ID K9HAW1_9PROT Unreviewed; 196 AA.
AC K9HAW1;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
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=C882_1298 {ECO:0000313|EMBL:EKV27703.1};
OS Caenispirillum salinarum AK4.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Novispirillaceae; Caenispirillum.
OX NCBI_TaxID=1238182 {ECO:0000313|EMBL:EKV27703.1, ECO:0000313|Proteomes:UP000009881};
RN [1] {ECO:0000313|EMBL:EKV27703.1, ECO:0000313|Proteomes:UP000009881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK4 {ECO:0000313|EMBL:EKV27703.1,
RC ECO:0000313|Proteomes:UP000009881};
RX PubMed=23409257;
RA Khatri I., Singh A., Korpole S., Pinnaka A.K., Subramanian S.;
RT "Draft Genome Sequence of an Alphaproteobacterium, Caenispirillum salinarum
RT AK4(T), Isolated from a Solar Saltern.";
RL Genome Announc. 1:E00199-12(2013).
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:EKV27703.1}.
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DR EMBL; ANHY01000018; EKV27703.1; -; Genomic_DNA.
DR RefSeq; WP_009541954.1; NZ_ANHY01000018.1.
DR AlphaFoldDB; K9HAW1; -.
DR STRING; 1238182.C882_1298; -.
DR PATRIC; fig|1238182.3.peg.3512; -.
DR eggNOG; COG0717; Bacteria.
DR OrthoDB; 9780956at2; -.
DR UniPathway; UPA00610; UER00665.
DR Proteomes; UP000009881; 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:UP000009881}.
FT DOMAIN 78..164
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 109..114
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00146"
FT BINDING 127
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 170
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00146"
FT BINDING 177
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00146"
FT BINDING 181
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00146"
SQ SEQUENCE 196 AA; 21878 MW; 526F9357D0CB1ED1 CRC64;
MKLSDTDIWR YLDDGKIQID PLPTQSQVGT MSVDLQLGNW FRSFRPGKAS FVDLAPPEGE
PTANLEELMT TTEVQGNEPF YLHPGDFALG ITIQKVTLPH DLAGRLDGRS SLARLGLMVH
ATAHTIDPGW SGRITLEFFN CGKLPLAMRP GMRICAISFE TLMSPVSKAY AEREQSKYKE
QLMPLPSRIG QERDKD
//
