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DCD_HELHP
ID   DCD_HELHP               Reviewed;         188 AA.
AC   Q7VJQ0;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2004, sequence version 2.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=dCTP deaminase {ECO:0000255|HAMAP-Rule:MF_00146};
DE            EC=3.5.4.13 {ECO:0000255|HAMAP-Rule:MF_00146};
DE   AltName: Full=Deoxycytidine triphosphate deaminase {ECO:0000255|HAMAP-Rule:MF_00146};
GN   Name=dcd {ECO:0000255|HAMAP-Rule:MF_00146}; OrderedLocusNames=HH_0193;
OS   Helicobacter hepaticus (strain ATCC 51449 / 3B1).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=235279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51449 / 3B1;
RX   PubMed=12810954; DOI=10.1073/pnas.1332093100;
RA   Suerbaum S., Josenhans C., Sterzenbach T., Drescher B., Brandt P., Bell M.,
RA   Droege M., Fartmann B., Fischer H.-P., Ge Z., Hoerster A., Holland R.,
RA   Klein K., Koenig J., Macko L., Mendz G.L., Nyakatura G., Schauer D.B.,
RA   Shen Z., Weber J., Frosch M., Fox J.G.;
RT   "The complete genome sequence of the carcinogenic bacterium Helicobacter
RT   hepaticus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7901-7906(2003).
CC   -!- FUNCTION: Catalyzes the deamination of dCTP to dUTP.
CC       {ECO:0000255|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:0000255|HAMAP-Rule:MF_00146};
CC   -!- PATHWAY: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP
CC       route): step 1/2. {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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAP76790.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE017125; AAP76790.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_011115036.1; NC_004917.1.
DR   AlphaFoldDB; Q7VJQ0; -.
DR   SMR; Q7VJQ0; -.
DR   STRING; 235279.HH_0193; -.
DR   EnsemblBacteria; AAP76790; AAP76790; HH_0193.
DR   KEGG; hhe:HH_0193; -.
DR   eggNOG; COG0717; Bacteria.
DR   HOGENOM; CLU_087476_4_0_7; -.
DR   OMA; FENHRYP; -.
DR   OrthoDB; 1598407at2; -.
DR   UniPathway; UPA00610; UER00665.
DR   Proteomes; UP000002495; 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   Pfam; PF00692; dUTPase; 1.
DR   SUPFAM; SSF51283; SSF51283; 1.
DR   TIGRFAMs; TIGR02274; dCTP_deam; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Nucleotide metabolism; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..188
FT                   /note="dCTP deaminase"
FT                   /id="PRO_0000155989"
FT   ACT_SITE        135
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT   BINDING         109..114
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT   BINDING         154
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT   BINDING         168
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT   BINDING         178
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
SQ   SEQUENCE   188 AA;  21035 MW;  36DF8367FF42C491 CRC64;
     MGLKSDTWIK KMSKKGMIEP FCEKQVGKNI VSYGLSSYGY DIRVGNEFMI FTNIGANLVD
     PKSFDERNVV EITTEENGYC LVPPNSFALA RTIEYFRIPR NVLAICLGKS TYARCGIIVN
     VTPFEPEFEG HITIEISNTT PLPAKIYANE GIAQVLFLEG DETCEVSYKD KKGKYQGQKG
     ITLPKVIK
 
 
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