ID A0A0A1DP35_NOCSI Unreviewed; 191 AA.
AC A0A0A1DP35;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 48.
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 ECO:0000313|EMBL:GEB14913.1};
GN ORFNames=KR76_24160 {ECO:0000313|EMBL:AIY19099.1}, NSI01_32280
GN {ECO:0000313|EMBL:GEB14913.1};
OS Nocardioides simplex (Arthrobacter simplex).
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Pimelobacter.
OX NCBI_TaxID=2045 {ECO:0000313|EMBL:AIY19099.1, ECO:0000313|Proteomes:UP000030300};
RN [1] {ECO:0000313|EMBL:AIY19099.1, ECO:0000313|Proteomes:UP000030300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM Ac-2033D {ECO:0000313|EMBL:AIY19099.1,
RC ECO:0000313|Proteomes:UP000030300};
RX PubMed=25573942;
RA Shtratnikova V.Y., Schelkunov M.I., Pekov Y.A., Fokina V.V.,
RA Logacheva M.D., Sokolov S.L., Bragin E.Y., Ashapkin V.V., Donova M.V.;
RT "Complete Genome Sequence of Steroid-Transforming Nocardioides simplex VKM
RT Ac-2033D.";
RL Genome Announc. 3:0-0(2015).
RN [2] {ECO:0000313|EMBL:GEB14913.1, ECO:0000313|Proteomes:UP000318936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 12069 {ECO:0000313|EMBL:GEB14913.1,
RC ECO:0000313|Proteomes:UP000318936};
RA Hosoyama A., Uohara A., Ohji S., Ichikawa N.;
RT "Whole genome shotgun sequence of Pimelobacter simplex NBRC 12069.";
RL Submitted (JUN-2019) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00146}.
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DR EMBL; CP009896; AIY19099.1; -; Genomic_DNA.
DR EMBL; BJMC01000015; GEB14913.1; -; Genomic_DNA.
DR RefSeq; WP_038681997.1; NZ_WBVM01000001.1.
DR AlphaFoldDB; A0A0A1DP35; -.
DR STRING; 2045.KR76_24160; -.
DR KEGG; psim:KR76_24160; -.
DR eggNOG; COG0717; Bacteria.
DR HOGENOM; CLU_087476_2_0_11; -.
DR UniPathway; UPA00610; UER00667.
DR Proteomes; UP000030300; Chromosome.
DR Proteomes; UP000318936; 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; 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:UP000030300}.
FT REGION 161..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 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 191 AA; 21174 MW; 6EA5A572BA75E7FB CRC64;
MLLSDRDITA EIDAGRIALE PYEPSMLQPS SIDVRLDRFF RVFDNHKYPS IDPAADQSDL
TRVVEPEGDE PFILHPGEFV LGSTYEVVTL PDDIAARVEG KSSLGRLGLL THATAGFVDP
GFSGHVTLEL ANVATLPIKL YPGMKIGQFC FFRLTSPSEH PYGSEKYGSR YQGQRGPTPS
RSFQNFHRTS I
//
