNUC7421 zone)

SWISSPROT: B4STE7_STRM5

ID   B4STE7_STRM5            Unreviewed;       157 AA.
AC   B4STE7;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   08-MAY-2019, entry version 81.
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=Smal_0285 {ECO:0000313|EMBL:ACF49990.1};
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas;
OC   Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008 {ECO:0000313|EMBL:ACF49990.1, ECO:0000313|Proteomes:UP000001867};
RN   [1] {ECO:0000313|EMBL:ACF49990.1, ECO:0000313|Proteomes:UP000001867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3 {ECO:0000313|EMBL:ACF49990.1,
RC   ECO:0000313|Proteomes:UP000001867};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L.,
RA   Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Taghavi S., Monchy S., Newman L., Vangronsveld J.,
RA   van der Lelie D., Richardson P.;
RT   "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL   Submitted (JUN-2008) 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: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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00116}.
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DR   EMBL; CP001111; ACF49990.1; -; Genomic_DNA.
DR   RefSeq; WP_006387785.1; NC_011071.1.
DR   STRING; 391008.Smal_0285; -.
DR   EnsemblBacteria; ACF49990; ACF49990; Smal_0285.
DR   KEGG; smt:Smal_0285; -.
DR   eggNOG; ENOG4108Z1K; Bacteria.
DR   eggNOG; COG0756; LUCA.
DR   HOGENOM; HOG000028968; -.
DR   KO; K01520; -.
DR   OMA; GVILINH; -.
DR   OrthoDB; 1669228at2; -.
DR   BioCyc; SMAL391008:SMAL_RS01445-MONOMER; -.
DR   UniPathway; UPA00610; UER00666.
DR   Proteomes; UP000001867; 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; B4STE7.
DR   SWISS-2DPAGE; B4STE7.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001867};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00116,
KW   ECO:0000256|SAAS:SAAS01176051, ECO:0000313|EMBL:ACF49990.1};
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}.
FT   DOMAIN       22    155       dUTPase. {ECO:0000259|Pfam:PF00692}.
FT   REGION       76     78       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00116}.
FT   REGION       93     95       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00116}.
FT   BINDING      89     89       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00116}.
SQ   SEQUENCE   157 AA;  16481 MW;  52F77F71A05DDF2A CRC64;
     MTQASTSQPL QVKLLDPRFG DSWPLPAYAT AASAGMDLRA ALDTALTLQP GDTALVPSGL
     AIHIADPHLC AVILPRSGLG HRHGIVLGNG TGLIDADYQG PLLISVWNRG REAFTIEPGD
     RIAQLVVVPI ARVNLQVVDT FTDSVRGTGG FGHTGVR
//

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