ID A0A2A2A276_9CORY Unreviewed; 187 AA.
AC A0A2A2A276;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
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 ORFNames=CKJ84_08340 {ECO:0000313|EMBL:PAT14325.1};
OS Corynebacterium sp. NML 120412.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=2029401 {ECO:0000313|EMBL:PAT14325.1, ECO:0000313|Proteomes:UP000218861};
RN [1] {ECO:0000313|EMBL:PAT14325.1, ECO:0000313|Proteomes:UP000218861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NML 120412 {ECO:0000313|EMBL:PAT14325.1,
RC ECO:0000313|Proteomes:UP000218861};
RA Bernier A.-M., Burdz T., Bernard K.;
RT "Whole genome sequences of 6 clinical strains closest to Corynebacterium
RT imitans.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Bifunctional enzyme that catalyzes both the deamination of
CC dCTP to dUTP and the hydrolysis of dUTP to dUMP without releasing the
CC toxic dUTP intermediate. {ECO:0000256|HAMAP-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: step
CC 1/1. {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: 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:PAT14325.1}.
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DR EMBL; NSGL01000003; PAT14325.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2A276; -.
DR UniPathway; UPA00610; UER00667.
DR Proteomes; UP000218861; Unassembled WGS sequence.
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 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}.
FT DOMAIN 70..178
FT /note="dUTPase-like"
FT /evidence="ECO:0000259|Pfam:PF00692"
FT ACT_SITE 129
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00146"
FT BINDING 101..106
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00146"
FT BINDING 119
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00146"
FT BINDING 127..129
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00146"
FT BINDING 148
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00146"
FT BINDING 162
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 174
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00146"
FT SITE 116..117
FT /note="Important for bifunctional activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00146"
SQ SEQUENCE 187 AA; 20194 MW; AEF63D641150FF40 CRC64;
MLLSDHDIRD AIDSGKLGID PYDAALVQPS SIDVRMDKFF RVFNNSKYTH IDPKLEMPDL
TTAVEVPEGE AFVLHPGEFV LASTLECFTL PADLAGRLEG KSSLGRLGLL THSTAGFIDP
GFSGHITLEL SNVANLPITL WPGMKVGQLA IFNMSSPAEV PYGSGALGSK YQGQRGPTPS
RAYLNFQ
//