ID DUT_DICDI Reviewed; 179 AA. AC Q54BW5; DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 24-MAY-2005, sequence version 1. DT 27-MAR-2024, entry version 116. DE RecName: Full=Deoxyuridine 5'-triphosphate nucleotidohydrolase, mitochondrial {ECO:0000303|PubMed:31910901}; DE Short=dUTPase {ECO:0000303|PubMed:31910901}; DE EC=3.6.1.23 {ECO:0000269|PubMed:31910901}; DE AltName: Full=dUTP pyrophosphatase {ECO:0000305}; DE Flags: Precursor; GN Name=dut; ORFNames=DDB_G0293374; OS Dictyostelium discoideum (Social amoeba). OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales; OC Dictyosteliaceae; Dictyostelium. OX NCBI_TaxID=44689; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AX4; RX PubMed=15875012; DOI=10.1038/nature03481; RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G., RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.; RT "The genome of the social amoeba Dictyostelium discoideum."; RL Nature 435:43-57(2005). RN [2] {ECO:0007744|PDB:5F9K} RP X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS) OF 38-179 IN COMPLEX WITH SUBSTRATE RP ANALOG DUP, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL RP PROPERTIES, PATHWAY, SUBUNIT, SUBCELLULAR LOCATION, AND CLEAVAGE OF TRANSIT RP PEPTIDE AFTER GLY-41. RX PubMed=31910901; DOI=10.1186/s13104-019-4879-7; RA Chia C.P., Inoguchi N., Varon K.C., Bartholomai B.M., Moriyama H.; RT "Mitochondrial localization of Dictyostelium discoideum dUTPase mediated by RT its N-terminus."; RL BMC Res. Notes 13:16-16(2020). 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:0000269|PubMed:31910901}. 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:0000269|PubMed:31910901}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:31910901}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.5 uM for dUTP {ECO:0000269|PubMed:31910901}; CC Note=kcat is 9.3 sec(-1) with dUTP as substrate. CC {ECO:0000269|PubMed:31910901}; CC pH dependence: CC Optimum pH is 8. {ECO:0000269|PubMed:31910901}; CC Temperature dependence: CC Optimum temperature is 60 degrees Celsius. CC {ECO:0000269|PubMed:31910901}; CC -!- PATHWAY: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP CC route): step 2/2. {ECO:0000269|PubMed:31910901}. CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:31910901}. CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:31910901}. CC -!- SIMILARITY: Belongs to the dUTPase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AAFI02000204; EAL60754.1; -; Genomic_DNA. DR RefSeq; XP_629169.1; XM_629167.1. DR PDB; 5F9K; X-ray; 2.18 A; A/B/C=38-179. DR PDBsum; 5F9K; -. DR AlphaFoldDB; Q54BW5; -. DR SMR; Q54BW5; -. DR STRING; 44689.Q54BW5; -. DR PaxDb; 44689-DDB0230111; -. DR EnsemblProtists; EAL60754; EAL60754; DDB_G0293374. DR GeneID; 8629190; -. DR KEGG; ddi:DDB_G0293374; -. DR dictyBase; DDB_G0293374; dut. DR eggNOG; KOG3370; Eukaryota. DR HOGENOM; CLU_068508_2_1_1; -. DR InParanoid; Q54BW5; -. DR OMA; RSGMGHK; -. DR PhylomeDB; Q54BW5; -. DR Reactome; R-DDI-499943; Interconversion of nucleotide di- and triphosphates. DR UniPathway; UPA00610; UER00666. DR PRO; PR:Q54BW5; -. DR Proteomes; UP000002195; Chromosome 6. DR GO; GO:0005739; C:mitochondrion; IDA:dictyBase. DR GO; GO:0004170; F:dUTP diphosphatase activity; IDA:dictyBase. DR GO; GO:0000287; F:magnesium ion binding; IDA:dictyBase. DR GO; GO:0006226; P:dUMP biosynthetic process; IBA:GO_Central. DR GO; GO:0046081; P:dUTP catabolic process; IBA:GO_Central. DR GO; GO:0009213; P:pyrimidine deoxyribonucleoside triphosphate catabolic process; ISS:dictyBase. DR CDD; cd07557; trimeric_dUTPase; 1. DR DisProt; DP02689; -. 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 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 1: Evidence at protein level; KW 3D-structure; Hydrolase; Magnesium; Metal-binding; Mitochondrion; KW Nucleotide metabolism; Reference proteome; Transit peptide. FT TRANSIT 1..41 FT /note="Mitochondrion" FT /evidence="ECO:0000269|PubMed:31910901" FT CHAIN 42..179 FT /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase, FT mitochondrial" FT /id="PRO_0000327582" FT BINDING 97..99 FT /ligand="dUTP" FT /ligand_id="ChEBI:CHEBI:61555" FT /evidence="ECO:0000305|PubMed:31910901, FT ECO:0007744|PDB:5F9K" FT BINDING 111..114 FT /ligand="dUTP" FT /ligand_id="ChEBI:CHEBI:61555" FT /evidence="ECO:0000305|PubMed:31910901, FT ECO:0007744|PDB:5F9K" FT BINDING 122 FT /ligand="dUTP" FT /ligand_id="ChEBI:CHEBI:61555" FT /evidence="ECO:0000305|PubMed:31910901, FT ECO:0007744|PDB:5F9K" FT BINDING 165 FT /ligand="dUTP" FT /ligand_id="ChEBI:CHEBI:61555" FT /evidence="ECO:0000250|UniProtKB:P33316" FT BINDING 170..171 FT /ligand="dUTP" FT /ligand_id="ChEBI:CHEBI:61555" FT /evidence="ECO:0000250|UniProtKB:P33316" FT STRAND 38..44 FT /evidence="ECO:0007829|PDB:5F9K" FT STRAND 51..54 FT /evidence="ECO:0007829|PDB:5F9K" FT STRAND 58..63 FT /evidence="ECO:0007829|PDB:5F9K" FT STRAND 68..70 FT /evidence="ECO:0007829|PDB:5F9K" FT STRAND 74..79 FT /evidence="ECO:0007829|PDB:5F9K" FT STRAND 82..84 FT /evidence="ECO:0007829|PDB:5F9K" FT STRAND 90..95 FT /evidence="ECO:0007829|PDB:5F9K" FT HELIX 98..104 FT /evidence="ECO:0007829|PDB:5F9K" FT STRAND 106..110 FT /evidence="ECO:0007829|PDB:5F9K" FT STRAND 122..127 FT /evidence="ECO:0007829|PDB:5F9K" FT STRAND 129..131 FT /evidence="ECO:0007829|PDB:5F9K" FT STRAND 133..135 FT /evidence="ECO:0007829|PDB:5F9K" FT STRAND 140..150 FT /evidence="ECO:0007829|PDB:5F9K" SQ SEQUENCE 179 AA; 19532 MW; 46187E1F460A533F CRC64; MPIEQKYFSL FSNLFKRLTT NNNNNNYLKM APPNFETFKV KKLSDKAIIP QRGSKGAAGY DLSSAHELVV PAHGKALAMT DLQIAIPDGT YGRIAPRSGL AWKNFIDCGA GVIDSDYRGN VGVVLFNHSD VDFKVAVGDR VAQLIFERIV TPEPLEVDEI DETQRGAGGF GSTGVKVQN //