DCD_CAMJE
ID DCD_CAMJE Reviewed; 186 AA.
AC Q9PN07; Q0P8W5;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 110.
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=Cj1292;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
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 -!- INTERACTION:
CC Q9PN07; Q9PMS6: Cj1374c; NbExp=3; IntAct=EBI-1271615, EBI-1271444;
CC -!- SIMILARITY: Belongs to the dCTP deaminase family. {ECO:0000255|HAMAP-
CC Rule:MF_00146}.
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DR EMBL; AL111168; CAL35406.1; -; Genomic_DNA.
DR PIR; A81272; A81272.
DR RefSeq; WP_002854086.1; NC_002163.1.
DR RefSeq; YP_002344682.1; NC_002163.1.
DR AlphaFoldDB; Q9PN07; -.
DR SMR; Q9PN07; -.
DR IntAct; Q9PN07; 18.
DR STRING; 192222.Cj1292; -.
DR BindingDB; Q9PN07; -.
DR PaxDb; Q9PN07; -.
DR PRIDE; Q9PN07; -.
DR EnsemblBacteria; CAL35406; CAL35406; Cj1292.
DR GeneID; 905584; -.
DR KEGG; cje:Cj1292; -.
DR PATRIC; fig|192222.6.peg.1274; -.
DR eggNOG; COG0717; Bacteria.
DR HOGENOM; CLU_087476_4_0_7; -.
DR OMA; FENHRYP; -.
DR UniPathway; UPA00610; UER00665.
DR Proteomes; UP000000799; 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 1: Evidence at protein level;
KW Hydrolase; Nucleotide metabolism; Nucleotide-binding; Reference proteome.
FT CHAIN 1..186
FT /note="dCTP deaminase"
FT /id="PRO_0000155972"
FT ACT_SITE 133
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT BINDING 107..112
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT BINDING 152
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"
FT BINDING 176
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
SQ SEQUENCE 186 AA; 20699 MW; 68DC660FB28FD33C CRC64;
MGLKADNWIR KMALEHKMIE PFCEANIGKG VVSYGLSSYG YDIRVGREFK IFTNVNSTVV
DPKNFVEENV VDFEGDVCIV PANSFALART IEYFKMPDNV LAICLGKSTY ARCGIIVNVT
PFEPGFEGHI TIEISNTTPL PAKIYANEGI AQVLFLQGDE KCDTTYKDKK GKYQAQTGIT
LPRILK