ID A0A2U9IE72_9CREN Unreviewed; 179 AA.
AC A0A2U9IE72;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
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=DFR85_06765 {ECO:0000313|EMBL:AWR94342.1};
OS Acidianus brierleyi.
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Acidianus.
OX NCBI_TaxID=41673 {ECO:0000313|EMBL:AWR94342.1, ECO:0000313|Proteomes:UP000248044};
RN [1] {ECO:0000313|EMBL:AWR94342.1, ECO:0000313|Proteomes:UP000248044}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1651 {ECO:0000313|EMBL:AWR94342.1,
RC ECO:0000313|Proteomes:UP000248044};
RA Counts J.A., Kelly R.M.;
RT "Complete Genome Sequences of Extremely Thermoacidophilic, Metal-Mobilizing
RT Type-Strain Members of the Archaeal Family Sulfolobaceae: Acidianus
RT brierleyi DSM-1651T, Acidianus sulfidivorans DSM-18786T, Metallosphaera
RT hakonensis DSM-7519T, and Metallosphaera prunae DSM-10039T.";
RL Submitted (MAY-2018) 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}.
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DR EMBL; CP029289; AWR94342.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9IE72; -.
DR KEGG; abri:DFR85_06765; -.
DR OrthoDB; 33242at2157; -.
DR UniPathway; UPA00610; UER00665.
DR Proteomes; UP000248044; 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 {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:UP000248044}.
FT DOMAIN 61..167
FT /note="dUTPase-like"
FT /evidence="ECO:0000259|Pfam:PF00692"
FT ACT_SITE 124
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00146"
FT BINDING 98..103
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00146"
FT BINDING 114
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00146"
FT BINDING 156
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00146"
FT BINDING 159
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00146"
FT BINDING 163
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00146"
SQ SEQUENCE 179 AA; 20312 MW; FEA3E99FAD26071A CRC64;
MILGDRDLKY YLEKGWIIID PLNSDSIREN GVDLRVGDQI ARFKNTNKIF TLDENDINEF
FIIEKGTEFI INPQEHVLLT TKEMIKLPSD VMAFVNMRSS FARLGLFVPP TIVDAGFEGQ
VTIEVLGSAF PIKIKEGTRF IHLIFAKTLT PVENPYHGKY QGQKGVTLAR FNLQASSNF
//
