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==dCTP deaminase-dUTPase from Bacillus halodurans==
<StructureSection load='4xjc' size='340' side='right'caption='[[4xjc]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4xjc]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Alkalihalobacillus_halodurans_C-125 Alkalihalobacillus halodurans C-125]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XJC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XJC FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.35&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=TTP:THYMIDINE-5-TRIPHOSPHATE'>TTP</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4xjc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xjc OCA], [https://pdbe.org/4xjc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xjc RCSB], [https://www.ebi.ac.uk/pdbsum/4xjc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xjc ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DCDB_HALH5 DCDB_HALH5] Bifunctional enzyme that catalyzes both the deamination of dCTP to dUTP and the hydrolysis of dUTP to dUMP without releasing the toxic dUTP intermediate.[HAMAP-Rule:MF_00146]<ref>PMID:25746996</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Analysis of the genome of Bacillus halodurans strain C125 indicated that two pathways leading from a cytosine deoxyribonucleotide to dUMP, used for dTMP synthesis, was encoded by the bacterium. The responsible genes, the comEB gene and the dcdB gene, encoding dCMP deaminase and the bifunctional dCTP deaminase:dUTPase (DCD:DUT) were both shown to be expressed in B. halodurans and both genes were subject to repression by the nucleosides, thymidine and deoxycytidine. The latter nucleoside presumably excerts its repression after deamination by cytidine deaminase. Both comEB and dcdB were cloned, overexpressed in E. coli and purified to homogeneity. The enzymes were both active and displayed the expected regulatory properties: activation by dCTP for dCMP deaminase and dTTP inhibition for both enzymes. Structurally, the B. halodurans enzyme resembled Mycobacterium tuberculosis enzyme the most. An investigation of sequenced genomes from other species of the genus Bacillus revealed that not only B. halodurans but also Bacillus pseudofirmus, Bacillus thuringiensis, Bacillus hemocellulosilyticus, Bacillus marmarensis, Bacillus cereus and Bacillus megaterium all encode both the dCMP deaminase and DCD:DUT enzymes. In addition, eight dcdB homologs were registered in entrez-NCBI from Bacillus species within the genus where the whole genome had not yet been sequenced.

Bacillus halodurans strain C125 encodes and synthesizes enzymes from both known pathways to form dUMP directly from cytosine deoxyribonucleotides.,Oehlenschlaeger CB, Lovgreen MN, Reinauer E, Lehtinen E, Pind ML, Harris P, Martinussen J, Willemoes M Appl Environ Microbiol. 2015 Mar 6. pii: AEM.00268-15. PMID:25746996<ref>PMID:25746996</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4xjc" style="background-color:#fffaf0;"></div>

==See Also==
*[[Deaminase 3D structures|Deaminase 3D structures]]
== References ==
<references/>
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</StructureSection>
[[Category: Alkalihalobacillus halodurans C-125]]
[[Category: Large Structures]]
[[Category: Harris P]]
[[Category: Loevgreen M]]
[[Category: Oehlenschlaeger C]]
[[Category: Willemoes M]]