HAMAP rule MF_02119
General rule information
[?]
| Accession | MF_02119 |
| Dates | 23-MAY-2011 (Created)
14-SEP-2023 (Last updated, Version 13) |
| Name | LipL |
| Scope(s) |
Bacteria Bacillota |
| 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; 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 | 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 | Reaction=L-lysyl-[lipoyl-carrier protein] + N(6)-[(R)-lipoyl]-L-lysyl- [glycine-cleavage complex H protein] = L-lysyl-[glycine-cleavage complex H protein] + N(6)-[(R)-lipoyl]-L-lysyl-[lipoyl-carrier 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=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 | 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=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
[?]
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
[?]
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. |