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Database: UniProt
Entry: A0A1Z4ECL2_9MYCO
LinkDB: A0A1Z4ECL2_9MYCO
Original site: A0A1Z4ECL2_9MYCO 
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
//
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