ID A0A0F7IDH0_9EURY Unreviewed; 167 AA.
AC A0A0F7IDH0;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Probable deoxyuridine 5'-triphosphate nucleotidohydrolase {ECO:0000256|HAMAP-Rule:MF_00635};
DE Short=dUTPase {ECO:0000256|HAMAP-Rule:MF_00635};
DE EC=3.6.1.23 {ECO:0000256|HAMAP-Rule:MF_00635};
DE AltName: Full=dUTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_00635};
GN Name=dut {ECO:0000256|HAMAP-Rule:MF_00635};
GN ORFNames=GAH_01762 {ECO:0000313|EMBL:AKG90959.1};
OS Geoglobus ahangari.
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Geoglobus.
OX NCBI_TaxID=113653 {ECO:0000313|EMBL:AKG90959.1, ECO:0000313|Proteomes:UP000034723};
RN [1] {ECO:0000313|EMBL:AKG90959.1, ECO:0000313|Proteomes:UP000034723}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=234 {ECO:0000313|EMBL:AKG90959.1,
RC ECO:0000313|Proteomes:UP000034723};
RA Manzella M.P., Holmes D.E., Rocheleau J.M., Chung A., Reguera G.,
RA Kashefi K.;
RT "The complete genome sequence of the hyperthermophilic, obligate iron-
RT reducing archaeon Geoglobus ahangari strain 234T.";
RL Submitted (APR-2015) 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_00635}.
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|HAMAP-Rule:MF_00635};
CC -!- PATHWAY: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP
CC route): step 2/2. {ECO:0000256|HAMAP-Rule:MF_00635}.
CC -!- SIMILARITY: Belongs to the dCTP deaminase family. Archaeal dUTPase
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00635}.
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DR EMBL; CP011267; AKG90959.1; -; Genomic_DNA.
DR RefSeq; WP_048096169.1; NZ_CP011267.1.
DR AlphaFoldDB; A0A0F7IDH0; -.
DR STRING; 113653.GAH_01762; -.
DR GeneID; 24804330; -.
DR KEGG; gah:GAH_01762; -.
DR PATRIC; fig|113653.22.peg.1731; -.
DR HOGENOM; CLU_103451_2_0_2; -.
DR InParanoid; A0A0F7IDH0; -.
DR OrthoDB; 50042at2157; -.
DR UniPathway; UPA00610; UER00666.
DR Proteomes; UP000034723; Chromosome.
DR GO; GO:0004170; F:dUTP diphosphatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006226; P:dUMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd07557; trimeric_dUTPase; 1.
DR Gene3D; 2.70.40.10; -; 1.
DR HAMAP; MF_00635; dUTPase_arch; 1.
DR InterPro; IPR029054; dUTPase-like.
DR InterPro; IPR036157; dUTPase-like_sf.
DR InterPro; IPR023537; dUTPase_archaeal.
DR InterPro; IPR033704; dUTPase_trimeric.
DR PANTHER; PTHR42680; DCTP DEAMINASE; 1.
DR PANTHER; PTHR42680:SF1; 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_00635};
KW Nucleotide metabolism {ECO:0000256|HAMAP-Rule:MF_00635};
KW Reference proteome {ECO:0000313|Proteomes:UP000034723}.
FT DOMAIN 76..153
FT /note="dUTPase-like"
FT /evidence="ECO:0000259|Pfam:PF00692"
SQ SEQUENCE 167 AA; 19190 MW; D92D52039CFDCF8A CRC64;
MGVLSKDEIR RLIESQSLIS DYVDLETQLQ PNGFDCTLRK VARISGEGRL DFDNSERRIP
ETEEMPFENE WVFLEKGYYR AYINEVVRIP NDMMALARPR SSLIRAGANI LTAVWDAGYV
GRSEVGLVVY NEDGLWLKRN ARIVQLVFFR LDGETEGYSG IYRGENV
//
