ID A0A329ZV32_9HELI Unreviewed; 185 AA.
AC A0A329ZV32;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
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=CCZ01_03505 {ECO:0000313|EMBL:RAX58152.1};
OS Helicobacter sp. 15-1451.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=2004995 {ECO:0000313|EMBL:RAX58152.1, ECO:0000313|Proteomes:UP000251881};
RN [1] {ECO:0000313|EMBL:RAX58152.1, ECO:0000313|Proteomes:UP000251881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=15-1451 {ECO:0000313|EMBL:RAX58152.1,
RC ECO:0000313|Proteomes:UP000251881};
RX PubMed=29225701; DOI=10.1186/s13099-017-0220-y;
RA Feng Y., Mannion A., Madden C.M., Swennes A.G., Townes C., Byrd C.,
RA Marini R.P., Fox J.G.;
RT "Cytotoxic Escherichia coli strains encoding colibactin and cytotoxic
RT necrotizing factor (CNF) colonize laboratory macaques.";
RL Gut Pathog. 9:71-71(2017).
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:RAX58152.1}.
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DR EMBL; NHYN01000005; RAX58152.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A329ZV32; -.
DR OrthoDB; 9780956at2; -.
DR UniPathway; UPA00610; UER00665.
DR Proteomes; UP000251881; 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:UP000251881}.
FT DOMAIN 76..179
FT /note="dUTPase-like"
FT /evidence="ECO:0000259|Pfam:PF00692"
FT ACT_SITE 133
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00146"
FT BINDING 107..112
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00146"
FT BINDING 152
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00146"
FT BINDING 166
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00146"
FT BINDING 172
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00146"
FT BINDING 176
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00146"
SQ SEQUENCE 185 AA; 20607 MW; 51DAFDE5AD5419BF CRC64;
MGLKEDLWIQ EQSLKHGMIE PFCDAQVGIG VVSYGLSSYG YDIRVSNEFK IFTNINATVV
DPKNFQATNA VDFCGDECIV PPNSFALART IEYFRIPRNV LAICLGKSTY ARCGIIVNVT
PFEPEFEGFI TIEISNTTPL PAKIYANEGI AQVLFFEGDN PCQTSYKDKN GKYQKQQGIT
LPKIL
//
