AC   MF_02119;
DC   Protein; auto
TR   HAMAP; MF_02119; -; 1; level=0
XX
Names: LipL
XX
case <OC:Listeria> or <OC:Enterococcus>
ID   LIPLL
DE   RecName: Full=Lipoyl-[GcvH]:protein N-lipoyltransferase;
DE            EC=2.3.1.200;
DE   AltName: Full=Lipoyl-[GcvH]:E2 amidotransferase;
else
ID   LIPL
DE   RecName: Full=Octanoyl-[GcvH]:protein N-octanoyltransferase;
DE            EC=2.3.1.204;
DE   AltName: Full=Octanoyl-[GcvH]:E2 amidotransferase;
end case
GN   Name=lipL;
XX
case <OC:Listeria> or <OC:Enterococcus>
CC   -!- FUNCTION: Catalyzes the amidotransfer (transamidation) of the lipoyl
CC       moiety from lipoyl-GcvH to the lipoyl domain of the E2 subunit of
CC       lipoate-dependent enzymes. Takes part in a pathway for scavenging of
CC       lipoic acid.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[lipoyl-carrier protein] + N(6)-[(R)-lipoyl]-L-lysyl-
CC         [glycine-cleavage complex H protein] = L-lysyl-[glycine-cleavage
CC         complex H protein] + N(6)-[(R)-lipoyl]-L-lysyl-[lipoyl-carrier
CC         protein]; Xref=Rhea:RHEA:16413, Rhea:RHEA-COMP:10494, Rhea:RHEA-
CC         COMP:10500, Rhea:RHEA-COMP:10501, Rhea:RHEA-COMP:10502,
CC         ChEBI:CHEBI:29969, ChEBI:CHEBI:83099; EC=2.3.1.200;
CC   -!- PATHWAY: Protein modification; protein lipoylation via exogenous
CC       pathway.
else
CC   -!- FUNCTION: Catalyzes the amidotransfer (transamidation) of the octanoyl
CC       moiety from octanoyl-GcvH to the lipoyl domain of the E2 subunit of
CC       lipoate-dependent enzymes.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[lipoyl-carrier protein] + N(6)-octanoyl-L-lysyl-
CC         [glycine-cleavage complex H protein] = L-lysyl-[glycine-cleavage
CC         complex H protein] + N(6)-octanoyl-L-lysyl-[lipoyl-carrier protein];
CC         Xref=Rhea:RHEA:20213, Rhea:RHEA-COMP:10500, Rhea:RHEA-COMP:10501,
CC         Rhea:RHEA-COMP:10503, Rhea:RHEA-COMP:10504, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:78809; EC=2.3.1.204;
CC   -!- PATHWAY: Protein modification; protein lipoylation via endogenous
CC       pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-
CC       protein].
end case
CC   -!- MISCELLANEOUS: The reaction proceeds via a thioester-linked acyl-enzyme
CC       intermediate.
CC   -!- SIMILARITY: Belongs to the octanoyltransferase LipL family.
XX
DR   PROSITE; PS51733; BPL_LPL_CATALYTIC; 1; trigger=yes
DR   Pfam; PF03099; BPL_LplA_LipB; 1; trigger=no
XX
KW   Acyltransferase
KW   Transferase
XX
case <OC:Listeria> or <OC:Enterococcus>
GO   GO:0017118; F:lipoyltransferase activity
else
GO   GO:0016415; F:octanoyltransferase activity
GO   GO:0009107; P:lipoate biosynthetic process
end case
GO   GO:0009249; P:protein lipoylation
XX
FT   From: LIPL_BACSU (P39648)
FT   ACT_SITE        150
FT                   /note="Acyl-thioester intermediate"
FT   Condition: C
FT   SITE            162
FT                   /note="Lowers pKa of active site Cys"
FT   Condition: K
XX
Size: 273-288;
Related: None;
Template: P39648; Q8Y489;
Scope:
 Bacteria; Bacillota
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: E.coli requires only 2 proteins for the endogenous pathway of protein lipoylation,
 LipB (MF_00013) and LipA (MF_00206), whereas B.subtilis (and probably many Bacillota) requires
 3 enzymes: LipM (MF_02118), LipL (MF_02119) and LipA (MF_00206).
 Listeria monocytogenes is a natural lipoic acid auxotroph and relies upon exogenous sources of
 lipoic acid for growth (PubMed:21768091). In this species, LipL takes part in a pathway for
 scavenging of lipoic acid derived from eukaryotic host cells. Enterococcus faecalis also lacks
 the ability to make lipoic acid (PubMed:21768091), that's why one can suppose LipL is involved
 in lipoate scavenging and not biosynthesis.
XX
# Revision 1.13 2023/09/14
//