AC   MF_00146;
DC   Protein; auto
TR   HAMAP; MF_00146; -; 1; level=0
XX
Names: dCTP_deaminase
XX
case <FTTag:bifunc1> and <FTTag:bifunc2>
ID   DCDB
DE   RecName: Full=dCTP deaminase, dUMP-forming;
DE            EC=3.5.4.30;
DE   AltName: Full=Bifunctional dCTP deaminase:dUTPase;
DE   AltName: Full=DCD-DUT;
else
ID   DCD
DE   RecName: Full=dCTP deaminase;
DE            EC=3.5.4.13;
DE   AltName: Full=Deoxycytidine triphosphate deaminase;
end case
GN   Name=dcd;
XX
case <FTTag:bifunc1> and <FTTag:bifunc2>
CC   -!- FUNCTION: Bifunctional enzyme that catalyzes both the deamination of
CC       dCTP to dUTP and the hydrolysis of dUTP to dUMP without releasing the
CC       toxic dUTP intermediate.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dCTP + 2 H2O = diphosphate + dUMP + NH4(+);
CC         Xref=Rhea:RHEA:19205, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:61481, ChEBI:CHEBI:246422;
CC         EC=3.5.4.30;
CC   -!- PATHWAY: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP: step
CC       1/1.
else
CC   -!- FUNCTION: Catalyzes the deamination of dCTP to dUTP.
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   -!- PATHWAY: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP
CC       route): step 1/2.
end case
CC   -!- SUBUNIT: Homotrimer.
CC   -!- SIMILARITY: Belongs to the dCTP deaminase family.
XX
DR   Pfam; PF00692; dUTPase; 1; trigger=no
DR   NCBIfam; TIGR02274; dCTP_deam; 1; trigger=no
XX
KW   Hydrolase
KW   Nucleotide metabolism
KW   Nucleotide-binding
XX
case <FTTag:bifunc1> and <FTTag:bifunc2>
GO   GO:0033973; F:dCTP deaminase (dUMP-forming) activity
GO   GO:0006226; P:dUMP biosynthetic process
else
GO   GO:0008829; F:dCTP deaminase activity
GO   GO:0006229; P:dUTP biosynthetic process
end case
XX
FT   From: DCDB_MYCTU (P9WP17)
FT   BINDING         101..106
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT   Optional; Condition: [KR]-S-[ST]-x-[GA]-R
FT   BINDING         127..129
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT   Optional; Condition: [TV]-L-E
FT   ACT_SITE        129
FT                   /note="Proton donor/acceptor"
FT   Condition: E
FT   BINDING         119
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT   Optional; Condition: D
FT   BINDING         148
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT   Tag: bifunc1; Optional; Condition: Q
FT   BINDING         162
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT   Optional; Condition: Y
FT   BINDING         170
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT   Optional; Condition: K
FT   BINDING         174
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT   Optional; Condition: Q
FT   SITE            116..117
FT                   /note="Important for bifunctional activity"
FT   Tag: bifunc2; Optional; Condition: G-[FWY]
XX
Size: 154-240;
Related: MF_00635;
Template: P28248; Q57872; P9WP17; Q9KFV3;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: Known bifunctional enzymes contain a Gly in position 116 (M.tuberculosis numbering),
 a Phe/Trp in position 117 and a Gln in position 148 (see PubMed:15539408 and PubMed:18164314).
XX
# Revision 1.25 2023/06/01
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