ID DCD_ACIB5 Reviewed; 189 AA. AC B7I774; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 10-FEB-2009, sequence version 1. DT 27-MAR-2024, entry version 77. 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}; GN OrderedLocusNames=AB57_0835; OS Acinetobacter baumannii (strain AB0057). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae; OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=480119; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AB0057; RX PubMed=18931120; DOI=10.1128/jb.00834-08; RA Adams M.D., Goglin K., Molyneaux N., Hujer K.M., Lavender H., Jamison J.J., RA MacDonald I.J., Martin K.M., Russo T., Campagnari A.A., Hujer A.M., RA Bonomo R.A., Gill S.R.; RT "Comparative genome sequence analysis of multidrug-resistant Acinetobacter RT baumannii."; RL J. Bacteriol. 190:8053-8064(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}. 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; CP001182; ACJ40633.1; -; Genomic_DNA. DR RefSeq; WP_000985728.1; NC_011586.2. DR AlphaFoldDB; B7I774; -. DR SMR; B7I774; -. DR GeneID; 66398272; -. DR KEGG; abn:AB57_0835; -. DR HOGENOM; CLU_087476_4_0_6; -. DR UniPathway; UPA00610; UER00665. DR Proteomes; UP000007094; 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..189 FT /note="dCTP deaminase" FT /id="PRO_1000189821" 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 171 FT /ligand="dCTP" FT /ligand_id="ChEBI:CHEBI:61481" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146" FT BINDING 181 FT /ligand="dCTP" FT /ligand_id="ChEBI:CHEBI:61481" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146" SQ SEQUENCE 189 AA; 21442 MW; 80F7A026AC9D7CF8 CRC64; MAIKSDRWIR EMSEKHGMIE PYAENQVRFD KNGEKLISYG VSSYGYDVRC AREFKVFTNV HSAIVDPKNF DEKSFIDIES DVCIIPPNSF ALARTIEYFR IPRNVLTVCL GKSTYARCGI IVNVTPLEPE WEGHVTLEFS NTTNLPARIY AGEGVAQMLF FESDEVCETS YKDRGGKYQG QTGVTLPKT //