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Database: UniProt
Entry: A0A0F3MHI1_9RICK
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Original site: A0A0F3MHI1_9RICK 
ID   A0A0F3MHI1_9RICK        Unreviewed;       188 AA.
AC   A0A0F3MHI1;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   13-SEP-2023, entry version 35.
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   ECO:0000313|EMBL:KJV55205.1};
GN   ORFNames=OCHUTO_0933 {ECO:0000313|EMBL:KJV55205.1};
OS   Orientia chuto str. Dubai.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Orientia.
OX   NCBI_TaxID=1359168 {ECO:0000313|EMBL:KJV55205.1, ECO:0000313|Proteomes:UP000033616};
RN   [1] {ECO:0000313|EMBL:KJV55205.1, ECO:0000313|Proteomes:UP000033616}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fuller {ECO:0000313|EMBL:KJV55205.1,
RC   ECO:0000313|Proteomes:UP000033616};
RA   Daugherty S.C., Su Q., Abolude K., Beier-Sexton M., Carlyon J.A.,
RA   Carter R., Day N.P., Dumler S.J., Dyachenko V., Godinez A., Kurtti T.J.,
RA   Lichay M., Mullins K.E., Ott S., Pappas-Brown V., Paris D.H., Patel P.,
RA   Richards A.L., Sadzewicz L., Sears K., Seidman D., Sengamalay N.,
RA   Stenos J., Tallon L.J., Vincent G., Fraser C.M., Munderloh U.,
RA   Dunning-Hotopp J.C.;
RT   "Genome Sequencing of Rickettsiales.";
RL   Submitted (FEB-2015) 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:KJV55205.1}.
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DR   EMBL; LANP01000026; KJV55205.1; -; Genomic_DNA.
DR   RefSeq; WP_045797528.1; NZ_LANP01000026.1.
DR   AlphaFoldDB; A0A0F3MHI1; -.
DR   STRING; 1359168.OCHUTO_0933; -.
DR   PATRIC; fig|1359168.3.peg.665; -.
DR   OrthoDB; 9780956at2; -.
DR   UniPathway; UPA00610; UER00665.
DR   Proteomes; UP000033616; 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; IPR011962; dCTP_deaminase.
DR   InterPro; IPR029054; dUTPase-like.
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; PF00692; dUTPase; 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:UP000033616}.
FT   DOMAIN          82..179
FT                   /note="dUTPase-like"
FT                   /evidence="ECO:0000259|Pfam:PF00692"
FT   ACT_SITE        137
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00146"
FT   BINDING         111..116
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00146"
FT   BINDING         135..137
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00146"
FT   BINDING         156
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00146"
FT   BINDING         170
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00146"
FT   BINDING         180
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00146"
SQ   SEQUENCE   188 AA;  21112 MW;  C81D9F0C5FC0D2F8 CRC64;
     MSIMSDNWIK KMAESENMIS PFIDKQVRTH NNQQILSYGL SSYGYDARVS NEFKIFTNTK
     PSVIDPKKFD QDCLITKITD ICIIPPNSFA LGATIEYFKM PRDVIAICIG KSTYARCGII
     VNITPLEPEC EGHITLEFSN TTPLPAKIYA GEGACQFLFF KGEQPCNTSY IDRNGRYTKQ
     IGVTLPTV
//
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