ID A0A1Z4ECL2_9MYCO Unreviewed; 190 AA.
AC A0A1Z4ECL2;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 24-JAN-2024, entry version 32.
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:BAX90697.1};
GN ORFNames=B2J96_01105 {ECO:0000313|EMBL:PRI17091.1}, MSG_00533
GN {ECO:0000313|EMBL:BAX90697.1};
OS Mycobacterium shigaense.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium simiae complex.
OX NCBI_TaxID=722731 {ECO:0000313|EMBL:BAX90697.1, ECO:0000313|Proteomes:UP000217736};
RN [1] {ECO:0000313|EMBL:PRI17091.1, ECO:0000313|Proteomes:UP000239044}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UN-152 {ECO:0000313|EMBL:PRI17091.1,
RC ECO:0000313|Proteomes:UP000239044};
RA Yoshida M., Fukano H., Hoshino Y.;
RT "Draft genome sequence of Mycobacterium shigaense sp. nov.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000217736}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UN-152 {ECO:0000313|Proteomes:UP000217736};
RA Fukano H., Yoshida M., Kazumi Y., Ogura Y., Mitarai S., Hayashi T.,
RA Hoshino Y.;
RT "Complete Genome Sequence of Mycobacterium shigaense.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:BAX90697.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCM 32072 {ECO:0000313|EMBL:BAX90697.1};
RA Yoshida M., Fukano H., Ogura Y., Kazumi Y., Mitarai S., Hayashi T.,
RA Hoshino Y.;
RT "Complete Genome Sequence of Mycobacterium shigaense.";
RL Genome Announc. 6:e00552-18(2018).
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}.
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DR EMBL; AP018164; BAX90697.1; -; Genomic_DNA.
DR EMBL; MWON01000001; PRI17091.1; -; Genomic_DNA.
DR KEGG; mshg:MSG_00533; -.
DR OrthoDB; 9780956at2; -.
DR UniPathway; UPA00610; UER00667.
DR Proteomes; UP000217736; Chromosome.
DR Proteomes; UP000239044; 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 69..178
FT /note="dUTPase-like"
FT /evidence="ECO:0000259|Pfam:PF00692"
FT REGION 161..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..190
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 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 190 AA; 20666 MW; 819FFB53EBC28E27 CRC64;
MLLSDRDLRA EITAGRLGID PFDDTLVQPS SIDVRLDCMF RVFNNTRYTH IDPAKQQDEL
TTLVEPAAGE PFVLHPGEFV LGSTLELITL PDDLAGRLEG KSSLGRLGLL THSTAGFIDP
GFSGHITLEL SNVANLPITL WPGMKIGQLC ILRLTSAAEH PYGSSRAGSK YQGQRGPTPS
RSYQNFISST
//