ID DCD_SULAC Reviewed; 172 AA. AC Q4JAM0; DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot. DT 02-AUG-2005, sequence version 1. DT 27-MAR-2024, entry version 95. DE RecName: Full=dCTP deaminase {ECO:0000255|HAMAP-Rule:MF_00146}; DE EC=3.5.4.13 {ECO:0000255|HAMAP-Rule:MF_00146}; DE AltName: Full=Deoxycytidine triphosphate deaminase {ECO:0000255|HAMAP-Rule:MF_00146}; GN Name=dcd {ECO:0000255|HAMAP-Rule:MF_00146}; GN OrderedLocusNames=Saci_0789; OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC OS 15157 / NCIMB 11770). OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae; OC Sulfolobus. OX NCBI_TaxID=330779; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770; RX PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005; RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E., RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.; RT "The genome of Sulfolobus acidocaldarius, a model organism of the RT Crenarchaeota."; RL J. Bacteriol. 187:4992-4999(2005). CC -!- FUNCTION: Catalyzes the deamination of dCTP to dUTP. CC {ECO:0000255|HAMAP-Rule:MF_00146}. CC -!- CATALYTIC ACTIVITY: CC Reaction=dCTP + H(+) + H2O = dUTP + NH4(+); Xref=Rhea:RHEA:22680, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, CC ChEBI:CHEBI:61481, ChEBI:CHEBI:61555; EC=3.5.4.13; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00146}; CC -!- PATHWAY: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP CC route): step 1/2. {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; CP000077; AAY80159.1; -; Genomic_DNA. DR RefSeq; WP_011277661.1; NZ_CP046615.1. DR AlphaFoldDB; Q4JAM0; -. DR SMR; Q4JAM0; -. DR STRING; 330779.Saci_0789; -. DR GeneID; 78441136; -. DR KEGG; sai:Saci_0789; -. DR PATRIC; fig|330779.12.peg.756; -. DR eggNOG; arCOG04048; Archaea. DR HOGENOM; CLU_087476_3_0_2; -. DR UniPathway; UPA00610; UER00665. DR Proteomes; UP000001018; Chromosome. DR GO; GO:0008829; F:dCTP deaminase activity; IEA:UniProtKB-UniRule. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0006226; P:dUMP biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006229; P:dUTP biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd07557; trimeric_dUTPase; 1. DR Gene3D; 2.70.40.10; -; 1. DR HAMAP; MF_00146; dCTP_deaminase; 1. DR InterPro; IPR011962; dCTP_deaminase. DR InterPro; IPR029054; dUTPase-like. 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; PF00692; dUTPase; 1. DR SUPFAM; SSF51283; dUTPase-like; 1. PE 3: Inferred from homology; KW Hydrolase; Nucleotide metabolism; Nucleotide-binding; Reference proteome. FT CHAIN 1..172 FT /note="dCTP deaminase" FT /id="PRO_0000156039" FT ACT_SITE 123 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146" FT BINDING 97..102 FT /ligand="dCTP" FT /ligand_id="ChEBI:CHEBI:61481" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146" FT BINDING 113 FT /ligand="dCTP" FT /ligand_id="ChEBI:CHEBI:61481" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146" FT BINDING 155 FT /ligand="dCTP" FT /ligand_id="ChEBI:CHEBI:61481" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146" FT BINDING 162 FT /ligand="dCTP" FT /ligand_id="ChEBI:CHEBI:61481" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146" SQ SEQUENCE 172 AA; 19800 MW; DB7B97D5BD614676 CRC64; MILGDRDLKY YLEKGWIKVE PIYGDSVREN GIDLRVGNEI ARFKKTDKVF DPDNPDYSFF DVQRGEEFII SPHEHVLLVT EEYMKLPNDV MAFVNLRSTF ARLGLFIPPT IVDAGFEGQL TIEVVGSSFP VKIRRGTRFL HLIFARTLTP VENPYQGKYQ GQKGVTIPRF KL //