DCD_ACIB5
ID DCD_ACIB5 Reviewed; 189 AA.
AC B7I774;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=AB57_0835;
OS Acinetobacter baumannii (strain AB0057).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=480119;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AB0057;
RX PubMed=18931120; DOI=10.1128/jb.00834-08;
RA Adams M.D., Goglin K., Molyneaux N., Hujer K.M., Lavender H., Jamison J.J.,
RA MacDonald I.J., Martin K.M., Russo T., Campagnari A.A., Hujer A.M.,
RA Bonomo R.A., Gill S.R.;
RT "Comparative genome sequence analysis of multidrug-resistant Acinetobacter
RT baumannii.";
RL J. Bacteriol. 190:8053-8064(2008).
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; CP001182; ACJ40633.1; -; Genomic_DNA.
DR RefSeq; WP_000985728.1; NC_011586.2.
DR AlphaFoldDB; B7I774; -.
DR SMR; B7I774; -.
DR GeneID; 60876998; -.
DR GeneID; 66398272; -.
DR KEGG; abn:AB57_0835; -.
DR HOGENOM; CLU_087476_4_0_6; -.
DR OMA; FENHRYP; -.
DR UniPathway; UPA00610; UER00665.
DR Proteomes; UP000007094; 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.
FT CHAIN 1..189
FT /note="dCTP deaminase"
FT /id="PRO_1000189821"
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"
SQ SEQUENCE 189 AA; 21442 MW; 80F7A026AC9D7CF8 CRC64;
MAIKSDRWIR EMSEKHGMIE PYAENQVRFD KNGEKLISYG VSSYGYDVRC AREFKVFTNV
HSAIVDPKNF DEKSFIDIES DVCIIPPNSF ALARTIEYFR IPRNVLTVCL GKSTYARCGI
IVNVTPLEPE WEGHVTLEFS NTTNLPARIY AGEGVAQMLF FESDEVCETS YKDRGGKYQG
QTGVTLPKT
