ID DCD_GEMAT Reviewed; 184 AA. AC C1A8Z5; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 26-MAY-2009, sequence version 1. DT 27-MAR-2024, entry version 68. 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=GAU_1663; OS Gemmatimonas aurantiaca (strain T-27 / DSM 14586 / JCM 11422 / NBRC OS 100505). OC Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales; OC Gemmatimonadaceae; Gemmatimonas. OX NCBI_TaxID=379066; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=T-27 / DSM 14586 / JCM 11422 / NBRC 100505; RA Takasaki K., Ichikawa N., Miura H., Matsushita S., Watanabe Y., Oguchi A., RA Ankai A., Yashiro I., Takahashi M., Terui Y., Fukui S., Yokoyama H., RA Tanikawa S., Hanada S., Kamagata Y., Fujita N.; RT "Complete genome sequence of Gemmatimonas aurantiaca T-27 that represents a RT novel phylum Gemmatimonadetes."; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. 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; AP009153; BAH38705.1; -; Genomic_DNA. DR RefSeq; WP_012683152.1; NC_012489.1. DR AlphaFoldDB; C1A8Z5; -. DR SMR; C1A8Z5; -. DR STRING; 379066.GAU_1663; -. DR KEGG; gau:GAU_1663; -. DR eggNOG; COG0717; Bacteria. DR HOGENOM; CLU_087476_4_0_0; -. DR OrthoDB; 9780202at2; -. DR UniPathway; UPA00610; UER00665. DR Proteomes; UP000002209; 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..184 FT /note="dCTP deaminase" FT /id="PRO_1000203359" 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 131..133 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 184 AA; 20719 MW; CB63687C7F5AA598 CRC64; MGLCSDRWIT RMSREHGMIE PFEDRQVRQG VISYGVSSYG YDMRVAREFK IFTNVLSSVV DPKAFDPKSF VEFEGDVCIV PPNSFALARS VEYFRIPRNV LTLTVGKSTY ARCGIITNVT PFEPEWEGYV TLEISNTTPL PAKIYANEGI AQVVFFTGDE PPEVSYGDKK GKYQGQHGVT LPRI //