DCD_CHLTR
ID DCD_CHLTR Reviewed; 190 AA.
AC O84042;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=CT_039;
OS Chlamydia trachomatis (strain D/UW-3/Cx).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=272561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D/UW-3/Cx;
RX PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT trachomatis.";
RL Science 282:754-759(1998).
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; AE001273; AAC67629.1; -; Genomic_DNA.
DR PIR; B71565; B71565.
DR RefSeq; NP_219541.1; NC_000117.1.
DR RefSeq; WP_009871386.1; NC_000117.1.
DR AlphaFoldDB; O84042; -.
DR SMR; O84042; -.
DR STRING; 813.O172_00210; -.
DR EnsemblBacteria; AAC67629; AAC67629; CT_039.
DR GeneID; 884070; -.
DR KEGG; ctr:CT_039; -.
DR PATRIC; fig|272561.5.peg.44; -.
DR HOGENOM; CLU_087476_4_0_0; -.
DR InParanoid; O84042; -.
DR OMA; FENHRYP; -.
DR UniPathway; UPA00610; UER00665.
DR Proteomes; UP000000431; Chromosome.
DR GO; GO:0008829; F:dCTP deaminase activity; IBA:GO_Central.
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 GO; GO:0015949; P:nucleobase-containing small molecule interconversion; IBA:GO_Central.
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..190
FT /note="dCTP deaminase"
FT /id="PRO_0000155977"
FT ACT_SITE 139
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT BINDING 113..118
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT BINDING 158
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT BINDING 172
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"
FT BINDING 182
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
SQ SEQUENCE 190 AA; 21414 MW; 7354BA4921D2071A CRC64;
MGIKEDNWIR KMAIEEGMIE PFADSQVKLH PETGEKLISY GLSSYGYDLR ISREFKVFTN
VYNSLVDPKC FTEDALISIV DDVCIIPPNS FALARSVEYF RIPRNVLTVC IGKSTYARCG
LIVNVTPFEP EWEGYVTIEI SNTTPLPAKV YANEGIAQVL FFEGDATCDV SYAERQGKYQ
KQQGITIPFV