ID K1E9D8_9MICO Unreviewed; 159 AA.
AC K1E9D8;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE RecName: Full=Deoxyuridine 5'-triphosphate nucleotidohydrolase {ECO:0000256|HAMAP-Rule:MF_00116};
DE Short=dUTPase {ECO:0000256|HAMAP-Rule:MF_00116};
DE EC=3.6.1.23 {ECO:0000256|HAMAP-Rule:MF_00116};
DE AltName: Full=dUTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_00116};
GN Name=dut {ECO:0000256|HAMAP-Rule:MF_00116};
GN ORFNames=B277_04317 {ECO:0000313|EMBL:EKA62062.1}, CWN80_08405
GN {ECO:0000313|EMBL:RWU83750.1};
OS Janibacter hoylei PVAS-1.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Janibacter.
OX NCBI_TaxID=1210046 {ECO:0000313|EMBL:EKA62062.1, ECO:0000313|Proteomes:UP000004474};
RN [1] {ECO:0000313|EMBL:RWU83750.1, ECO:0000313|Proteomes:UP000288711}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PVAS-1 {ECO:0000313|EMBL:RWU83750.1,
RC ECO:0000313|Proteomes:UP000288711};
RX PubMed=19643890; DOI=10.1099/ijs.0.002527-0;
RA Shivaji S., Chaturvedi P., Begum Z., Pindi P.K., Manorama R.,
RA Padmanaban D.A., Shouche Y.S., Pawar S., Vaishampayan P., Dutt C.B.,
RA Datta G.N., Manchanda R.K., Rao U.R., Bhargava P.M., Narlikar J.V.;
RT "Janibacter hoylei sp. nov., Bacillus isronensis sp. nov. and Bacillus
RT aryabhattai sp. nov., isolated from cryotubes used for collecting air from
RT the upper atmosphere.";
RL Int. J. Syst. Evol. Microbiol. 59:2977-2986(2009).
RN [2] {ECO:0000313|EMBL:EKA62062.1, ECO:0000313|Proteomes:UP000004474}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PVAS-1 {ECO:0000313|EMBL:EKA62062.1,
RC ECO:0000313|Proteomes:UP000004474};
RX PubMed=23144385; DOI=10.1128/JB.01728-12;
RA Pawar S.P., Dhotre D.P., Shetty S.A., Chowdhury S.P., Chaudhari B.L.,
RA Shouche Y.S.;
RT "Genome Sequence of Janibacter hoylei MTCC8307, Isolated from the
RT Stratospheric Air.";
RL J. Bacteriol. 194:6629-6630(2012).
RN [3] {ECO:0000313|EMBL:RWU83750.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PVAS-1 {ECO:0000313|EMBL:RWU83750.1};
RA Seuylemezian A., Cooper K., Vaishampayan P.;
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: This enzyme is involved in nucleotide metabolism: it produces
CC dUMP, the immediate precursor of thymidine nucleotides and it decreases
CC the intracellular concentration of dUTP so that uracil cannot be
CC incorporated into DNA. {ECO:0000256|HAMAP-Rule:MF_00116}.
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, ECO:0000256|HAMAP-
CC Rule:MF_00116};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00116};
CC -!- PATHWAY: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP
CC route): step 2/2. {ECO:0000256|HAMAP-Rule:MF_00116}.
CC -!- SIMILARITY: Belongs to the dUTPase family.
CC {ECO:0000256|ARBA:ARBA00006581, ECO:0000256|HAMAP-Rule:MF_00116}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00116}.
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:EKA62062.1}.
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DR EMBL; ALWX01000015; EKA62062.1; -; Genomic_DNA.
DR EMBL; PIPF01000007; RWU83750.1; -; Genomic_DNA.
DR RefSeq; WP_007925472.1; NZ_PIPF01000007.1.
DR AlphaFoldDB; K1E9D8; -.
DR STRING; 1210046.B277_04317; -.
DR eggNOG; COG0756; Bacteria.
DR OrthoDB; 9809956at2; -.
DR UniPathway; UPA00610; UER00666.
DR Proteomes; UP000004474; Unassembled WGS sequence.
DR Proteomes; UP000288711; Unassembled WGS sequence.
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:0046081; P:dUTP catabolic 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; IPR008181; dUTPase.
DR InterPro; IPR029054; dUTPase-like.
DR InterPro; IPR036157; dUTPase-like_sf.
DR InterPro; IPR033704; dUTPase_trimeric.
DR NCBIfam; TIGR00576; dut; 1.
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, ECO:0000256|HAMAP-Rule:MF_00116};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00116};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00116};
KW Nucleotide metabolism {ECO:0000256|ARBA:ARBA00023080, ECO:0000256|HAMAP-
KW Rule:MF_00116}.
FT DOMAIN 18..148
FT /note="dUTPase-like"
FT /evidence="ECO:0000259|Pfam:PF00692"
FT REGION 127..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 68..70
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00116"
FT BINDING 81
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00116"
FT BINDING 85..87
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00116"
SQ SEQUENCE 159 AA; 16372 MW; A6175833325B565A CRC64;
MADARQIAVP VQLLHRDAVV PAYAKHGDAG ADLASVAELT LAPGERHLVP TGVAMAIPHG
WVGLVHPRSG LAARHGISVV NAPGTVDSGY RGEVLVNLVN LDPTDSFTVH VGDRIAQLVL
QEVGEGSFEP VDSLPPSQRG ETGHGSSGGF GPPSTTGRE
//
