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HAMAP rule MF_02118

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General rule information [?]

Accession MF_02118
Dates 23-MAY-2011 (Created)
13-JAN-2023 (Last updated, Version 7)
Name LipM
Scope
Bacteria; Bacillota
Template P54511 (LIPM_BACSU)
Triggered by

Propagated annotation [?]


Identifier, protein and gene names [?]

Identifier
LIPM
Protein name
RecName: Full=Octanoyltransferase LipM;
EC 2.3.1.181;
AltName: Full=Octanoyl-[acyl-carrier-protein]:[GcvH] N-octanoyltransferase;
Gene name
lipM

Comments [?]

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 RHEA:17665: L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein]
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 [?]

Acyltransferase
Transferase

Gene Ontology [?]

GO:0016415; Molecular function: octanoyltransferase activity.
GO:0009107; Biological process: lipoate biosynthetic process.
GO:0009249; Biological process: protein lipoylation.

Cross-references [?]

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

Features [?]

From: LIPM_BACSU (P54511)
Key     From     To       Description   Tag   Condition   FTGroup
ACT_SITE     150     150       Acyl-thioester intermediate     C  
SITE     165     165       Lowers pKa of active site Cys     K  

Additional information [?]

Size range 269-278 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 Bacillota) requires 3 enzymes: LipM (MF_02118), LipL (MF_02119) and LipA (MF_00206).


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