HAMAP rule MF_02118
General rule information
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| Accession | MF_02118 |
| Dates | 23-MAY-2011 (Created)
13-JAN-2023 (Last updated, Version 7) |
| Name | LipM |
| Scope(s) |
Bacteria Bacillota |
| Template(s) | P54511 (LIPM_BACSU); [ Recover all ] |
| Triggered by |
HAMAP; MF_02118 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| Identifier | LIPM |
| Protein name | RecName: Full=Octanoyltransferase LipM; EC=2.3.1.181; AltName: Full=Octanoyl-[acyl-carrier-protein]:[GcvH] N-octanoyltransferase; |
| Gene name | Name=lipM; |
Comments
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| FUNCTION | Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domain of GcvH, an intermediate carrier during protein lipoylation. |
| CATALYTIC ACTIVITY | Reaction=L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)- octanoyl-L-lysyl-[protein]; Xref=Rhea:RHEA:17665, Rhea:RHEA- COMP:9636, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9752, Rhea:RHEA- COMP:9928, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:64479, ChEBI:CHEBI:78463, ChEBI:CHEBI:78809; EC=2.3.1.181; |
| PATHWAY | Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier- protein]. |
| SUBUNIT | Monomer. |
| MISCELLANEOUS | In the reaction, the free carboxyl group of octanoic acid is attached via an amide linkage to the epsilon-amino group of a specific lysine residue of lipoyl domains of lipoate-dependent enzymes. The reaction proceeds via an octanoyl-thioester enzyme intermediate. |
| SIMILARITY | Belongs to the octanoyltransferase LipM family. |
Keywords
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Gene Ontology
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| GO:0016415; Molecular function:octanoyltransferase activity |
| GO:0009107; Biological process:lipoate biosynthetic process |
| GO:0009249; Biological process:protein lipoylation |
Cross-references
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Features
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| From: LIPM_BACSU (P54511) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| ACT_SITE | 150 | 150 | /note="Acyl-thioester intermediate" | C | ||||||||
| SITE | 165 | 165 | /note="Lowers pKa of active site Cys" | K | ||||||||
Additional information
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| Size range | 269-278 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). |