DCD_ACIAM
ID DCD_ACIAM Reviewed; 173 AA.
AC Q02103;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 80.
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};
OS Acidianus ambivalens (Desulfurolobus ambivalens).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Acidianus.
OX NCBI_TaxID=2283;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Lei 10 / DSM 3772 / JCM 9191;
RX PubMed=1437556; DOI=10.1093/nar/20.20.5389;
RA Kletzin A.;
RT "Molecular characterisation of a DNA ligase gene of the extremely
RT thermophilic archaeon Desulfurolobus ambivalens shows close phylogenetic
RT relationship to eukaryotic ligases.";
RL Nucleic Acids Res. 20:5389-5396(1992).
RN [2]
RP SIMILARITY.
RX PubMed=7899076; DOI=10.1093/nar/23.4.565;
RA Ouzounis C., Kyrpides N., Sander C.;
RT "Novel protein families in archaean genomes.";
RL Nucleic Acids Res. 23:565-570(1995).
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, ECO:0000305}.
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DR EMBL; X63438; CAA45033.1; -; Genomic_DNA.
DR PIR; S26382; S26382.
DR AlphaFoldDB; Q02103; -.
DR SMR; Q02103; -.
DR PRIDE; Q02103; -.
DR UniPathway; UPA00610; UER00665.
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.
FT CHAIN 1..173
FT /note="dCTP deaminase"
FT /id="PRO_0000156025"
FT ACT_SITE 123
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT BINDING 97..102
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT BINDING 113
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT BINDING 155
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT BINDING 162
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
SQ SEQUENCE 173 AA; 19858 MW; B4D922503CD4B25A CRC64;
MILGDRDLKY YLEKGWIVIS PLTQDTIREN GVDLRVGGEI ARFKKTDEIY EDGKDPRSFY
EIEKGDEFII YPNEHVLLVT EEYVKLPNDV MAFVNLRSSF ARLGLFVPPT IVDAGFEGQL
TIEVLGSAFP VKIKRGTRFL HLIFARTLTP VENPYHGKYQ GQQGVTLPKF KFR
