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Database: UniProt
Entry: A0A243RAR1_9ACTN
LinkDB: A0A243RAR1_9ACTN
Original site: A0A243RAR1_9ACTN 
ID   A0A243RAR1_9ACTN        Unreviewed;       191 AA.
AC   A0A243RAR1;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
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=CA983_39170 {ECO:0000313|EMBL:OUC91743.1};
OS   Streptomyces swartbergensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=487165 {ECO:0000313|EMBL:OUC91743.1, ECO:0000313|Proteomes:UP000195105};
RN   [1] {ECO:0000313|EMBL:OUC91743.1, ECO:0000313|Proteomes:UP000195105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HMC13 {ECO:0000313|EMBL:OUC91743.1};
RA   Le Roes-Hill M., Prins A., Durrell K.A.;
RT   "Biotechnological potential of actinobacteria isolated from South African
RT   environments.";
RL   Submitted (MAY-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: 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:OUC91743.1}.
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DR   EMBL; NGFN01000441; OUC91743.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A243RAR1; -.
DR   UniPathway; UPA00610; UER00667.
DR   Proteomes; UP000195105; 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..179
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         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;  21439 MW;  0DD3E0939EA2E454 CRC64;
     MLLSDKDIRA EIDAGRVRID PYDDAMVQPS SIDVRLDRYF RVFENHRYPH IDPSIEQADL
     TRLVEPEGDE PFILHPGEFV LASTYEVISL PDDLASRLEG KSSLGRLGLV THSTAGFIDP
     GFSGHVTLEL SNLATLPIKL WPGMKIGQLC MFRLSSPADF PYGSERYGSR YQGQRGPTAS
     RSFLNFHRSQ V
//
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