ID DCD_RICAE Reviewed; 188 AA. AC C3PMB0; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 16-JUN-2009, sequence version 1. DT 02-SEP-2026, entry version 79. 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=RAF_ORF0095; OS Rickettsia africae (strain ESF-5). OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Rickettsiales; Rickettsiaceae; Rickettsieae; Rickettsia; OC spotted fever group. OX NCBI_TaxID=347255; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ESF-5; RX PubMed=19379498; DOI=10.1186/1471-2164-10-166; RA Fournier P.-E., El Karkouri K., Leroy Q., Robert C., Giumelli B., RA Renesto P., Socolovschi C., Parola P., Audic S., Raoult D.; RT "Analysis of the Rickettsia africae genome reveals that virulence RT acquisition in Rickettsia species may be explained by genome reduction."; RL BMC Genomics 10:166-166(2009). CC -!- FUNCTION: Catalyzes the deamination of dCTP to dUTP. CC {ECO:0000255|HAMAP-Rule:MF_00146}. CC -!- CATALYTIC ACTIVITY: CC Reaction=dCTP + H2O + H(+) = 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; CP001612; ACP53070.1; -; Genomic_DNA. DR RefSeq; WP_004996797.1; NC_012633.1. DR AlphaFoldDB; C3PMB0; -. DR SMR; C3PMB0; -. DR GeneID; 79936898; -. DR GeneID; 95361829; -. DR KEGG; raf:RAF_ORF0095; -. DR HOGENOM; CLU_087476_4_0_5; -. DR UniPathway; UPA00610; UER00665. DR Proteomes; UP000002305; Chromosome. DR GO; GO:0008829; F:dCTP deaminase activity; IEA:UniProtKB-UniRule. 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 FunFam; 2.70.40.10:FF:000001; dCTP deaminase; 1. DR Gene3D; 2.70.40.10; -; 1. DR HAMAP; MF_00146; dCTP_deaminase; 1. 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; PF22769; DCD; 1. DR SUPFAM; SSF51283; dUTPase-like; 1. PE 3: Inferred from homology; KW Hydrolase; Nucleotide metabolism; Nucleotide-binding; Reference proteome. FT CHAIN 1..188 FT /note="dCTP deaminase" FT /id="PRO_1000203365" FT ACT_SITE 137 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146" FT BINDING 111..116 FT /ligand="dCTP" FT /ligand_id="ChEBI:CHEBI:61481" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146" FT BINDING 135..137 FT /ligand="dCTP" FT /ligand_id="ChEBI:CHEBI:61481" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146" FT BINDING 156 FT /ligand="dCTP" FT /ligand_id="ChEBI:CHEBI:61481" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146" FT BINDING 170 FT /ligand="dCTP" FT /ligand_id="ChEBI:CHEBI:61481" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146" FT BINDING 179 FT /ligand="dCTP" FT /ligand_id="ChEBI:CHEBI:61481" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146" FT BINDING 180 FT /ligand="dCTP" FT /ligand_id="ChEBI:CHEBI:61481" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146" SQ SEQUENCE 188 AA; 21328 MW; 34EF8EBA5D3A9257 CRC64; MAIMSDKWIK EAVINHSMIR PFAEKQVRVH NKEKIISYGL SSYGYDARVS NEFKIFTNIN STTVDPKNFS EYNLVDREVD VCIIPPNSFA LGRTIEYFKI PRDVLVICVG KSTYARCGII VNVTPLEPEW EGHVTLEFSN TTPLPAKIYA NEGACQFLFL KSDQICDTSY ADRQGKYMKQ VGVTLPLT //