(data stored in ACNUC29543 zone)

SWISSPROT: DCD_ACIBT

ID   DCD_ACIBT               Reviewed;         189 AA.
AC   A3M2T0;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   08-MAY-2019, entry version 77.
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=A1S_0784;
OS   Acinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 /
OS   NCDC KC755 / 5377).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter;
OC   Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=400667;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377;
RX   PubMed=17344419; DOI=10.1101/gad.1510307;
RA   Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N.,
RA   Gerstein M., Snyder M.;
RT   "New insights into Acinetobacter baumannii pathogenesis revealed by
RT   high-density pyrosequencing and transposon mutagenesis.";
RL   Genes Dev. 21:601-614(2007).
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
CC       (dUTP 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.
CC       {ECO:0000255|HAMAP-Rule:MF_00146}.
DR   EMBL; CP000521; ABO11224.2; -; Genomic_DNA.
DR   SMR; A3M2T0; -.
DR   EnsemblBacteria; ABO11224; ABO11224; A1S_0784.
DR   KEGG; acb:A1S_0784; -.
DR   HOGENOM; HOG000228600; -.
DR   KO; K01494; -.
DR   UniPathway; UPA00610; UER00665.
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;
DR   PRODOM; A3M2T0.
DR   SWISS-2DPAGE; A3M2T0.
KW   Hydrolase; Nucleotide metabolism; Nucleotide-binding.
FT   CHAIN         1    189       dCTP deaminase.
FT                                /FTId=PRO_1000096400.
FT   NP_BIND     112    117       dCTP binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00146}.
FT   NP_BIND     136    138       dCTP binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00146}.
FT   ACT_SITE    138    138       Proton donor/acceptor.
FT                                {ECO:0000255|HAMAP-Rule:MF_00146}.
FT   BINDING     157    157       dCTP. {ECO:0000255|HAMAP-Rule:MF_00146}.
FT   BINDING     171    171       dCTP. {ECO:0000255|HAMAP-Rule:MF_00146}.
FT   BINDING     181    181       dCTP. {ECO:0000255|HAMAP-Rule:MF_00146}.
SQ   SEQUENCE   189 AA;  21456 MW;  D118A026AC9D7CEE CRC64;
     MAIKSDRWIR EMSEKHGMIE PYAENQVRFD KNGEKLISYG VSSYGYDVRC AREFKVFTNV
     HSAIVDPKNF DEKSFIDIES DVCIIPPNSF ALARTIEYFR IPRNVLTVCL GKSTYARCGI
     IVNVTPLEPE WEGHVTLEFS NTTNLPARIY AGEGVAQMLF FESDEICETS YKDRGGKYQG
     QTGVTLPKT
//

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