AC   MF_01602;
DC   Protein; auto
TR   HAMAP; MF_01602; -; 1; level=0
XX
Names: LplA
XX
ID   LPLA
DE   RecName: Full=Lipoate-protein ligase A;
DE            EC=6.3.1.20;
DE   AltName: Full=Lipoate--protein ligase;
GN   Name=lplA;
XX
CC   -!- FUNCTION: Catalyzes both the ATP-dependent activation of exogenously
CC       supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl
CC       onto the lipoyl domains of lipoate-dependent enzymes.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-lipoate + ATP + L-lysyl-[lipoyl-carrier protein] = AMP +
CC         diphosphate + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[lipoyl-carrier
CC         protein]; Xref=Rhea:RHEA:49288, Rhea:RHEA-COMP:10500, Rhea:RHEA-
CC         COMP:10502, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:83088, ChEBI:CHEBI:83099,
CC         ChEBI:CHEBI:456215; EC=6.3.1.20;
CC   -!- PATHWAY: Protein modification; protein lipoylation via exogenous
CC       pathway; protein N(6)-(lipoyl)lysine from lipoate: step 1/2.
CC   -!- PATHWAY: Protein modification; protein lipoylation via exogenous
CC       pathway; protein N(6)-(lipoyl)lysine from lipoate: step 2/2.
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- MISCELLANEOUS: In the transfer reaction, the free carboxyl group of
CC       lipoic acid is attached via an amide linkage to the epsilon-amino group
CC       of a specific lysine residue of lipoyl domains of lipoate-dependent
CC       enzymes.
CC   -!- SIMILARITY: Belongs to the LplA family.
XX
DR   PROSITE; PS51733; BPL_LPL_CATALYTIC; 1; trigger=yes
DR   Pfam; PF03099; BPL_LplA_LipB; 1; trigger=no
DR   NCBIfam; TIGR00545; Lipoyltrans; 1; trigger=no
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KW   ATP-binding
KW   Cytoplasm
KW   Nucleotide-binding
KW   Ligase
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GO   GO:0016979; F:lipoate-protein ligase activity
GO   GO:0009249; P:protein lipoylation
GO   GO:0005737; C:cytoplasm
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FT   From: LPLA_ECOLI (P32099)
FT   BINDING         76..79
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: G-A-V-[FY]
FT   BINDING         71
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: R
FT   BINDING         134
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: K
FT   BINDING         134
FT                   /ligand="(R)-lipoate"
FT                   /ligand_id="ChEBI:CHEBI:83088"
FT   Condition: K
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Size: 337-339;
Related: None;
Template: P32099; Q9HKT1;
Scope:
 Bacteria; Pseudomonadota
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
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# Revision 1.25 2023/09/14
//