ID DCD_NITMU Reviewed; 189 AA. AC Q2Y7L1; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 20-DEC-2005, sequence version 1. DT 27-MAR-2024, entry version 93. 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=Nmul_A1965; OS Nitrosospira multiformis (strain ATCC 25196 / NCIMB 11849 / C 71). OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales; OC Nitrosomonadaceae; Nitrosospira. OX NCBI_TaxID=323848; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25196 / NCIMB 11849 / C 71; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., RA Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Lykidis A., Richardson P.; RT "Complete sequence of chromosome 1 of Nitrosospira multiformis ATCC RT 25196."; RL Submitted (AUG-2005) 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; CP000103; ABB75260.1; -; Genomic_DNA. DR RefSeq; WP_011381280.1; NZ_FNVK01000004.1. DR AlphaFoldDB; Q2Y7L1; -. DR SMR; Q2Y7L1; -. DR STRING; 323848.Nmul_A1965; -. DR KEGG; nmu:Nmul_A1965; -. DR eggNOG; COG0717; Bacteria. DR HOGENOM; CLU_087476_4_0_4; -. DR OrthoDB; 9780956at2; -. DR UniPathway; UPA00610; UER00665. DR Proteomes; UP000002718; 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..189 FT /note="dCTP deaminase" FT /id="PRO_1000009771" FT ACT_SITE 138 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146" FT BINDING 112..117 FT /ligand="dCTP" FT /ligand_id="ChEBI:CHEBI:61481" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146" FT BINDING 136..138 FT /ligand="dCTP" FT /ligand_id="ChEBI:CHEBI:61481" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146" FT BINDING 157 FT /ligand="dCTP" FT /ligand_id="ChEBI:CHEBI:61481" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146" FT BINDING 171 FT /ligand="dCTP" FT /ligand_id="ChEBI:CHEBI:61481" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146" FT BINDING 181 FT /ligand="dCTP" FT /ligand_id="ChEBI:CHEBI:61481" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146" SQ SEQUENCE 189 AA; 21360 MW; E33D41E0955966CB CRC64; MTIKSDKWIR RMAMEHGMIE PFEPNQVKHA PDGHKIVSYG TSSYGYDIRC SDEFKLFTNI NSAIVDPKNF DSNSFVDVKS NICLIPPNSF ALARTVEYFR IPRNVLTICL GKSTYARCGI IVNVTPFEPE WEGFVTLEFS NTTPLPAKIY ANEGVAQVIF FESDEICETS YKDRGGKYQG QHGVTLPKI //