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HAMAP rule MF_02119

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General rule information [?]

Accession MF_02119
Dates 23-MAY-2011 (Created)
13-JAN-2023 (Last updated, Version 12)
Name LipL
Scope(s) Bacteria
Template(s) P39648 (LIPL_BACSU); Q8Y489 (LIPLL_LISMO); [ Recover all ]
Triggered by HAMAP; MF_02119 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

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

Comments [?]

case <OC:Listeria> or <OC:Enterococcus>
FUNCTIONCatalyzes 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 Reaction=(R)-N(6)-lipoyl-L-lysyl-[glycine-cleavage complex H protein] + L-lysyl-[lipoyl-carrier protein] = (R)-N(6)-lipoyl-L-lysyl-[lipoyl- carrier protein] + L-lysyl-[glycine-cleavage complex H protein]; Xref=Rhea:RHEA:16413, Rhea:RHEA-COMP:10494, Rhea:RHEA-COMP:10500, Rhea:RHEA-COMP:10501, Rhea:RHEA-COMP:10502, ChEBI:CHEBI:29969, ChEBI:CHEBI:83099; EC=;
PATHWAYProtein modification; protein lipoylation via exogenous pathway.
FUNCTIONCatalyzes the amidotransfer (transamidation) of the octanoyl moiety from octanoyl-GcvH to the lipoyl domain of the E2 subunit of lipoate-dependent enzymes.
CATALYTIC ACTIVITY Reaction=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]; Xref=Rhea:RHEA:20213, Rhea:RHEA-COMP:10500, Rhea:RHEA-COMP:10501, Rhea:RHEA-COMP:10503, Rhea:RHEA-COMP:10504, ChEBI:CHEBI:29969, ChEBI:CHEBI:78809; EC=;
PATHWAYProtein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier- protein].
end case
MISCELLANEOUSThe reaction proceeds via a thioester-linked acyl-enzyme intermediate.
SIMILARITYBelongs to the octanoyltransferase LipL family.

Keywords [?]

Gene Ontology [?]

case <OCellular component:Listeria> or <OC:Enterococcus>
GO:0017118; Molecular function:lipoyltransferase activity
else; https://www.ebi.ac.uk/QuickGO/term/else
GO:0016415; Molecular function:octanoyltransferase activity
GO:0009107; Biological process:lipoate biosynthetic process
end case
GO:0009249; Biological process:protein lipoylation

Cross-references [?]

Pfam PF03099; BPL_LplA_LipB; 1;

Features [?]

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

Additional information [?]

Size range 273-288 amino acids
Related rules None
Fusion Nter: None Cter: 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.

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