ID DCD_NEIMA Reviewed; 188 AA. AC P63903; A1IR88; Q9JRE8; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 27-MAR-2024, entry version 94. 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}; OrderedLocusNames=NMA1060; OS Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 / OS Z2491). OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae; OC Neisseria. OX NCBI_TaxID=122587; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15465 / Z2491; RX PubMed=10761919; DOI=10.1038/35006655; RA Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M., RA Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M., RA Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K., RA Leather S., Moule S., Mungall K.L., Quail M.A., Rajandream M.A., RA Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G., RA Barrell B.G.; RT "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis RT Z2491."; RL Nature 404:502-506(2000). 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; AL157959; CAM08274.1; -; Genomic_DNA. DR RefSeq; WP_002224592.1; NC_003116.1. DR AlphaFoldDB; P63903; -. DR SMR; P63903; -. DR EnsemblBacteria; CAM08274; CAM08274; NMA1060. DR GeneID; 61281080; -. DR KEGG; nma:NMA1060; -. DR HOGENOM; CLU_087476_4_0_4; -. DR UniPathway; UPA00610; UER00665. DR Proteomes; UP000000626; 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. FT CHAIN 1..188 FT /note="dCTP deaminase" FT /id="PRO_0000155998" 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 180 FT /ligand="dCTP" FT /ligand_id="ChEBI:CHEBI:61481" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146" SQ SEQUENCE 188 AA; 21295 MW; 2CA4459F4E78FDF6 CRC64; MSIKSDKWIR RMSEEFGMID PFEPNQIKEA DGKRIISYGT SSYGYDIRCA NEFKIFTNIN STIVDPKNFD PKNFVTVEDD CCIIPPNSFA LARTVEYFRI PRNVLTVCLG KSTYARCGII VNVTPFEPEW EGYVTLEFSN TTPLPAKIYA GEGVAQVLFF ESDEICETSY KDRNGKYMGQ TGVTLPKA //