{PDOC01017}
{PS01313; LIPB}
{BEGIN}
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* Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase (lipB) signature *
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Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase   [1,2,3]  (gene
lipB) is  the  bacterial  enzyme  that creates an amide linkage that joins the
free carboxyl  group of octanoyl acid to the epsilon-amino group of a specific
lysine residue in lipoyl domains (see <PDOC50968>).

Such an  enzyme  has  also  be  found in fungi [4], where it is located in the
mitochondria. It  also  seems  to  exist  in  plants  and  is  encoded  in the
chloroplast genome of the red alga Cyanidium caldarium.

As a signature for lipB, we selected the most conserved region, located in the
central part  of  the  enzyme.  This  region  contains  one  of  two conserved
histidines.

-Consensus pattern: R-G(2)-x(2)-T-[FYWCAH]-H-x(2)-[GHS]-Q-x-[LIVMT]-x-Y
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: September 2011 / Text revised.

[ 1] Morris T.W., Reed K.E., Cronan J.E. Jr.
     "Lipoic acid metabolism in Escherichia coli: the lplA and lipB genes
     define redundant pathways for ligation of lipoyl groups to
     apoprotein."
     J. Bacteriol. 177:1-10(1995).
     PubMed=8002607
[ 2] Zhao X., Miller J.R., Cronan J.E.
     "The reaction of LipB, the octanoyl-[acyl carrier protein]:protein
     N-octanoyltransferase of lipoic acid synthesis, proceeds through an
     acyl-enzyme intermediate."
     Biochemistry 44:16737-16746(2005).
     PubMed=16342964; DOI=10.1021/bi051865y
[ 3] Christensen Q.H., Cronan J.E.
     "Lipoic acid synthesis: a new family of octanoyltransferases generally
     annotated as lipoate protein ligases."
     Biochemistry 49:10024-10036(2010).
     PubMed=20882995; DOI=10.1021/bi101215f
[ 4] Chen X.J.
     "Cloning and characterization of the lipoyl-protein ligase gene LIPB
     from the yeast Kluyveromyces lactis: synergistic respiratory
     deficiency due to mutations in LIPB and mitochondrial F1-ATPase
     subunits."
     Mol. Gen. Genet. 255:341-349(1997).
     PubMed=9268025

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