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Entry: A0A0B3C183_9PSED
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ID   A0A0B3C183_9PSED        Unreviewed;       188 AA.
AC   A0A0B3C183;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 42.
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   ECO:0000313|EMBL:KHO66669.1};
GN   ORFNames=PT85_00245 {ECO:0000313|EMBL:KHO66669.1}, SAMN05421672_11050
GN   {ECO:0000313|EMBL:SIQ79265.1};
OS   Pseudomonas flexibilis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=706570 {ECO:0000313|EMBL:KHO66669.1, ECO:0000313|Proteomes:UP000030980};
RN   [1] {ECO:0000313|EMBL:KHO66669.1, ECO:0000313|Proteomes:UP000030980}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 14085 {ECO:0000313|EMBL:KHO66669.1,
RC   ECO:0000313|Proteomes:UP000030980};
RA   Shin S.-K., Yi H.;
RT   "Genome sequence of Pseudomonas tuomuerensis JCM 14085.";
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:SIQ79265.1, ECO:0000313|Proteomes:UP000186079}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29606 {ECO:0000313|EMBL:SIQ79265.1,
RC   ECO:0000313|Proteomes:UP000186079};
RA   Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL   Submitted (JAN-2017) 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; JTAK01000001; KHO66669.1; -; Genomic_DNA.
DR   EMBL; FTMC01000010; SIQ79265.1; -; Genomic_DNA.
DR   RefSeq; WP_027590810.1; NZ_JTAK01000001.1.
DR   AlphaFoldDB; A0A0B3C183; -.
DR   STRING; 706570.PT85_00245; -.
DR   OrthoDB; 9780956at2; -.
DR   UniPathway; UPA00610; UER00665.
DR   Proteomes; UP000030980; Unassembled WGS sequence.
DR   Proteomes; UP000186079; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030980}.
FT   DOMAIN          82..184
FT                   /note="dUTPase-like"
FT                   /evidence="ECO:0000259|Pfam:PF00692"
FT   ACT_SITE        137
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00146"
FT   BINDING         111..116
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00146"
FT   BINDING         135..137
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         170
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"
FT   BINDING         180
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00146"
SQ   SEQUENCE   188 AA;  21224 MW;  4AB0271298BE1140 CRC64;
     MSIKSDKWIR RMAQEHGMIE PFVERQVRTE GSERLISYGV SSYGYDVRCA DEFKVFTNIH
     SATVDPKNFD EKSFVDVKGP VCIIPPNSFA LARTVEYFRI PRDVLTICLG KSTYARCGII
     VNVTPLEPEW EGHVTLEFSN TTTLPAKIYA NEGVAQMLFL QSDEPCEVSY RDRGGKYQGQ
     TGVTLPRA
//
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