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Database: UniProt
Entry: D0I6V0_GRIHO
LinkDB: D0I6V0_GRIHO
Original site: D0I6V0_GRIHO 
ID   D0I6V0_GRIHO            Unreviewed;       198 AA.
AC   D0I6V0;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   24-JAN-2024, entry version 65.
DE   RecName: Full=dCTP deaminase {ECO:0000256|HAMAP-Rule:MF_00146};
DE            EC=3.5.4.13 {ECO:0000256|HAMAP-Rule:MF_00146};
DE   AltName: Full=Deoxycytidine triphosphate deaminase {ECO:0000256|HAMAP-Rule:MF_00146};
GN   Name=dcd {ECO:0000256|HAMAP-Rule:MF_00146};
GN   ORFNames=VHA_001469 {ECO:0000313|EMBL:EEY72369.1};
OS   Grimontia hollisae CIP 101886.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Grimontia.
OX   NCBI_TaxID=675812 {ECO:0000313|EMBL:EEY72369.1, ECO:0000313|Proteomes:UP000003604};
RN   [1] {ECO:0000313|EMBL:EEY72369.1, ECO:0000313|Proteomes:UP000003604}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 101886 {ECO:0000313|EMBL:EEY72369.1,
RC   ECO:0000313|Proteomes:UP000003604};
RG   Los Alamos National Laboratory (LANL);
RG   National Microbial Pathogen Data Resource (NMPDR);
RA   Saunders E.H., Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C.,
RA   Bruce D., Brettin T.S., Colwell R.R., Huq A., Grim C.J., Hasan N.A.,
RA   Bartels D., Vonstein V.;
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the deamination of dCTP to dUTP.
CC       {ECO:0000256|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:0000256|HAMAP-Rule:MF_00146};
CC   -!- PATHWAY: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP
CC       route): step 1/2. {ECO:0000256|HAMAP-Rule:MF_00146}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000256|HAMAP-Rule:MF_00146}.
CC   -!- SIMILARITY: Belongs to the dCTP deaminase family. {ECO:0000256|HAMAP-
CC       Rule:MF_00146}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00146}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EEY72369.1}.
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DR   EMBL; ADAQ01000011; EEY72369.1; -; Genomic_DNA.
DR   RefSeq; WP_005503311.1; NZ_ADAQ01000011.1.
DR   AlphaFoldDB; D0I6V0; -.
DR   GeneID; 58897171; -.
DR   eggNOG; COG0717; Bacteria.
DR   OrthoDB; 9780956at2; -.
DR   UniPathway; UPA00610; UER00665.
DR   Proteomes; UP000003604; Unassembled WGS sequence.
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; IPR010550; dCTP_deam_bac.
DR   InterPro; IPR011962; dCTP_deaminase.
DR   InterPro; IPR036157; dUTPase-like_sf.
DR   InterPro; IPR033704; dUTPase_trimeric.
DR   NCBIfam; TIGR02274; dCTP_deam; 1.
DR   PANTHER; PTHR42680; DCTP DEAMINASE; 1.
DR   PANTHER; PTHR42680:SF3; DCTP DEAMINASE; 1.
DR   Pfam; PF06559; DCD; 1.
DR   SUPFAM; SSF51283; dUTPase-like; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00146};
KW   Nucleotide metabolism {ECO:0000256|ARBA:ARBA00023080, ECO:0000256|HAMAP-
KW   Rule:MF_00146}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00146};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003604}.
FT   ACT_SITE        138
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00146"
FT   BINDING         110..115
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00146"
FT   BINDING         128
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00146"
FT   BINDING         136..138
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00146"
FT   BINDING         171
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00146"
FT   BINDING         178
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00146"
FT   BINDING         182
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00146"
SQ   SEQUENCE   198 AA;  21940 MW;  37C3865B0B05D0DB CRC64;
     MRLSDKHIRE YLDDGMIAIE PRPSDDAISG VTVDVTLGNQ FRVFTEHCVP FIDLSGPRED
     VSAQLDKVMS DEIELADGEA FFLHPGQLAL AVTHEVVTLP DDIVGWLDGR SSLARLGLMV
     HVTAHRIDPG WQGRIVLEFY NSGRLPLALR PGMPIGALSF EIMSSDAEKP YHKRHNAKYK
     NQQGAVASRI GEDHMNGK
//
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