ID A0A0R1XHU8_9LACO Unreviewed; 171 AA.
AC A0A0R1XHU8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=dUTP diphosphatase {ECO:0000256|ARBA:ARBA00012379};
DE EC=3.6.1.23 {ECO:0000256|ARBA:ARBA00012379};
GN ORFNames=FD32_GL001394 {ECO:0000313|EMBL:KRM29634.1};
OS Limosilactobacillus panis DSM 6035.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Limosilactobacillus.
OX NCBI_TaxID=1423782 {ECO:0000313|EMBL:KRM29634.1, ECO:0000313|Proteomes:UP000051412};
RN [1] {ECO:0000313|EMBL:KRM29634.1, ECO:0000313|Proteomes:UP000051412}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6035 {ECO:0000313|EMBL:KRM29634.1,
RC ECO:0000313|Proteomes:UP000051412};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRM29634.1}.
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DR EMBL; AZGM01000022; KRM29634.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R1XHU8; -.
DR STRING; 1423782.FD32_GL001394; -.
DR PATRIC; fig|1423782.4.peg.1452; -.
DR Proteomes; UP000051412; Unassembled WGS sequence.
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; 1.
DR SUPFAM; SSF51283; dUTPase-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide metabolism {ECO:0000256|ARBA:ARBA00023080};
KW Reference proteome {ECO:0000313|Proteomes:UP000051412}.
FT DOMAIN 67..169
FT /note="dUTPase-like"
FT /evidence="ECO:0000259|Pfam:PF00692"
SQ SEQUENCE 171 AA; 19017 MW; 6BBE1B0349AABA82 CRC64;
MSKKANDGLS LPKRQTAKAA GYDFAASEDF TLPSIWKGNF LKALWALFKQ KKVSDEDFQS
ADACLKPYLV PTGVKAYMQD NEFLLLANRS SGPLKRRLIL PNGIGIVDAD YYDNDSNEGE
IFFQLINFGL RDYHIKKGER IGQGIFMPFL LADGETAPHA QRTGGFGSTK K
//
