DCDB_RHOJR
ID DCDB_RHOJR Reviewed; 189 AA.
AC Q0S5R4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=dCTP deaminase, dUMP-forming {ECO:0000255|HAMAP-Rule:MF_00146};
DE EC=3.5.4.30 {ECO:0000255|HAMAP-Rule:MF_00146};
DE AltName: Full=Bifunctional dCTP deaminase:dUTPase {ECO:0000255|HAMAP-Rule:MF_00146};
DE AltName: Full=DCD-DUT {ECO:0000255|HAMAP-Rule:MF_00146};
GN Name=dcd {ECO:0000255|HAMAP-Rule:MF_00146}; OrderedLocusNames=RHA1_ro05342;
OS Rhodococcus jostii (strain RHA1).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX NCBI_TaxID=101510;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHA1;
RX PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA Eltis L.D.;
RT "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT catabolic powerhouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
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:0000255|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:0000255|HAMAP-Rule:MF_00146};
CC -!- PATHWAY: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP: step
CC 1/1. {ECO:0000255|HAMAP-Rule:MF_00146}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_00146}.
CC -!- SIMILARITY: Belongs to the dCTP deaminase family. {ECO:0000255|HAMAP-
CC Rule:MF_00146}.
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DR EMBL; CP000431; ABG97122.1; -; Genomic_DNA.
DR RefSeq; WP_005238072.1; NC_008268.1.
DR AlphaFoldDB; Q0S5R4; -.
DR SMR; Q0S5R4; -.
DR STRING; 101510.RHA1_ro05342; -.
DR EnsemblBacteria; ABG97122; ABG97122; RHA1_ro05342.
DR GeneID; 66784783; -.
DR KEGG; rha:RHA1_ro05342; -.
DR eggNOG; COG0717; Bacteria.
DR HOGENOM; CLU_087476_2_0_11; -.
DR OMA; FENHRYP; -.
DR UniPathway; UPA00610; UER00667.
DR Proteomes; UP000008710; Chromosome.
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 Pfam; PF00692; dUTPase; 1.
DR SUPFAM; SSF51283; SSF51283; 1.
DR TIGRFAMs; TIGR02274; dCTP_deam; 1.
PE 3: Inferred from homology;
KW Hydrolase; Nucleotide metabolism; Nucleotide-binding; Reference proteome.
FT CHAIN 1..189
FT /note="dCTP deaminase, dUMP-forming"
FT /id="PRO_1000009798"
FT ACT_SITE 129
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT BINDING 101..106
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT BINDING 119
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT BINDING 127..129
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT BINDING 148
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT BINDING 162
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT BINDING 174
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT SITE 116..117
FT /note="Important for bifunctional activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
SQ SEQUENCE 189 AA; 20451 MW; 0FAFF7FADB04378C CRC64;
MLLSDRDLRA EISAGRLGID PFDDSMVQPS SVDVRLDSLF RVFNNTRYTH IDPAQRQDEL
TTLVEPAEGE PFVLHPGEFV LGSTLEVCSL PDDLAGRLEG KSSLGRLGLL THSTAGFIDP
GFNGHITLEL SNVANLPITL WPGMKIGQLC LLRLSSAAEH PYGSSAVGSK YQGQRGPTPS
KAYLNFAQS
