DCD_KORCO
ID DCD_KORCO Reviewed; 177 AA.
AC B1L7R6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=Kcr_0133;
OS Korarchaeum cryptofilum (strain OPF8).
OC Archaea; Candidatus Korarchaeota; Candidatus Korarchaeum.
OX NCBI_TaxID=374847;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OPF8;
RX PubMed=18535141; DOI=10.1073/pnas.0801980105;
RA Elkins J.G., Podar M., Graham D.E., Makarova K.S., Wolf Y., Randau L.,
RA Hedlund B.P., Brochier-Armanet C., Kunin V., Anderson I., Lapidus A.,
RA Goltsman E., Barry K., Koonin E.V., Hugenholtz P., Kyrpides N., Wanner G.,
RA Richardson P., Keller M., Stetter K.O.;
RT "A korarchaeal genome reveals new insights into the evolution of the
RT Archaea.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:8102-8107(2008).
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; CP000968; ACB06893.1; -; Genomic_DNA.
DR RefSeq; WP_012308790.1; NC_010482.1.
DR AlphaFoldDB; B1L7R6; -.
DR SMR; B1L7R6; -.
DR STRING; 374847.Kcr_0133; -.
DR EnsemblBacteria; ACB06893; ACB06893; Kcr_0133.
DR GeneID; 6093422; -.
DR KEGG; kcr:Kcr_0133; -.
DR eggNOG; arCOG04048; Archaea.
DR HOGENOM; CLU_087476_3_0_2; -.
DR InParanoid; B1L7R6; -.
DR OMA; RTSWIRK; -.
DR OrthoDB; 91282at2157; -.
DR PhylomeDB; B1L7R6; -.
DR UniPathway; UPA00610; UER00665.
DR Proteomes; UP000001686; 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..177
FT /note="dCTP deaminase"
FT /id="PRO_1000117975"
FT ACT_SITE 126
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT BINDING 100..105
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT BINDING 116
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT BINDING 159
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT BINDING 166
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
SQ SEQUENCE 177 AA; 19975 MW; 91EE39238C8AAE96 CRC64;
MLLSDKAIRS LIREGKLIID PLYEDSIREN GVDMRIGPEI AFPIVRGEVM DPTKDDPSLH
FTVRRFSDEG IIIPGNTSIL LVTEEYIKMP DDVAALCGLR SSIARWGFIA APTLVDAGFE
GQLTIEVMWT RPAPVRLYRG IRFLHVVFFR TEGKVERPYS GAYQGQRGVT LPKRLEK