ID DCD_SHEFN Reviewed; 194 AA. AC Q081H6; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 31-OCT-2006, sequence version 1. DT 27-MAR-2024, entry version 93. 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=Sfri_2243; OS Shewanella frigidimarina (strain NCIMB 400). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=318167; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCIMB 400; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., Nealson K.H., RA Newman D., Tiedje J.M., Zhou J., Romine M.F., Culley D.E., Serres M., RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.; RT "Complete sequence of Shewanella frigidimarina NCIMB 400."; RL Submitted (AUG-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; CP000447; ABI72089.1; -; Genomic_DNA. DR RefSeq; WP_011637699.1; NC_008345.1. DR AlphaFoldDB; Q081H6; -. DR SMR; Q081H6; -. DR STRING; 318167.Sfri_2243; -. DR KEGG; sfr:Sfri_2243; -. DR eggNOG; COG0717; Bacteria. DR HOGENOM; CLU_087476_2_0_6; -. DR OrthoDB; 9780956at2; -. DR UniPathway; UPA00610; UER00665. DR Proteomes; UP000000684; 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..194 FT /note="dCTP deaminase" FT /id="PRO_1000009809" FT REGION 174..194 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 138 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146" FT BINDING 110..115 FT /ligand="dCTP" FT /ligand_id="ChEBI:CHEBI:61481" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146" FT BINDING 128 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 171 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" FT BINDING 182 FT /ligand="dCTP" FT /ligand_id="ChEBI:CHEBI:61481" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146" SQ SEQUENCE 194 AA; 21379 MW; FD4B3E301CFB3F35 CRC64; MRLTDIEIEQ CLDNGTIIID PRPGIEAISG VSVDVRLGSQ FRVFKDHTAP YIDLSGPSAE MQIALDRIMS DKIEIADDQA FFLHPGELAL AVTYESVTLP ADIVGWLDGR SSLARLGLMV HVTAHRIDPG WQGKIVLEFF NSGKLPLALR PGMTIGALNF ERLSSAVARP YNTRKSSKYK DQQEAVASRI SQDK //