ID   Q2GHG6_EHRCR            Unreviewed;       187 AA.
AC   Q2GHG6;
DT   21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2006, sequence version 1.
DT   04-NOV-2026, entry version 114.
DE   RecName: Full=dCTP deaminase {ECO:0000256|HAMAP-Rule:MF_00146};
DE            EC=3.5.4.13 {ECO:0000256|HAMAP-Rule:MF_00146};
DE   AltName: Full=Deoxycytidine triphosphate deaminase {ECO:0000256|HAMAP-Rule:MF_00146};
GN   Name=dcd {ECO:0000256|HAMAP-Rule:MF_00146};
GN   OrderedLocusNames=ECH_0296 {ECO:0000313|EMBL:ABD45481.1};
OS   Ehrlichia chaffeensis (strain ATCC CRL-10679 / Arkansas).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Rickettsiales; Anaplasmataceae; Ehrlichia.
OX   NCBI_TaxID=205920 {ECO:0000313|EMBL:ABD45481.1, ECO:0000313|Proteomes:UP000008320};
RN   [1] {ECO:0000313|EMBL:ABD45481.1, ECO:0000313|Proteomes:UP000008320}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC CRL-10679 / Arkansas {ECO:0000313|Proteomes:UP000008320};
RX   PubMed=16482227; DOI=10.1371/journal.pgen.0020021;
RA   Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V.,
RA   Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M.,
RA   Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N., Nelson W.,
RA   Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J., Daugherty S.C.,
RA   Davidsen T., Durkin A.S., Gwinn M., Haft D.H., Selengut J.D.,
RA   Sullivan S.A., Zafar N., Zhou L., Benahmed F., Forberger H., Halpin R.,
RA   Mulligan S., Robinson J., White O., Rikihisa Y., Tettelin H.;
RT   "Comparative genomics of emerging human ehrlichiosis agents.";
RL   PLoS Genet. 2:208-222(2006).
CC   -!- FUNCTION: Catalyzes the deamination of dCTP to dUTP.
CC       {ECO:0000256|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:0000256|HAMAP-Rule:MF_00146};
CC   -!- PATHWAY: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP
CC       route): step 1/2. {ECO:0000256|HAMAP-Rule:MF_00146}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000256|HAMAP-Rule:MF_00146}.
CC   -!- SIMILARITY: Belongs to the dCTP deaminase family. {ECO:0000256|HAMAP-
CC       Rule:MF_00146}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00146}.
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DR   EMBL; CP000236; ABD45481.1; -; Genomic_DNA.
DR   RefSeq; WP_011452519.1; NC_007799.1.
DR   AlphaFoldDB; Q2GHG6; -.
DR   STRING; 205920.ECH_0296; -.
DR   KEGG; ech:ECH_0296; -.
DR   eggNOG; COG0717; Bacteria.
DR   HOGENOM; CLU_087476_4_0_5; -.
DR   OMA; AAEHRMI; -.
DR   OrthoDB; 9780956at2; -.
DR   UniPathway; UPA00610; UER00665.
DR   Proteomes; UP000008320; 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 {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00146};
KW   Nucleotide metabolism {ECO:0000256|ARBA:ARBA00023080, ECO:0000256|HAMAP-
KW   Rule:MF_00146};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00146}; Reference proteome {ECO:0000313|Proteomes:UP000008320}.
FT   ACT_SITE        133
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00146"
FT   BINDING         107..112
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00146"
FT   BINDING         131..133
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00146"
FT   BINDING         152
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00146"
FT   BINDING         166
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00146"
FT   BINDING         172
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00146"
FT   BINDING         176
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00146"
SQ   SEQUENCE   187 AA;  21086 MW;  66065049F315F9B0 CRC64;
     MSVMPDHWIK DKAIKEKMID PFIDYKRSSG ILSYGLSSYG YDARIDNKFK VFTNVNSVTV
     DPKNFPLGSF IDKEEDVCII PPNSFVLAKT VEYFKIPKDI LVMCVGKSTY ARCGIVVNVT
     PLEPGWEGYV TLEFSNTTPL PAKIYAFEGA CQFIFLKGDS QCNLSYNEMQ GKYMNQLDVT
     LPIVNNS
//