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Family Report for: Thioesterase_acyl-transferase

Name Class
Gene_locus (17)
ThYme25 TE-19
Paper (5)
InterproIPR003157 Acyl transferase, LuxD
CommentThis bacterial family of Acyl transferases (ACT or myristoyl-acp-specific thioesterases) catalyses the first step in the bioluminescent fatty acid reductase system, which is required for aldehyde biosynthesis. This enzyme belongs to the LuxD family. Together with acyl-protein synthetase (LuxE) and reductase (LuxC), it belongs to a multienzyme complex. This complex channels activated fatty acids into the aldehyde substrate for the luciferase-catalyzed bacterial bioluminescence reaction. The C-terminal region of LuxD interacts with LuxE to causes a conformational change. LuxD has a calculated M(r) of 34,384 and comprises 305 aa residues. Induction of luminescence only occurs at high cell density. Some bacteria have N-acylhomoserine lactone autoinducers for luminescence. Warning: the serine 77 in GXSXG motif is not the active site serine 114 as determined by X ray structure AASLS in Vibrio harveyi see Lawson et al., 2003. Family TE19 in ThYme database
PfamPF02273 Acyl_transf_2
PIRSFPIRSF009416 lux-specific fatty acid reductase, acyl-ACP thioesterase subunit

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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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