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==Swit_4259, an Acetoacetate Decarboxylase-like Enzyme from Sphingomonas wittichii RW1==
<StructureSection load='5upb' size='340' side='right'caption='[[5upb]], [[Resolution|resolution]] 1.91&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5upb]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhizorhabdus_wittichii_RW1 Rhizorhabdus wittichii RW1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UPB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UPB 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]] 1.912&#8491;</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=5upb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5upb OCA], [https://pdbe.org/5upb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5upb RCSB], [https://www.ebi.ac.uk/pdbsum/5upb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5upb ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
The Gram-negative bacterium Sphingomonas wittichii RW1 is notable for its ability to metabolize a variety of aromatic hydrocarbons. Not surprisingly, the S. wittichii genome contains a number of putative aromatic hydrocarbon-degrading gene clusters. One of these includes an enzyme of unknown function, Swit_4259, which belongs to the acetoacetate decarboxylase-like superfamily (ADCSF). Here, it is reported that Swit_4259 is a small (28.8 kDa) tetrameric ADCSF enzyme that, unlike the prototypical members of the superfamily, does not have acetoacetate decarboxylase activity. Structural characterization shows that the tertiary structure of Swit_4259 is nearly identical to that of the true decarboxylases, but there are important differences in the fine structure of the Swit_4259 active site that lead to a divergence in function. In addition, it is shown that while it is a poor substrate, Swit_4259 can catalyze the hydration of 2-oxo-hex-3-enedioate to yield 2-oxo-4-hydroxyhexanedioate. It is also demonstrated that Swit_4259 has pyruvate aldolase-dehydratase activity, a feature that is common to all of the family V ADCSF enzymes studied to date. The enzymatic activity, together with the genomic context, suggests that Swit_4259 may be a hydratase with a role in the metabolism of an as-yet-unknown hydrocarbon. These data have implications for engineering bioremediation pathways to degrade specific pollutants, as well as structure-function relationships within the ADCSF in general.

Swit_4259, an acetoacetate decarboxylase-like enzyme from Sphingomonas wittichii RW1.,Mydy LS, Mashhadi Z, Knight TW, Fenske T, Hagemann T, Hoppe RW, Han L, Miller TR, Schwabacher AW, Silvaggi NR Acta Crystallogr F Struct Biol Commun. 2017 Dec 1;73(Pt 12):672-681. doi:, 10.1107/S2053230X17015862. Epub 2017 Nov 14. PMID:29199988<ref>PMID:29199988</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Rhizorhabdus wittichii RW1]]
[[Category: Mydy LS]]
[[Category: Silvaggi NR]]