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            <funder>This work was supported by the Agence Nationale de la Recherche (ANR), ANR Blanc (An)aeroUbi ANR-15-CE11-0001-02. We thank Amélie Amblard and Mikael Martin for technical assistance and the GEM team at TIMC for discussions and suggestions. S.B. and Y.C. give thanks for the support of the discovery platform and data science group at EDyP. Proteomic experiments were partly supported by the Proteomics French Infrastructure (ANR-10-INBS-08-01 grant) and the Labex GRAL (ANR-10-LABX-49-01). Diffraction data were collected at the synchrotron SOLEIL, beamlines Proxima 1 and Proxima 2 (Saint-Aubin, France). We are most grateful to the beamline scientists, in particular Pierre Legrand and Bill Sheperd. C.F., C.-D.-T.V., M.L., and M.F. acknowledge support from the French National Research Agency (Labex program DYNAMO, ANR-11-LABX-0011), and from Fondation de l'Orangerie for Individual Philanthropy.</funder>
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                <term xml:lang="en">sequential reactions</term>
                <term xml:lang="en">metabolic pathway</term>
                <term xml:lang="en">SCP2</term>
                <term xml:lang="en">ubiquinone</term>
                <term xml:lang="en">lipid biosynthesis</term>
                <term xml:lang="en">multiprotein complex</term>
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              <p>Ubiquinone (UQ) is a polyprenylated lipid that is conserved from bacteria to humans and is crucial to cellular respiration. How the cell orchestrates the efficient synthesis of UQ, which involves the modification of extremely hydrophobic substrates by multiple sequential enzymes, remains an unresolved issue. Here, we demonstrate that seven Ubi proteins form the Ubi complex, a stable metabolon that catalyzes the last six reactions of the UQ biosynthetic pathway in Escherichia coli. The SCP2 domain of UbiJ forms an extended hydrophobic cavity that binds UQ intermediates inside the 1 MDa Ubi complex. We purify the Ubi complex from cytoplasmic extracts and demonstrate that UQ biosynthesis occurs in this fraction, challenging the current thinking of a membrane-associated biosynthetic process. Collectively, our results document a rare case of stable metabolon and highlight how the supramolecular organization of soluble enzymes allows the modification of hydrophobic substrates in a hydrophilic environment.</p>
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