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Annotation rule MF_02119
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General rule information [?]

Accession MF_02119
Dates 23-MAY-2011 (Created)
30-MAR-2020 (Last updated, Version 10)
Name LipL
Scope
Bacteria; Firmicutes
Templates P39648 (LIPL_BACSU); Q8Y489 (LIPLL_LISMO): [Recover all]
Triggered by

Propagated annotation [?]


Identifier, protein and gene names [?]

case <OC:Listeria> or <OC:Enterococcus>
Identifier
LIPLL
Protein name
RecName: Full=Lipoyl-[GcvH]:protein N-lipoyltransferase;
EC 2.3.1.200;
AltName: Full=Lipoyl-[GcvH]:E2 amidotransferase;
else
Identifier
LIPL
Protein name
RecName: Full=Octanoyl-[GcvH]:protein N-octanoyltransferase;
EC 2.3.1.204;
AltName: Full=Octanoyl-[GcvH]:E2 amidotransferase;
end case
Gene name
lipL

Comments [?]

case <OC:Listeria> or <OC:Enterococcus>
Function Catalyzes the amidotransfer (transamidation) of the lipoyl moiety from lipoyl-GcvH to the lipoyl domain of the E2 subunit of lipoate-dependent enzymes. Takes part in a pathway for scavenging of lipoic acid.
Catalytic activity RHEA:16413: L-lysyl-[lipoyl-carrier protein] + N(6)-lipoyl-L-lysyl-[glycine-cleavage complex H protein] = (R)-N(6)-lipoyl-L-lysyl-[lipoyl-carrier protein] + L-lysyl-[glycine-cleavage complex H protein]
EC 2.3.1.200
Pathway Protein modification; protein lipoylation via exogenous pathway.
else
Function Catalyzes the amidotransfer (transamidation) of the octanoyl moiety from octanoyl-GcvH to the lipoyl domain of the E2 subunit of lipoate-dependent enzymes.
Catalytic activity RHEA:20213: L-lysyl-[lipoyl-carrier protein] + N(6)-octanoyl-L-lysyl-[glycine-cleavage complex H protein] = L-lysyl-[glycine-cleavage complex H protein] + N(6)-octanoyl-L-lysyl-[lipoyl-carrier protein]
EC 2.3.1.204
Pathway Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein].
end case
Miscellaneous The reaction proceeds via a thioester-linked acyl-enzyme intermediate.
Similarity Belongs to the octanoyltransferase LipL family.

Keywords [?]

Acyltransferase
Transferase

Gene Ontology [?]

case <OC:Listeria> or <OC:Enterococcus>
GO:0017118; Molecular function: lipoyltransferase activity.
else
GO:0016415; Molecular function: octanoyltransferase activity.
GO:0009107; Biological process: lipoate biosynthetic process.
end case
GO:0009249; Biological process: protein lipoylation.

Cross-references [?]

PROSITE PS51733; BPL_LPL_CATALYTIC; 1; trigger=PRU01067;
Pfam PF03099; BPL_LplA_LipB; 1;

Features [?]

From: LIPL_BACSU (P39648)
Key     From     To       Description   Tag   Condition   FTGroup
ACT_SITE     150     150       Acyl-thioester intermediate     C  
SITE     162     162       Lowers pKa of active site Cys     K  

Additional information [?]

Size range 273-288 amino acids
Related rules None
Fusion 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 Firmicutes) 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.


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