AC   MF_02118;
DC   Protein; auto
TR   HAMAP; MF_02118; -; 1; level=0
XX
Names: LipM
XX
ID   LIPM
DE   RecName: Full=Octanoyltransferase LipM;
DE            EC=2.3.1.181;
DE   AltName: Full=Octanoyl-[acyl-carrier-protein]:[GcvH] N-octanoyltransferase;
GN   Name=lipM;
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CC   -!- FUNCTION: Catalyzes the transfer of endogenously produced octanoic acid
CC       from octanoyl-acyl-carrier-protein onto the lipoyl domain of GcvH, an
CC       intermediate carrier during protein lipoylation.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-
CC         octanoyl-L-lysyl-[protein]; Xref=Rhea:RHEA:17665, Rhea:RHEA-
CC         COMP:9636, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9752, Rhea:RHEA-
CC         COMP:9928, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78463, ChEBI:CHEBI:78809; EC=2.3.1.181;
CC   -!- PATHWAY: Protein modification; protein lipoylation via endogenous
CC       pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-
CC       protein].
CC   -!- SUBUNIT: Monomer.
CC   -!- MISCELLANEOUS: In the reaction, the free carboxyl group of octanoic
CC       acid is attached via an amide linkage to the epsilon-amino group of a
CC       specific lysine residue of lipoyl domains of lipoate-dependent enzymes.
CC       The reaction proceeds via an octanoyl-thioester enzyme intermediate.
CC   -!- SIMILARITY: Belongs to the octanoyltransferase LipM family.
XX
DR   PROSITE; PS51733; BPL_LPL_CATALYTIC; 1; trigger=yes
DR   Pfam; PF03099; BPL_LplA_LipB; 1; trigger=no
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KW   Acyltransferase
KW   Transferase
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GO   GO:0016415; F:octanoyltransferase activity
GO   GO:0009107; P:lipoate biosynthetic process
GO   GO:0009249; P:protein lipoylation
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FT   From: LIPM_BACSU (P54511)
FT   ACT_SITE        150
FT                   /note="Acyl-thioester intermediate"
FT   Condition: C
FT   SITE            165
FT                   /note="Lowers pKa of active site Cys"
FT   Condition: K
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Size: 269-278;
Related: None;
Template: P54511;
Scope:
 Bacteria; Bacillota
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: 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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# Revision 1.7 2023/01/13
//