(data stored in ACNUC7421 zone)

SWISSPROT: DCDB_FRASN

ID   DCDB_FRASN              Reviewed;         201 AA.
AC   A8LDU1;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   08-MAY-2019, entry version 71.
DE   RecName: Full=dCTP deaminase, dUMP-forming {ECO:0000255|HAMAP-Rule:MF_00146};
DE            EC=3.5.4.30 {ECO:0000255|HAMAP-Rule:MF_00146};
DE   AltName: Full=Bifunctional dCTP deaminase:dUTPase {ECO:0000255|HAMAP-Rule:MF_00146};
DE   AltName: Full=DCD-DUT {ECO:0000255|HAMAP-Rule:MF_00146};
GN   Name=dcd {ECO:0000255|HAMAP-Rule:MF_00146};
GN   OrderedLocusNames=Franean1_0239;
OS   Frankia sp. (strain EAN1pec).
OC   Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=298653;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EAN1pec;
RX   PubMed=17151343; DOI=10.1101/gr.5798407;
RA   Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA   Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N.,
RA   Couloux A., Cournoyer B., Cruveiller S., Daubin V., Demange N.,
RA   Francino M.P., Goltsman E., Huang Y., Kopp O.R., Labarre L.,
RA   Lapidus A., Lavire C., Marechal J., Martinez M., Mastronunzio J.E.,
RA   Mullin B.C., Niemann J., Pujic P., Rawnsley T., Rouy Z.,
RA   Schenowitz C., Sellstedt A., Tavares F., Tomkins J.P., Vallenet D.,
RA   Valverde C., Wall L.G., Wang Y., Medigue C., Benson D.R.;
RT   "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT   reflect host range and host plant biogeography.";
RL   Genome Res. 17:7-15(2007).
CC   -!- FUNCTION: Bifunctional enzyme that catalyzes both the deamination
CC       of dCTP to dUTP and the hydrolysis of dUTP to dUMP without
CC       releasing the toxic dUTP intermediate. {ECO:0000255|HAMAP-
CC       Rule:MF_00146}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dCTP + 2 H2O = diphosphate + dUMP + NH4(+);
CC         Xref=Rhea:RHEA:19205, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:61481, ChEBI:CHEBI:246422;
CC         EC=3.5.4.30; Evidence={ECO:0000255|HAMAP-Rule:MF_00146};
CC   -!- PATHWAY: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP:
CC       step 1/1. {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; CP000820; ABW09706.1; -; Genomic_DNA.
DR   RefSeq; WP_012157683.1; NC_009921.1.
DR   SMR; A8LDU1; -.
DR   STRING; 298653.Franean1_0239; -.
DR   EnsemblBacteria; ABW09706; ABW09706; Franean1_0239.
DR   KEGG; fre:Franean1_0239; -.
DR   eggNOG; ENOG4105DHP; Bacteria.
DR   eggNOG; COG0717; LUCA.
DR   HOGENOM; HOG000228601; -.
DR   KO; K01494; -.
DR   OMA; GQLCLFR; -.
DR   OrthoDB; 1598407at2; -.
DR   BioCyc; FSP298653:G1G9X-228-MONOMER; -.
DR   UniPathway; UPA00610; UER00667.
DR   Proteomes; UP000001313; Chromosome.
DR   GO; GO:0033973; F:dCTP deaminase (dUMP-forming) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008829; F:dCTP deaminase activity; IEA:InterPro.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0006226; P:dUMP biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006229; P:dUTP biosynthetic process; IEA:InterPro.
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; A8LDU1.
DR   SWISS-2DPAGE; A8LDU1.
KW   Complete proteome; Hydrolase; Nucleotide metabolism;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN         1    201       dCTP deaminase, dUMP-forming.
FT                                /FTId=PRO_1000096426.
FT   NP_BIND     101    106       dCTP binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00146}.
FT   NP_BIND     127    129       dCTP binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00146}.
FT   ACT_SITE    129    129       Proton donor/acceptor.
FT                                {ECO:0000255|HAMAP-Rule:MF_00146}.
FT   BINDING     119    119       dCTP. {ECO:0000255|HAMAP-Rule:MF_00146}.
FT   BINDING     148    148       dCTP. {ECO:0000255|HAMAP-Rule:MF_00146}.
FT   BINDING     162    162       dCTP. {ECO:0000255|HAMAP-Rule:MF_00146}.
FT   BINDING     174    174       dCTP. {ECO:0000255|HAMAP-Rule:MF_00146}.
FT   SITE        116    117       Important for bifunctional activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_00146}.
SQ   SEQUENCE   201 AA;  22015 MW;  16D858AC3E5128EF CRC64;
     MLLSDRDIRA EITAGRVRLD PYDEGLIQPS SVDLRLDRAF RVFQNHRYSH IDPAVEQEDL
     TELVAPEGDE PFVLHPGEFV LGSTLEVVTL PEDLAGRLEG KSSLGRLGLL THSTAGFIDP
     GFSGHVTLEL SNVATLPIKL WPGMKIGQLC LFRLSTPAEH PYGSAIYGSR YQGQRGPTPS
     RAYRDFTRAA VPEIPNGSHG A
//

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