ID   DCDB_METST              Reviewed;         197 AA.
AC   Q2NFH1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   27-MAR-2024, entry version 93.
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};
GN   OrderedLocusNames=Msp_1048;
OS   Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 /
OS   MCB-3).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanosphaera.
OX   NCBI_TaxID=339860;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3;
RX   PubMed=16385054; DOI=10.1128/jb.188.2.642-658.2006;
RA   Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H., Hedderich R.,
RA   Gottschalk G., Thauer R.K.;
RT   "The genome sequence of Methanosphaera stadtmanae reveals why this human
RT   intestinal archaeon is restricted to methanol and H2 for methane formation
RT   and ATP synthesis.";
RL   J. Bacteriol. 188:642-658(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; CP000102; ABC57432.1; -; Genomic_DNA.
DR   RefSeq; WP_011406631.1; NC_007681.1.
DR   AlphaFoldDB; Q2NFH1; -.
DR   SMR; Q2NFH1; -.
DR   STRING; 339860.Msp_1048; -.
DR   GeneID; 41325617; -.
DR   KEGG; mst:Msp_1048; -.
DR   eggNOG; arCOG04048; Archaea.
DR   HOGENOM; CLU_087476_2_1_2; -.
DR   OrthoDB; 33242at2157; -.
DR   UniPathway; UPA00610; UER00667.
DR   Proteomes; UP000001931; 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; 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; PF06559; DCD; 1.
DR   Pfam; PF00692; dUTPase; 1.
DR   SUPFAM; SSF51283; dUTPase-like; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Nucleotide metabolism; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..197
FT                   /note="dCTP deaminase, dUMP-forming"
FT                   /id="PRO_1000009755"
FT   ACT_SITE        133
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT   BINDING         105..110
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT   BINDING         123
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT   BINDING         131..133
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT   BINDING         152
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT   BINDING         166
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   BINDING         178
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT   SITE            120..121
FT                   /note="Important for bifunctional activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
SQ   SEQUENCE   197 AA;  22041 MW;  4327E93440A3473D CRC64;
     MAILSDKDIK KYLDEGRIVI DPITNEKQIQ PSSVDLRLGD QFKGFKIITK PYIDPFDNTD
     LESYMSSITV EEDKPFIIHP GEFTLATTYE NVKLPDDIVA RVEGRSSMGR LGITMHVTAG
     YIDPGFEGNI TLEISNIGKM PVALYPGQRV CQIVFETMTS PSEKPYGHED RDSKYMGQTG
     PQVSKIKEDF DIINGGK
//