(data stored in SCRATCH3701 zone)

SWISSPROT: DCD_RICTY

ID   DCD_RICTY               Reviewed;         188 AA.
AC   Q68XU3;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   11-DEC-2019, entry version 82.
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=RT0063;
OS   Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=257363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-144 / Wilmington;
RX   PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA   McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA   McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA   Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA   Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT   of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(2004).
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}.
DR   EMBL; AE017197; AAU03549.1; -; Genomic_DNA.
DR   RefSeq; WP_011190536.1; NC_006142.1.
DR   SMR; Q68XU3; -.
DR   STRING; 257363.RT0063; -.
DR   EnsemblBacteria; AAU03549; AAU03549; RT0063.
DR   KEGG; rty:RT0063; -.
DR   eggNOG; ENOG4105DHP; Bacteria.
DR   eggNOG; COG0717; LUCA.
DR   HOGENOM; HOG000228600; -.
DR   KO; K01494; -.
DR   OMA; FENHRYP; -.
DR   OrthoDB; 1598407at2; -.
DR   BioCyc; RTYP257363:G1G0L-64-MONOMER; -.
DR   UniPathway; UPA00610; UER00665.
DR   Proteomes; UP000000604; 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;
DR   PRODOM; Q68XU3.
DR   SWISS-2DPAGE; Q68XU3.
KW   Hydrolase; Nucleotide metabolism; Nucleotide-binding.
FT   CHAIN           1..188
FT                   /note="dCTP deaminase"
FT                   /id="PRO_0000274886"
FT   NP_BIND         111..116
FT                   /note="dCTP binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT   NP_BIND         135..137
FT                   /note="dCTP binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT   ACT_SITE        137
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT   BINDING         156
FT                   /note="dCTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT   BINDING         170
FT                   /note="dCTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT   BINDING         179
FT                   /note="dCTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT   BINDING         180
FT                   /note="dCTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
SQ   SEQUENCE   188 AA;  21345 MW;  034B81A961394DD2 CRC64;
     MTIMSDKWIK DAVIKQSMIR PFAEKQVRVH NKEKIISYGL SSYGYDARVS NEFKIFTNIN
     STTVDPKNFS EDNLVDREVD ECIIPPNSFA LGRTIEYFKI PRDVLVICVG KSTYARCGII
     VNVTPLEPEW EGHVTLEFSN TTPLPAKIYA NEGACQFLFL KSDQICDTSY AERQGKYMKQ
     VGVTLPLT
//

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