ID   DCD_CUPMC               Reviewed;         188 AA.
AC   Q1LJP8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=Rmet_2755;
OS   Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS   CH34) (Ralstonia metallidurans).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=266264;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34;
RX   PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA   Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA   Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA   Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT   "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT   master survivalist in harsh and anthropogenic environments.";
RL   PLoS ONE 5:E10433-E10433(2010).
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}.
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DR   EMBL; CP000352; ABF09628.1; -; Genomic_DNA.
DR   RefSeq; WP_008646296.1; NC_007973.1.
DR   AlphaFoldDB; Q1LJP8; -.
DR   SMR; Q1LJP8; -.
DR   STRING; 266264.Rmet_2755; -.
DR   EnsemblBacteria; ABF09628; ABF09628; Rmet_2755.
DR   GeneID; 60820795; -.
DR   KEGG; rme:Rmet_2755; -.
DR   eggNOG; COG0717; Bacteria.
DR   HOGENOM; CLU_087476_4_0_4; -.
DR   OMA; FENHRYP; -.
DR   OrthoDB; 1598407at2; -.
DR   UniPathway; UPA00610; UER00665.
DR   Proteomes; UP000002429; 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   Pfam; PF00692; dUTPase; 1.
DR   SUPFAM; SSF51283; SSF51283; 1.
DR   TIGRFAMs; TIGR02274; dCTP_deam; 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_1000009795"
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;  21209 MW;  E3B65CD4905728B7 CRC64;
     MSIKSDKWIR RMAEQHGMIE PFEPGQVRES DGRKIVSYGT SSYGYDIRCA DEFKIFTNIN
     STIVDPKNFD EKSFVDFKGD VCIIPPNSFA LARTMEYFRI PRSVLTICLG KSTYARCGII
     VNVTPFEPEW EGYVTLEFSN TTPLPAKIYA GEGCAQVLFF ESDEICETSY ADRGGKYQGQ
     QGVTLPKT