AC   MF_00013;
DC   Protein; auto
TR   HAMAP; MF_00013; -; 1; level=0
XX
Names: LipB
XX
ID   LIPB
case <OC:Bacteria>
DE   RecName: Full=Octanoyltransferase;
DE            EC=2.3.1.181;
DE   AltName: Full=Lipoate-protein ligase B;
DE   AltName: Full=Lipoyl/octanoyl transferase;
DE   AltName: Full=Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase;
else
DE   RecName: Full=Probable octanoyltransferase;
DE            EC=2.3.1.181;
DE   AltName: Full=Lipoate-protein ligase B;
DE   AltName: Full=Lipoyl/octanoyl transferase;
DE   AltName: Full=Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase;
end case
GN   Name=lipB;
XX
CC   -!- FUNCTION: Catalyzes the transfer of endogenously produced octanoic acid
CC       from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-
CC       dependent enzymes. Lipoyl-ACP can also act as a substrate although
CC       octanoyl-ACP is likely to be the physiological substrate.
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]: step 1/2.
case <OC:Bacteria> or <OC:Archaea>
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
end case
case <OG:Chloroplast>
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
end case
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   -!- SIMILARITY: Belongs to the LipB family.
XX
DR   PROSITE; PS51733; BPL_LPL_CATALYTIC; 1; trigger=yes
DR   PROSITE; PS01313; LIPB; 1; trigger=no
DR   Pfam; PF03099; BPL_LplA_LipB; 1; trigger=no
DR   NCBIfam; TIGR00214; LipB; 1; trigger=no
XX
case <OC:Bacteria> or <OC:Archaea>
KW   Cytoplasm
end case
KW   Transferase
KW   Acyltransferase
XX
GO   GO:0016746; F:acyltransferase activity
case <OG:Chloroplast>
GO   GO:0009507; C:chloroplast
end case
case <OC:Bacteria> or <OC:Archaea>
GO   GO:0005737; C:cytoplasm
end case
XX
FT   From: LIPB_MYCTU (P9WK83)
FT   BINDING         76..83
FT                   /ligand="substrate"
FT   Condition: R-G-G-x(2)-[TS]-x-H
FT   BINDING         145..147
FT                   /ligand="substrate"
FT   Condition: [AS]-x-[GA]
FT   BINDING         158..160
FT                   /ligand="substrate"
FT   Condition: G-x-[ASG]
FT   ACT_SITE        176
FT                   /note="Acyl-thioester intermediate"
FT   Condition: C
FT   SITE            142
FT                   /note="Lowers pKa of active site Cys"
FT   Condition: K
XX
Size: 180-330;
Related: None;
Template: P60720; P9WK83;
Scope:
 Bacteria
 Archaea
 Plastid
Fusion:
 Nter: <Unknown>
 Cter: <Nudix>
Duplicate: in PICTO
Plasmid: None
Comments: Unknown N-terminal domains in Deinococcus radiodurans and
 Porphyromonas gingivalis. Nudix-like C-terminal domain in Myxococcus xanthus.
XX
# Revision 1.45 2023/06/01
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