ID   DCD_BURTA               Reviewed;         189 AA.
AC   Q2T083;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 98.
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};
GN   OrderedLocusNames=BTH_I0860;
OS   Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CCUG 48851 /
OS   CIP 106301 / E264).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=271848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700388 / DSM 13276 / CCUG 48851 / CIP 106301 / E264;
RX   PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA   Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA   DeShazer D.;
RT   "Bacterial genome adaptation to niches: divergence of the potential
RT   virulence genes in three Burkholderia species of different survival
RT   strategies.";
RL   BMC Genomics 6:174-174(2005).
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}.
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DR   EMBL; CP000086; ABC37933.1; -; Genomic_DNA.
DR   RefSeq; WP_009892477.1; NZ_CP008785.1.
DR   PDB; 4DHK; X-ray; 2.05 A; A/B=1-189.
DR   PDBsum; 4DHK; -.
DR   AlphaFoldDB; Q2T083; -.
DR   SMR; Q2T083; -.
DR   GeneID; 66546398; -.
DR   KEGG; bte:BTH_I0860; -.
DR   HOGENOM; CLU_087476_4_0_4; -.
DR   UniPathway; UPA00610; UER00665.
DR   Proteomes; UP000001930; Chromosome I.
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   1: Evidence at protein level;
KW   3D-structure; Hydrolase; Nucleotide metabolism; Nucleotide-binding.
FT   CHAIN           1..189
FT                   /note="dCTP deaminase"
FT                   /id="PRO_1000009695"
FT   ACT_SITE        138
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT   BINDING         112..117
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT   BINDING         136..138
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT   BINDING         157
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT   BINDING         171
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT   BINDING         181
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT   HELIX           6..16
FT                   /evidence="ECO:0007829|PDB:4DHK"
FT   STRAND          19..21
FT                   /evidence="ECO:0007829|PDB:4DHK"
FT   STRAND          24..29
FT                   /evidence="ECO:0007829|PDB:4DHK"
FT   STRAND          35..42
FT                   /evidence="ECO:0007829|PDB:4DHK"
FT   STRAND          45..50
FT                   /evidence="ECO:0007829|PDB:4DHK"
FT   STRAND          52..57
FT                   /evidence="ECO:0007829|PDB:4DHK"
FT   HELIX           72..74
FT                   /evidence="ECO:0007829|PDB:4DHK"
FT   STRAND          75..85
FT                   /evidence="ECO:0007829|PDB:4DHK"
FT   STRAND          89..100
FT                   /evidence="ECO:0007829|PDB:4DHK"
FT   STRAND          105..111
FT                   /evidence="ECO:0007829|PDB:4DHK"
FT   HELIX           113..116
FT                   /evidence="ECO:0007829|PDB:4DHK"
FT   TURN            117..119
FT                   /evidence="ECO:0007829|PDB:4DHK"
FT   STRAND          120..123
FT                   /evidence="ECO:0007829|PDB:4DHK"
FT   STRAND          132..141
FT                   /evidence="ECO:0007829|PDB:4DHK"
FT   STRAND          143..145
FT                   /evidence="ECO:0007829|PDB:4DHK"
FT   STRAND          147..150
FT                   /evidence="ECO:0007829|PDB:4DHK"
FT   STRAND          153..162
FT                   /evidence="ECO:0007829|PDB:4DHK"
SQ   SEQUENCE   189 AA;  21340 MW;  BA0AD2D1FDD169A2 CRC64;
     MSIKSDKWIR RMAEEHKMIE PFVPDQVRAA EDGRRIVSYG TSSYGYDIRC ADEFKIFTNI
     NSTIVDPKNF DEGSFVDFKG DVCIIPPNSF ALARTVEYFR IPRTVLTVCL GKSTYARCGI
     IVNVTPFEPE WEGYVTLEFS NTTPLPAKIY ANEGVAQVLF FESDEVCDVS YADRGGKYQG
     QRGVTLPKT
//