DCD_BURTA
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 03-AUG-2022, entry version 91.
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=BTH_I0860;
OS Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 /
OS E264).
OC Bacteria; Proteobacteria; 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 / 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 PRIDE; Q2T083; -.
DR EnsemblBacteria; ABC37933; ABC37933; BTH_I0860.
DR GeneID; 66546398; -.
DR KEGG; bte:BTH_I0860; -.
DR HOGENOM; CLU_087476_4_0_4; -.
DR OMA; FENHRYP; -.
DR OrthoDB; 1598407at2; -.
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 Pfam; PF00692; dUTPase; 1.
DR SUPFAM; SSF51283; SSF51283; 1.
DR TIGRFAMs; TIGR02274; dCTP_deam; 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
