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Annotation rule MF_02119 |
General rule information
[?]
Accession |
MF_02119 |
Dates |
23-MAY-2011 (Created) 30-MAR-2020 (Last updated, Version 10) |
Scope |
Bacteria; Firmicutes |
Propagated annotation
[?]
Identifier, protein and gene names
[?]
case <OC:Listeria> or <OC:Enterococcus>
Protein name |
RecName:
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Full=Lipoyl-[GcvH]:protein N-lipoyltransferase;
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EC 2.3.1.200;
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AltName:
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Full=Lipoyl-[GcvH]:E2 amidotransferase;
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else
Protein name |
RecName:
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Full=Octanoyl-[GcvH]:protein N-octanoyltransferase;
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EC 2.3.1.204;
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AltName:
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Full=Octanoyl-[GcvH]:E2 amidotransferase;
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end case
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
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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
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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. |
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.
From: LIPL_BACSU (P39648) |
Key
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From
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To
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Description
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Tag
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Condition
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FTGroup
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ACT_SITE
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150
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150
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Acyl-thioester intermediate
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C
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SITE
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162
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162
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Lowers pKa of active site Cys
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K
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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. |