ID DCDB_HALSA Reviewed; 195 AA. AC Q9HSG3; DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 27-MAR-2024, entry version 124. DE RecName: Full=dCTP deaminase, dUMP-forming {ECO:0000255|HAMAP-Rule:MF_00146}; DE EC=3.5.4.30 {ECO:0000255|HAMAP-Rule:MF_00146}; DE AltName: Full=Bifunctional dCTP deaminase:dUTPase {ECO:0000255|HAMAP-Rule:MF_00146}; DE AltName: Full=DCD-DUT {ECO:0000255|HAMAP-Rule:MF_00146}; GN Name=dcd {ECO:0000255|HAMAP-Rule:MF_00146}; Synonyms=dtd; GN OrderedLocusNames=VNG_0245G; OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1) OS (Halobacterium halobium). OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales; OC Halobacteriaceae; Halobacterium; Halobacterium salinarum NRC-34001. OX NCBI_TaxID=64091; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1; RX PubMed=11016950; DOI=10.1073/pnas.190337797; RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D., RA Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D., RA Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R., RA Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P., RA Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M., RA Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J., RA Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L., RA DasSarma S.; RT "Genome sequence of Halobacterium species NRC-1."; RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000). CC -!- FUNCTION: Bifunctional enzyme that catalyzes both the deamination of CC dCTP to dUTP and the hydrolysis of dUTP to dUMP without releasing the CC toxic dUTP intermediate. {ECO:0000255|HAMAP-Rule:MF_00146}. CC -!- CATALYTIC ACTIVITY: CC Reaction=dCTP + 2 H2O = diphosphate + dUMP + NH4(+); CC Xref=Rhea:RHEA:19205, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:61481, ChEBI:CHEBI:246422; CC EC=3.5.4.30; Evidence={ECO:0000255|HAMAP-Rule:MF_00146}; CC -!- PATHWAY: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP: step CC 1/1. {ECO:0000255|HAMAP-Rule:MF_00146}. CC -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_00146}. CC -!- SIMILARITY: Belongs to the dCTP deaminase family. {ECO:0000255|HAMAP- CC Rule:MF_00146}. 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; AE004437; AAG18843.1; -; Genomic_DNA. DR PIR; G84184; G84184. DR RefSeq; WP_010902137.1; NC_002607.1. DR AlphaFoldDB; Q9HSG3; -. DR SMR; Q9HSG3; -. DR STRING; 64091.VNG_0245G; -. DR PaxDb; 64091-VNG_0245G; -. DR GeneID; 68693209; -. DR KEGG; hal:VNG_0245G; -. DR PATRIC; fig|64091.14.peg.178; -. DR HOGENOM; CLU_087476_2_1_2; -. DR InParanoid; Q9HSG3; -. DR OrthoDB; 33242at2157; -. DR PhylomeDB; Q9HSG3; -. DR UniPathway; UPA00610; UER00667. DR Proteomes; UP000000554; Chromosome. DR GO; GO:0033973; F:dCTP deaminase (dUMP-forming) activity; IEA:UniProtKB-UniRule. DR GO; GO:0008829; F:dCTP deaminase activity; IBA:GO_Central. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0006226; P:dUMP biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0006229; P:dUTP biosynthetic process; IEA:InterPro. DR GO; GO:0015949; P:nucleobase-containing small molecule interconversion; IBA:GO_Central. DR CDD; cd07557; trimeric_dUTPase; 1. DR Gene3D; 2.70.40.10; -; 1. DR HAMAP; MF_00146; dCTP_deaminase; 1. DR InterPro; IPR010550; dCTP_deam_bac. DR InterPro; IPR011962; dCTP_deaminase. DR InterPro; IPR036157; dUTPase-like_sf. DR InterPro; IPR033704; dUTPase_trimeric. DR NCBIfam; TIGR02274; dCTP_deam; 1. DR PANTHER; PTHR42680; DCTP DEAMINASE; 1. DR PANTHER; PTHR42680:SF3; DCTP DEAMINASE; 1. DR Pfam; PF06559; DCD; 1. DR SUPFAM; SSF51283; dUTPase-like; 1. PE 3: Inferred from homology; KW Hydrolase; Nucleotide metabolism; Nucleotide-binding; Reference proteome. FT CHAIN 1..195 FT /note="dCTP deaminase, dUMP-forming" FT /id="PRO_0000156028" FT REGION 161..195 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 133 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146" FT BINDING 105..110 FT /ligand="dCTP" FT /ligand_id="ChEBI:CHEBI:61481" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146" FT BINDING 123 FT /ligand="dCTP" FT /ligand_id="ChEBI:CHEBI:61481" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146" FT BINDING 131..133 FT /ligand="dCTP" FT /ligand_id="ChEBI:CHEBI:61481" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146" FT BINDING 152 FT /ligand="dCTP" FT /ligand_id="ChEBI:CHEBI:61481" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146" FT BINDING 166 FT /ligand="dCTP" FT /ligand_id="ChEBI:CHEBI:61481" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146" FT BINDING 173 FT /ligand="dCTP" FT /ligand_id="ChEBI:CHEBI:61481" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146" FT BINDING 177 FT /ligand="dCTP" FT /ligand_id="ChEBI:CHEBI:61481" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146" FT SITE 120..121 FT /note="Important for bifunctional activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146" SQ SEQUENCE 195 AA; 21542 MW; 86CCDA4D48BC0C9D CRC64; MILSDQDILA RLADGDLAIE PLEDVDLQVQ PASVDVRLGR RFLEFERANV PCIHPNREDE VDEYVTETVV EDGDEFILHP GDFVLGTTKE RVEVPRDLVA QVEGRSSLGR LAVVVHATAG FIDPGFNGRV TLELSNLGKV PVALTPEMRI SQLVFTELTS PADRPYGDER GSKYQDQDGP QASRIRGDRE FGGTQ //