ID   DCDB_HATHI              Reviewed;         172 AA.
AC   Q9ZNJ8;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   13-SEP-2023, entry version 77.
DE   RecName: Full=dCTP deaminase, dUMP-forming {ECO:0000255|HAMAP-Rule:MF_00146};
DE            EC=3.5.4.30 {ECO:0000255|HAMAP-Rule:MF_00146};
DE   AltName: Full=Bifunctional dCTP deaminase:dUTPase {ECO:0000255|HAMAP-Rule:MF_00146};
DE   AltName: Full=DCD-DUT {ECO:0000255|HAMAP-Rule:MF_00146};
GN   Name=dcd {ECO:0000255|HAMAP-Rule:MF_00146};
OS   Hathewaya histolytica (Clostridium histolyticum).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; Hathewaya.
OX   NCBI_TaxID=1498;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 19401 / DSM 2158 / JCM 1403 / NCIMB 503 / NCTC 503;
RX   PubMed=9922257; DOI=10.1128/jb.181.3.923-933.1999;
RA   Matsushita O., Jung C.-M., Katayama S., Minami J., Takahashi Y., Okabe A.;
RT   "Gene duplication and multiplicity of collagenases in Clostridium
RT   histolyticum.";
RL   J. Bacteriol. 181:923-933(1999).
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. {ECO:0000255|HAMAP-Rule:MF_00146}.
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; Evidence={ECO:0000255|HAMAP-Rule:MF_00146};
CC   -!- PATHWAY: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP: step
CC       1/1. {ECO:0000255|HAMAP-Rule:MF_00146}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_00146}.
CC   -!- SIMILARITY: Belongs to the dCTP deaminase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00146}.
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DR   EMBL; AB014075; BAA34543.1; -; Genomic_DNA.
DR   PIR; T44356; T44356.
DR   AlphaFoldDB; Q9ZNJ8; -.
DR   SMR; Q9ZNJ8; -.
DR   OrthoDB; 9780202at2; -.
DR   UniPathway; UPA00610; UER00667.
DR   GO; GO:0033973; F:dCTP deaminase (dUMP-forming) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008829; F:dCTP deaminase activity; IEA:InterPro.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0006226; P:dUMP biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006229; P:dUTP biosynthetic process; IEA:InterPro.
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; Nucleotide metabolism; Nucleotide-binding.
FT   CHAIN           1..172
FT                   /note="dCTP deaminase, dUMP-forming"
FT                   /id="PRO_0000155980"
FT   ACT_SITE        121
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT   BINDING         93..98
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT   BINDING         111
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT   BINDING         119..121
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT   BINDING         138
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT   BINDING         151
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT   SITE            108..109
FT                   /note="Important for bifunctional activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
SQ   SEQUENCE   172 AA;  19919 MW;  520A07EF3ED0C7E3 CRC64;
     MILSGKEIKN RLNKDIFIEP FSDNQLNPNS YNLRLHNELL VYENNVLDMK KENKAKKITI
     PEEGLLLEPG KLYLGRTIEH TRTEKLVPML EGRSSVGRLG LFIHITAGFG DIGFSGFWTL
     EIFCVQPIRI YPNIEICQIY YHNIEGEYEK YTSGKYQNNT GVQPSLLFKD FE
//