ID   DCDB_HALH5              Reviewed;         177 AA.
AC   Q9KFV3;
DT   10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 122.
DE   RecName: Full=dCTP deaminase, dUMP-forming {ECO:0000255|HAMAP-Rule:MF_00146, ECO:0000305};
DE            EC=3.5.4.30 {ECO:0000255|HAMAP-Rule:MF_00146, ECO:0000269|PubMed:25746996};
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   Synonyms=dcdB {ECO:0000303|PubMed:25746996}; OrderedLocusNames=BH0368;
OS   Halalkalibacterium halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS   / JCM 9153 / C-125) (Bacillus halodurans).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC   Halalkalibacterium (ex Joshi et al. 2022).
OX   NCBI_TaxID=272558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA   Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA   Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT   "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT   and genomic sequence comparison with Bacillus subtilis.";
RL   Nucleic Acids Res. 28:4317-4331(2000).
RN   [2] {ECO:0007744|PDB:4XJC}
RP   X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEX WITH TTP, FUNCTION,
RP   CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, SUBUNIT, AND INDUCTION.
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=25746996; DOI=10.1128/aem.00268-15;
RA   Oehlenschlaeger C.B., Lovgreen M.N., Reinauer E., Lehtinen E., Pind M.L.,
RA   Harris P., Martinussen J., Willemoes M.;
RT   "Bacillus halodurans strain C125 encodes and synthesizes enzymes from both
RT   known pathways to form dUMP directly from cytosine deoxyribonucleotides.";
RL   Appl. Environ. Microbiol. 81:3395-3404(2015).
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       ECO:0000269|PubMed:25746996}.
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         ECO:0000269|PubMed:25746996};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:25746996};
CC   -!- ACTIVITY REGULATION: Inhibited by dTTP. {ECO:0000269|PubMed:25746996}.
CC   -!- PATHWAY: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP: step
CC       1/1. {ECO:0000255|HAMAP-Rule:MF_00146, ECO:0000305}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_00146,
CC       ECO:0000269|PubMed:25746996}.
CC   -!- INDUCTION: Repressed by both deoxycytidine and thymidine.
CC       {ECO:0000269|PubMed:25746996}.
CC   -!- SIMILARITY: Belongs to the dCTP deaminase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00146}.
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DR   EMBL; BA000004; BAB04087.1; -; Genomic_DNA.
DR   PIR; H83695; H83695.
DR   RefSeq; WP_010896547.1; NC_002570.2.
DR   PDB; 4XJC; X-ray; 2.35 A; A/B/C/D/E/F=1-177.
DR   PDBsum; 4XJC; -.
DR   AlphaFoldDB; Q9KFV3; -.
DR   SMR; Q9KFV3; -.
DR   STRING; 272558.gene:10726221; -.
DR   KEGG; bha:BH0368; -.
DR   eggNOG; COG0717; Bacteria.
DR   HOGENOM; CLU_087476_2_1_9; -.
DR   OrthoDB; 9780202at2; -.
DR   BRENDA; 3.5.4.13; 661.
DR   BRENDA; 3.5.4.30; 661.
DR   UniPathway; UPA00610; UER00667.
DR   Proteomes; UP000001258; 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   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   1: Evidence at protein level;
KW   3D-structure; Hydrolase; Magnesium; Nucleotide metabolism;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..177
FT                   /note="dCTP deaminase, dUMP-forming"
FT                   /id="PRO_0000155964"
FT   ACT_SITE        125
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P28248, ECO:0000255|HAMAP-
FT                   Rule:MF_00146"
FT   BINDING         98..103
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00146,
FT                   ECO:0000305|PubMed:25746996"
FT   BINDING         110
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000305|PubMed:25746996"
FT   BINDING         115..118
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000305|PubMed:25746996"
FT   BINDING         123..125
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00146,
FT                   ECO:0000305|PubMed:25746996"
FT   BINDING         144
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00146,
FT                   ECO:0000305|PubMed:25746996"
FT   BINDING         157..160
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000305|PubMed:25746996"
FT   BINDING         164
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00146,
FT                   ECO:0000305|PubMed:25746996"
FT   SITE            112..113
FT                   /note="Important for bifunctional activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT   HELIX           5..13
FT                   /evidence="ECO:0007829|PDB:4XJC"
FT   STRAND          16..21
FT                   /evidence="ECO:0007829|PDB:4XJC"
FT   HELIX           24..26
FT                   /evidence="ECO:0007829|PDB:4XJC"
FT   STRAND          32..36
FT                   /evidence="ECO:0007829|PDB:4XJC"
FT   STRAND          38..43
FT                   /evidence="ECO:0007829|PDB:4XJC"
FT   TURN            45..47
FT                   /evidence="ECO:0007829|PDB:4XJC"
FT   STRAND          49..51
FT                   /evidence="ECO:0007829|PDB:4XJC"
FT   STRAND          53..55
FT                   /evidence="ECO:0007829|PDB:4XJC"
FT   STRAND          59..63
FT                   /evidence="ECO:0007829|PDB:4XJC"
FT   STRAND          66..71
FT                   /evidence="ECO:0007829|PDB:4XJC"
FT   STRAND          76..86
FT                   /evidence="ECO:0007829|PDB:4XJC"
FT   STRAND          91..97
FT                   /evidence="ECO:0007829|PDB:4XJC"
FT   HELIX           99..102
FT                   /evidence="ECO:0007829|PDB:4XJC"
FT   TURN            103..105
FT                   /evidence="ECO:0007829|PDB:4XJC"
FT   STRAND          106..108
FT                   /evidence="ECO:0007829|PDB:4XJC"
FT   STRAND          112..114
FT                   /evidence="ECO:0007829|PDB:4XJC"
FT   STRAND          119..128
FT                   /evidence="ECO:0007829|PDB:4XJC"
FT   STRAND          130..132
FT                   /evidence="ECO:0007829|PDB:4XJC"
FT   STRAND          134..137
FT                   /evidence="ECO:0007829|PDB:4XJC"
FT   STRAND          140..152
FT                   /evidence="ECO:0007829|PDB:4XJC"
FT   TURN            160..163
FT                   /evidence="ECO:0007829|PDB:4XJC"
FT   HELIX           172..174
FT                   /evidence="ECO:0007829|PDB:4XJC"
SQ   SEQUENCE   177 AA;  19897 MW;  D15AE75387847E2B CRC64;
     MILSGKTISE KLTEKELEIT PLTEEQIQPA SVDLRLGPHF VTIDDSKEAV ISFERPIRYR
     EWTTSDETIV LPPHTFLLAT TMETVKLPNH LTAFVEGRSS VGRLGLFIQN AGWVDPGFNG
     QITLELFNAN RLPIELPIGR RICQLVFAEV TGEVAPYQGK YLFQKGATMS EIYKDAF
//