DCDB_ALKHC
ID DCDB_ALKHC Reviewed; 177 AA.
AC Q9KFV3;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 115.
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 Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
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; 272558.10172981; -.
DR EnsemblBacteria; BAB04087; BAB04087; BAB04087.
DR KEGG; bha:BH0368; -.
DR eggNOG; COG0717; Bacteria.
DR HOGENOM; CLU_087476_2_1_9; -.
DR OMA; FENHRYP; -.
DR OrthoDB; 1598407at2; -.
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 Pfam; PF00692; dUTPase; 1.
DR SUPFAM; SSF51283; SSF51283; 1.
DR TIGRFAMs; TIGR02274; dCTP_deam; 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
