ID DCD_HELHP Reviewed; 188 AA. AC Q7VJQ0; DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2004, sequence version 2. DT 27-MAR-2024, entry version 102. 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=HH_0193; OS Helicobacter hepaticus (strain ATCC 51449 / 3B1). OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=235279; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51449 / 3B1; RX PubMed=12810954; DOI=10.1073/pnas.1332093100; RA Suerbaum S., Josenhans C., Sterzenbach T., Drescher B., Brandt P., Bell M., RA Droege M., Fartmann B., Fischer H.-P., Ge Z., Hoerster A., Holland R., RA Klein K., Koenig J., Macko L., Mendz G.L., Nyakatura G., Schauer D.B., RA Shen Z., Weber J., Frosch M., Fox J.G.; RT "The complete genome sequence of the carcinogenic bacterium Helicobacter RT hepaticus."; RL Proc. Natl. Acad. Sci. U.S.A. 100:7901-7906(2003). 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}. CC -!- SEQUENCE CAUTION: CC Sequence=AAP76790.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE017125; AAP76790.1; ALT_INIT; Genomic_DNA. DR RefSeq; WP_011115036.1; NC_004917.1. DR AlphaFoldDB; Q7VJQ0; -. DR SMR; Q7VJQ0; -. DR STRING; 235279.HH_0193; -. DR GeneID; 82134823; -. DR KEGG; hhe:HH_0193; -. DR eggNOG; COG0717; Bacteria. DR HOGENOM; CLU_087476_4_0_7; -. DR OrthoDB; 9780956at2; -. DR UniPathway; UPA00610; UER00665. DR Proteomes; UP000002495; 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 NCBIfam; TIGR02274; dCTP_deam; 1. DR PANTHER; PTHR42680; DCTP DEAMINASE; 1. DR PANTHER; PTHR42680:SF3; DCTP DEAMINASE; 1. DR Pfam; PF00692; dUTPase; 1. DR SUPFAM; SSF51283; dUTPase-like; 1. PE 3: Inferred from homology; KW Hydrolase; Nucleotide metabolism; Nucleotide-binding; Reference proteome. FT CHAIN 1..188 FT /note="dCTP deaminase" FT /id="PRO_0000155989" FT ACT_SITE 135 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146" FT BINDING 109..114 FT /ligand="dCTP" FT /ligand_id="ChEBI:CHEBI:61481" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146" FT BINDING 154 FT /ligand="dCTP" FT /ligand_id="ChEBI:CHEBI:61481" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146" FT BINDING 168 FT /ligand="dCTP" FT /ligand_id="ChEBI:CHEBI:61481" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146" FT BINDING 178 FT /ligand="dCTP" FT /ligand_id="ChEBI:CHEBI:61481" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146" SQ SEQUENCE 188 AA; 21035 MW; 36DF8367FF42C491 CRC64; MGLKSDTWIK KMSKKGMIEP FCEKQVGKNI VSYGLSSYGY DIRVGNEFMI FTNIGANLVD PKSFDERNVV EITTEENGYC LVPPNSFALA RTIEYFRIPR NVLAICLGKS TYARCGIIVN VTPFEPEFEG HITIEISNTT PLPAKIYANE GIAQVLFLEG DETCEVSYKD KKGKYQGQKG ITLPKVIK //