ID B9DJC8_STACT Unreviewed; 169 AA.
AC B9DJC8;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=dUTP diphosphatase {ECO:0000256|ARBA:ARBA00012379};
DE EC=3.6.1.23 {ECO:0000256|ARBA:ARBA00012379};
GN Name=dut {ECO:0000313|EMBL:CAL27400.1};
GN OrderedLocusNames=Sca_0486 {ECO:0000313|EMBL:CAL27400.1};
OS Staphylococcus carnosus (strain TM300).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=396513 {ECO:0000313|EMBL:CAL27400.1, ECO:0000313|Proteomes:UP000000444};
RN [1] {ECO:0000313|EMBL:CAL27400.1, ECO:0000313|Proteomes:UP000000444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TM300 {ECO:0000313|EMBL:CAL27400.1,
RC ECO:0000313|Proteomes:UP000000444};
RX PubMed=19060169; DOI=10.1128/AEM.01982-08;
RA Rosenstein R., Nerz C., Biswas L., Resch A., Raddatz G., Schuster S.C.,
RA Goetz F.;
RT "Genome analysis of the meat starter culture bacterium Staphylococcus
RT carnosus TM300.";
RL Appl. Environ. Microbiol. 75:811-822(2009).
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};
CC -!- SIMILARITY: Belongs to the dUTPase family.
CC {ECO:0000256|ARBA:ARBA00006581}.
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DR EMBL; AM295250; CAL27400.1; -; Genomic_DNA.
DR RefSeq; WP_015899744.1; NC_012121.1.
DR AlphaFoldDB; B9DJC8; -.
DR GeneID; 60545815; -.
DR KEGG; sca:SCA_0486; -.
DR eggNOG; COG0756; Bacteria.
DR HOGENOM; CLU_068508_4_0_9; -.
DR OrthoDB; 9809956at2; -.
DR BioCyc; SCAR396513:SCA_RS02485-MONOMER; -.
DR Proteomes; UP000000444; Chromosome.
DR GO; GO:0004170; F:dUTP diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0006226; P:dUMP biosynthetic process; IEA:InterPro.
DR GO; GO:0046081; P:dUTP catabolic process; IEA:InterPro.
DR CDD; cd07557; trimeric_dUTPase; 1.
DR Gene3D; 2.70.40.10; -; 1.
DR InterPro; IPR008181; dUTPase.
DR InterPro; IPR029054; dUTPase-like.
DR InterPro; IPR036157; dUTPase-like_sf.
DR InterPro; IPR033704; dUTPase_trimeric.
DR PANTHER; PTHR11241; DEOXYURIDINE 5'-TRIPHOSPHATE NUCLEOTIDOHYDROLASE; 1.
DR PANTHER; PTHR11241:SF0; DEOXYURIDINE 5'-TRIPHOSPHATE NUCLEOTIDOHYDROLASE; 1.
DR Pfam; PF00692; dUTPase; 2.
DR SUPFAM; SSF51283; dUTPase-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CAL27400.1};
KW Nucleotide metabolism {ECO:0000256|ARBA:ARBA00023080}.
FT DOMAIN 12..97
FT /note="dUTPase-like"
FT /evidence="ECO:0000259|Pfam:PF00692"
FT DOMAIN 123..167
FT /note="dUTPase-like"
FT /evidence="ECO:0000259|Pfam:PF00692"
SQ SEQUENCE 169 AA; 18698 MW; 3C23B783CE1B1A36 CRC64;
MTNLQIKLLS DNATMPTRAN ATDAGYDIYA AETVILEPQE KALIATDIAV NIPKGYVGLL
TSRSGVSSKT HLVVETGKID AGYQGHMKIN IKNDSQEFDT EEDAYFNIQN KFEHGYVSKF
VNTNYTIHKG DRLAQLVIVP IWKPELEPVK EFSNETARGE KGFGSSGTR
//
