AC   PRU01066;
DC   Domain;
TR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1; level=0
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Names: Biotinyl/lipoyl domain
Function: Biotin and lipoic acid moieties are the covalently bound cofactors
 of several multicomponent enzyme complexes that catalyze key metabolic
 reactions. They are attached to a lysine residue, via an amide bond,
 by specific biotinyl and lipoyl protein ligases.
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case <Feature:PS50968:41-42=M-K> or <Feature:PS50968:42-43=K-M>
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
else case <Feature:PS50968:42=K>
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC       Note=Binds 1 lipoyl cofactor covalently.;
end case
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case <Feature:PS50968:41-42=M-K> or <Feature:PS50968:42-43=K-M>
KW   Biotin
else case <Feature:PS50968:42=K>
KW   Lipoyl
end case
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FT   From: PS50968
case <Feature:PS50968:41-42=M-K> or <Feature:PS50968:42-43=K-M>
FT   DOMAIN          from..to
FT                   /note="Biotinyl-binding #"
FT   MOD_RES         42
FT                   /note="N6-biotinyllysine"
FT   Condition: K
else
FT   DOMAIN          from..to
FT                   /note="Lipoyl-binding #"
FT   MOD_RES         42
FT                   /note="N6-lipoyllysine"
FT   Condition: K
end case
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Chop: Nter=0; Cter=0;
Size: 57-96;
Related: None;
Repeats: 1-3;
Topology: Undefined;
Example: P0A6T9; P0ABD8;
Scope:
 Bacteria
 Eukaryota
 Archaea
Comments: None;
XX
# Revision 1.6 2019/11/22
//