ID DCD_XYLFA Reviewed; 191 AA. AC Q9PFB6; DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 27-MAR-2024, 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=XF_0762; OS Xylella fastidiosa (strain 9a5c). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xylella. OX NCBI_TaxID=160492; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=9a5c; RX PubMed=10910347; DOI=10.1038/35018003; RA Simpson A.J.G., Reinach F.C., Arruda P., Abreu F.A., Acencio M., RA Alvarenga R., Alves L.M.C., Araya J.E., Baia G.S., Baptista C.S., RA Barros M.H., Bonaccorsi E.D., Bordin S., Bove J.M., Briones M.R.S., RA Bueno M.R.P., Camargo A.A., Camargo L.E.A., Carraro D.M., Carrer H., RA Colauto N.B., Colombo C., Costa F.F., Costa M.C.R., Costa-Neto C.M., RA Coutinho L.L., Cristofani M., Dias-Neto E., Docena C., El-Dorry H., RA Facincani A.P., Ferreira A.J.S., Ferreira V.C.A., Ferro J.A., Fraga J.S., RA Franca S.C., Franco M.C., Frohme M., Furlan L.R., Garnier M., Goldman G.H., RA Goldman M.H.S., Gomes S.L., Gruber A., Ho P.L., Hoheisel J.D., RA Junqueira M.L., Kemper E.L., Kitajima J.P., Krieger J.E., Kuramae E.E., RA Laigret F., Lambais M.R., Leite L.C.C., Lemos E.G.M., Lemos M.V.F., RA Lopes S.A., Lopes C.R., Machado J.A., Machado M.A., Madeira A.M.B.N., RA Madeira H.M.F., Marino C.L., Marques M.V., Martins E.A.L., Martins E.M.F., RA Matsukuma A.Y., Menck C.F.M., Miracca E.C., Miyaki C.Y., RA Monteiro-Vitorello C.B., Moon D.H., Nagai M.A., Nascimento A.L.T.O., RA Netto L.E.S., Nhani A. Jr., Nobrega F.G., Nunes L.R., Oliveira M.A., RA de Oliveira M.C., de Oliveira R.C., Palmieri D.A., Paris A., Peixoto B.R., RA Pereira G.A.G., Pereira H.A. Jr., Pesquero J.B., Quaggio R.B., RA Roberto P.G., Rodrigues V., de Rosa A.J.M., de Rosa V.E. Jr., de Sa R.G., RA Santelli R.V., Sawasaki H.E., da Silva A.C.R., da Silva A.M., RA da Silva F.R., Silva W.A. Jr., da Silveira J.F., Silvestri M.L.Z., RA Siqueira W.J., de Souza A.A., de Souza A.P., Terenzi M.F., Truffi D., RA Tsai S.M., Tsuhako M.H., Vallada H., Van Sluys M.A., Verjovski-Almeida S., RA Vettore A.L., Zago M.A., Zatz M., Meidanis J., Setubal J.C.; RT "The genome sequence of the plant pathogen Xylella fastidiosa."; RL Nature 406:151-159(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 -!- SIMILARITY: Belongs to the dCTP deaminase family. {ECO:0000255|HAMAP- CC Rule:MF_00146}. 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; AE003849; AAF83572.1; -; Genomic_DNA. DR PIR; G82765; G82765. DR RefSeq; WP_010893285.1; NC_002488.3. DR AlphaFoldDB; Q9PFB6; -. DR SMR; Q9PFB6; -. DR STRING; 160492.XF_0762; -. DR KEGG; xfa:XF_0762; -. DR eggNOG; COG0717; Bacteria. DR HOGENOM; CLU_087476_4_0_6; -. DR UniPathway; UPA00610; UER00665. DR Proteomes; UP000000812; 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. FT CHAIN 1..191 FT /note="dCTP deaminase" FT /id="PRO_0000156022" FT ACT_SITE 138 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146" FT BINDING 112..117 FT /ligand="dCTP" FT /ligand_id="ChEBI:CHEBI:61481" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146" FT BINDING 136..138 FT /ligand="dCTP" FT /ligand_id="ChEBI:CHEBI:61481" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146" FT BINDING 157 FT /ligand="dCTP" FT /ligand_id="ChEBI:CHEBI:61481" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146" FT BINDING 173 FT /ligand="dCTP" FT /ligand_id="ChEBI:CHEBI:61481" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146" FT BINDING 183 FT /ligand="dCTP" FT /ligand_id="ChEBI:CHEBI:61481" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146" SQ SEQUENCE 191 AA; 21531 MW; D7B23653F94B3649 CRC64; MSIKSDRWIR HMAQQHGMIA PFEPGQIKQN ATGQRIVSYG TSSYGYDVRC SREFKIFTNI NSTIVDPKQF DNGSFIDVES DVCIIPPNSF ALARTIEYFR IPRNVLVICL GKSTYARCGI IVNVTPLEPE WEGHVTLEFS NTTPLPARIY ANEGVAQMLF LQADPDDVCQ TSYRDRNGKY QGQTGVTLPR T //