ID A0A972GCI3_9CHLR Unreviewed; 184 AA. AC A0A972GCI3; DT 22-FEB-2023, integrated into UniProtKB/TrEMBL. DT 22-FEB-2023, sequence version 1. DT 29-MAY-2024, entry version 5. DE RecName: Full=dCTP deaminase {ECO:0000256|HAMAP-Rule:MF_00146}; DE EC=3.5.4.13 {ECO:0000256|HAMAP-Rule:MF_00146}; DE AltName: Full=Deoxycytidine triphosphate deaminase {ECO:0000256|HAMAP-Rule:MF_00146}; GN Name=dcd {ECO:0000256|HAMAP-Rule:MF_00146}; GN ORFNames=GFH27_549303n85 {ECO:0000313|EMBL:NOK83224.1}; OS Chloroflexi bacterium AL-W. OC Bacteria; Chloroflexota. OX NCBI_TaxID=2686371 {ECO:0000313|EMBL:NOK83224.1, ECO:0000313|Proteomes:UP000655226}; RN [1] {ECO:0000313|EMBL:NOK83224.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AL-W {ECO:0000313|EMBL:NOK83224.1}; RA Saghai A., Zivanovic Y., Moreira D., Lopez-Garcia P.; RT "Lithoflexus mexicanensis, a novel phototrophic Chloroflexi lineage RT exhibiting a clonal pattern along a depth gradient."; RL Submitted (DEC-2019) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the deamination of dCTP to dUTP. CC {ECO:0000256|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:0000256|HAMAP-Rule:MF_00146}; CC -!- PATHWAY: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP CC route): step 1/2. {ECO:0000256|HAMAP-Rule:MF_00146}. CC -!- SUBUNIT: Homotrimer. {ECO:0000256|HAMAP-Rule:MF_00146}. CC -!- SIMILARITY: Belongs to the dCTP deaminase family. {ECO:0000256|HAMAP- CC Rule:MF_00146}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00146}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:NOK83224.1}. 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; WYDX01000011; NOK83224.1; -; Genomic_DNA. DR Proteomes; UP000655226; Unassembled WGS sequence. DR GO; GO:0008829; F:dCTP deaminase activity; IEA:UniProtKB-UniRule. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0006229; P:dUTP biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0015949; P:nucleobase-containing small molecule interconversion; IEA:TreeGrafter. 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; 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 SUPFAM; SSF51283; dUTPase-like; 1. PE 3: Inferred from homology; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00146}; KW Nucleotide metabolism {ECO:0000256|ARBA:ARBA00023080, ECO:0000256|HAMAP- KW Rule:MF_00146}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00146}; KW Reference proteome {ECO:0000313|Proteomes:UP000655226}. FT ACT_SITE 133 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00146" FT BINDING 107..112 FT /ligand="dCTP" FT /ligand_id="ChEBI:CHEBI:61481" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00146" FT BINDING 131..133 FT /ligand="dCTP" FT /ligand_id="ChEBI:CHEBI:61481" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00146" FT BINDING 152 FT /ligand="dCTP" FT /ligand_id="ChEBI:CHEBI:61481" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00146" FT BINDING 166 FT /ligand="dCTP" FT /ligand_id="ChEBI:CHEBI:61481" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00146" FT BINDING 172 FT /ligand="dCTP" FT /ligand_id="ChEBI:CHEBI:61481" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00146" FT BINDING 176 FT /ligand="dCTP" FT /ligand_id="ChEBI:CHEBI:61481" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00146" SQ SEQUENCE 184 AA; 21053 MW; 8BEF4C58217E0349 CRC64; MSIKADRWIR RMALEESMIE PFVERQVRDE VISYGLSSYG YDMRIANEFK VFTNVFNTLV DPKCFDERSF VDITADYCDI PPNSFALARS VEFFRIPRNV LAICLGKSTY ARCGIILNTT PFEPGWRGYV TLEISNTTPL PARIYANEGI GQVLFFESDE DCETSYADKH GKYLDQIGVV LPKL //