(data stored in SCRATCH zone)

SWISSPROT: E3J623_FRAIE

ID   E3J623_FRAIE            Unreviewed;       198 AA.
AC   E3J623;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   08-MAY-2019, entry version 56.
DE   RecName: Full=dCTP deaminase, dUMP-forming {ECO:0000256|HAMAP-Rule:MF_00146};
DE            EC=3.5.4.30 {ECO:0000256|HAMAP-Rule:MF_00146};
DE   AltName: Full=Bifunctional dCTP deaminase:dUTPase {ECO:0000256|HAMAP-Rule:MF_00146};
DE   AltName: Full=DCD-DUT {ECO:0000256|HAMAP-Rule:MF_00146};
GN   Name=dcd {ECO:0000256|HAMAP-Rule:MF_00146};
GN   OrderedLocusNames=FraEuI1c_0226 {ECO:0000313|EMBL:ADP78314.1};
OS   Frankia inefficax (strain DSM 45817 / CECT 9037 / EuI1c).
OC   Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=298654 {ECO:0000313|EMBL:ADP78314.1, ECO:0000313|Proteomes:UP000002484};
RN   [1] {ECO:0000313|EMBL:ADP78314.1, ECO:0000313|Proteomes:UP000002484}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45817 / CECT 9037 / EuI1c
RC   {ECO:0000313|Proteomes:UP000002484};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA   Beauchemin N., Sen A., Sur S.A., Gtari M., Wall L., Tisa L., Woyke T.;
RT   "Complete sequence of Frankia sp. EuI1c.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-Rule:MF_00146};
CC   -!- PATHWAY: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP:
CC       step 1/1. {ECO:0000256|HAMAP-Rule:MF_00146}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000256|HAMAP-Rule:MF_00146,
CC       ECO:0000256|SAAS:SAAS01039256}.
CC   -!- SIMILARITY: Belongs to the dCTP deaminase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00146, ECO:0000256|SAAS:SAAS00909595}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00146}.
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DR   EMBL; CP002299; ADP78314.1; -; Genomic_DNA.
DR   RefSeq; WP_013421437.1; NC_014666.1.
DR   STRING; 298654.FraEuI1c_0226; -.
DR   EnsemblBacteria; ADP78314; ADP78314; FraEuI1c_0226.
DR   KEGG; fri:FraEuI1c_0226; -.
DR   eggNOG; ENOG4105DHP; Bacteria.
DR   eggNOG; COG0717; LUCA.
DR   HOGENOM; HOG000228601; -.
DR   KO; K01494; -.
DR   OMA; GQLCLFR; -.
DR   OrthoDB; 1598407at2; -.
DR   BioCyc; FSP298654:G1GOT-228-MONOMER; -.
DR   UniPathway; UPA00610; UER00667.
DR   Proteomes; UP000002484; 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; E3J623.
DR   SWISS-2DPAGE; E3J623.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002484};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00146,
KW   ECO:0000256|SAAS:SAAS01087242};
KW   Nucleotide metabolism {ECO:0000256|HAMAP-Rule:MF_00146,
KW   ECO:0000256|SAAS:SAAS01087248};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00146,
KW   ECO:0000256|SAAS:SAAS01039263};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002484}.
FT   DOMAIN       70    177       dUTPase. {ECO:0000259|Pfam:PF00692}.
FT   NP_BIND     101    106       dCTP binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_00146}.
FT   NP_BIND     127    129       dCTP binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_00146}.
FT   ACT_SITE    129    129       Proton donor/acceptor.
FT                                {ECO:0000256|HAMAP-Rule:MF_00146}.
FT   BINDING     119    119       dCTP. {ECO:0000256|HAMAP-Rule:MF_00146}.
FT   BINDING     148    148       dCTP. {ECO:0000256|HAMAP-Rule:MF_00146}.
FT   BINDING     162    162       dCTP. {ECO:0000256|HAMAP-Rule:MF_00146}.
FT   BINDING     174    174       dCTP. {ECO:0000256|HAMAP-Rule:MF_00146}.
FT   SITE        116    117       Important for bifunctional activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_00146}.
SQ   SEQUENCE   198 AA;  21590 MW;  27B6EE3E76FD0561 CRC64;
     MLLSDRDIRA EITAGRVCLD PYDPGLIQPS SVDLRLDRAF RVFQNHRYSH IDPAAEQEDL
     TELVAPEGDE PFVLHPGEFV LGSTLEVITL PDDLAGRLEG KSSLGRLGLL THSTAGFIDP
     GFSGHVTLEL SNVATLPIKL WPGMKIGQLC LFRLSSPAEH PYGAAIYGSR YQGQRGPTPS
     RAYRDFTRAA VPPVADQA
//

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