ID U1PVD1_9EURY Unreviewed; 206 AA.
AC U1PVD1;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 40.
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=J07HQW2_02828 {ECO:0000313|EMBL:ERG96351.1};
OS Haloquadratum walsbyi J07HQW2.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloquadratum.
OX NCBI_TaxID=1238425 {ECO:0000313|EMBL:ERG96351.1, ECO:0000313|Proteomes:UP000030710};
RN [1] {ECO:0000313|EMBL:ERG96351.1, ECO:0000313|Proteomes:UP000030710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J07HQW2 {ECO:0000313|Proteomes:UP000030710};
RX PubMed=23637883;
RA Podell S., Ugalde J.A., Narasingarao P., Banfield J.F., Heidelberg K.B.,
RA Allen E.E.;
RT "Assembly-driven community genomics of a hypersaline microbial ecosystem.";
RL PLoS ONE 8:E61692-E61692(2013).
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 ---------------------------------------------------------------------------
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; KE356561; ERG96351.1; -; Genomic_DNA.
DR AlphaFoldDB; U1PVD1; -.
DR STRING; 1238425.J07HQW2_02828; -.
DR eggNOG; arCOG04048; Archaea.
DR HOGENOM; CLU_087476_2_1_2; -.
DR UniPathway; UPA00610; UER00665.
DR Proteomes; UP000030710; 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: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}.
FT DOMAIN 74..181
FT /note="dUTPase-like"
FT /evidence="ECO:0000259|Pfam:PF00692"
FT REGION 165..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 133
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00146"
FT BINDING 105..110
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00146"
FT BINDING 123
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 173
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00146"
FT BINDING 177
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00146"
SQ SEQUENCE 206 AA; 22559 MW; D33FF8B00C35D207 CRC64;
MILSDDDILA RLETGELVVE PIDDLDMQVQ PASIDLRLGE EFLEFQRTNI SCIHPNRQEE
VSEYVSETII PEGDEFILHP GDFVLGTTKE RVDIPPDLLA TVEGRSSLGR LAVVIHATAG
VVDPGYCGQI TLELSNLGTA PVALTPGMRV SQLVFTELTQ SSARPYGAAR DSKYQNQTGP
QASRIGEDPE FDQTDDTAHQ HNQNTT
//
