ID A0A399FY14_9ACTN Unreviewed; 196 AA.
AC A0A399FY14;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=NI17_018535 {ECO:0000313|EMBL:UOE18762.1}, NI17_20885
GN {ECO:0000313|EMBL:RII00356.1};
OS Thermobifida halotolerans.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Thermobifida.
OX NCBI_TaxID=483545 {ECO:0000313|EMBL:RII00356.1};
RN [1] {ECO:0000313|EMBL:RII00356.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44931 {ECO:0000313|EMBL:RII00356.1};
RA Toth A., Tancsics T.A., Farkas T., Papp P., Olasz F., Balint B.,
RA Herczeg R., Nagy I., Baka E., Kukolya J.;
RT "De novo genome project of the cellulose decomposer Thermobifida
RT halotolerans type strain.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:UOE18762.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 44931 {ECO:0000313|EMBL:UOE18762.1};
RA Nagy I., Horvath B., Kukolya J., Nagy I., Orsini M.;
RT "De novo genome project of the cellulose decomposer Thermobifida
RT halotolerans type strain.";
RL Submitted (OCT-2020) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JRUV01000294; RII00356.1; -; Genomic_DNA.
DR EMBL; CP063196; UOE18762.1; -; Genomic_DNA.
DR RefSeq; WP_068691226.1; NZ_LIZN01000008.1.
DR AlphaFoldDB; A0A399FY14; -.
DR STRING; 483545.GCA_001660385_04774; -.
DR OrthoDB; 9780956at2; -.
DR UniPathway; UPA00610; UER00667.
DR Proteomes; UP000265719; 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; 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:UP000265719}.
FT REGION 165..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..185
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 196 AA; 21712 MW; DC09028D6F865C7D CRC64;
MLLSDRDIRA AIESGRVKLD PYDPALIQPS SIDVRLDRYF RVFENHRYPH IDPAVEQPGL
TRLVEPEGDE AFVLHPGEFV LASTYETVTL PDDIASRLEG KSSLGRLGLL THSTAGFIDP
GFSGHVTLEL SNVATLPIKL YPGMKIGQLC MFQLSSPAEH PYGSEACGSR YQGQRGPTPS
RSYRNFARTP VRRGDQ
//
