{PDOC51733}
{PS51733; BPL_LPL_CATALYTIC}
{BEGIN}
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* Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL) catalytic domain profile *
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Biotin and   lipoic  acid  are  the  covalently  bound  cofactors  of  various
multicomponent enzyme  complexes  that  catalyze  key  metabolic reactions. In
these enzymes complexes, biotin and lipoic acid are attached via amide linkage
through their  carboxyl group and the epsilon-amino group of a specific lysine
residue of  a protein module known respectively as the biotinyl and the lipoyl
domain (see  <PDOC50968>).  Covalent  attachment  of biotin and lipoic acid to
these enzyme  complexes  occurs  post-translationally,  and  it is mediated by
biotinylating and  lipoylating  protein  enzymes, which specifically recognize
the biotinyl  and  lipoyl  domains,  ensuring their correct post-translational
modification. Lipoylating and biotinylating enzymes are evolutionarily related
protein families containing a homologous catalytic module [1].

Amino acid  sequence  conservation  between  the catalytic modules of biotinyl
protein ligases  (BPLs)  and  lipoyl  protein  ligases (LPLs) is very low, and
mainly affects  residues that are important for the scaffold of the structure,
such as  those  contributing to the hydrophobic core. Despite the poor overall
sequence similarity,  a single lysine residue is strictly conserved in all LPL
and BPL  sequences.  This lysine residue is likely to bind specifically to the
carbonyl oxygen of the carboxyl group of biotin or at the end of the hydrogen-
carbon tail  of the lipoyl moiety [1]. The BPL/LPL catalytic domain contains a
seven-stranded mixed  beta-sheet  on  one  side  and four alpha-helices on the
other side (see <PDB:1WQ7>) [2].

The profile we developed covers the entire BPL/LPL catalytic domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: September 2014 / First entry.

[ 1] Reche P.A.
     "Lipoylating and biotinylating enzymes contain a homologous catalytic
     module."
     Protein Sci. 9:1922-1929(2000).
     PubMed=11106165; DOI=10.1110/ps.9.10.1922
[ 2] Bagautdinov B., Kuroishi C., Sugahara M., Kunishima N.
     "Crystal structures of biotin protein ligase from Pyrococcus
     horikoshii OT3 and its complexes: structural basis of biotin
     activation."
     J. Mol. Biol. 353:322-333(2005).
     PubMed=16169557; DOI=10.1016/j.jmb.2005.08.032

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