ID DCD_CALMQ Reviewed; 179 AA. AC A8MC64; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 04-DEC-2007, sequence version 1. DT 27-MAR-2024, entry version 84. 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=Cmaq_0525; OS Caldivirga maquilingensis (strain ATCC 700844 / DSM 13496 / JCM 10307 / OS IC-167). OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae; OC Caldivirga. OX NCBI_TaxID=397948; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700844 / DSM 13496 / JCM 10307 / IC-167; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., RA Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C., RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Ivanova N., Biddle J.F., Zhang Z., Fitz-Gibbon S.T., Lowe T.M., RA Saltikov C., House C.H., Richardson P.; RT "Complete sequence of Caldivirga maquilingensis IC-167."; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. 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; CP000852; ABW01370.1; -; Genomic_DNA. DR RefSeq; WP_012185590.1; NC_009954.1. DR AlphaFoldDB; A8MC64; -. DR SMR; A8MC64; -. DR STRING; 397948.Cmaq_0525; -. DR GeneID; 5709628; -. DR KEGG; cma:Cmaq_0525; -. DR eggNOG; arCOG04048; Archaea. DR HOGENOM; CLU_087476_3_0_2; -. DR OrthoDB; 33242at2157; -. DR UniPathway; UPA00610; UER00665. DR Proteomes; UP000001137; 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..179 FT /note="dCTP deaminase" FT /id="PRO_1000189829" FT ACT_SITE 127 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146" FT BINDING 101..106 FT /ligand="dCTP" FT /ligand_id="ChEBI:CHEBI:61481" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146" FT BINDING 117 FT /ligand="dCTP" FT /ligand_id="ChEBI:CHEBI:61481" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146" FT BINDING 165 FT /ligand="dCTP" FT /ligand_id="ChEBI:CHEBI:61481" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146" SQ SEQUENCE 179 AA; 19846 MW; 4B9050D6981C76FF CRC64; MILARGEILK LIKDGSLGIE PFTEDVVREN GLDLRVGNEY AIYAFENQVI DPCELESTRH LFSIVEAKDG RIIIPPRSFA LLTTMEYVKF PRDVIGFCNL RSTLARYGLG VPPTIIDTGF EGNITIEVIN NSGNYVVLRP GMRFLHVVLA KTIGEAKYQG KYLGQRGVTP PKGLKGECS //