ExPASy Proteomics Server

Accession	MF_01602
Dates	17-MAR-2004 (Created) 25-NOV-2009 (Last updated, Version 11)

Data class

Protein

Predictors

HAMAP; MF_01602; [distribution of match scores in UniProtKB];[seed alignment for MF_01602]

Names

LplA

Identifier

LPLA

Protein name

RecName: Full=Lipoate-protein ligase A; EC=2.7.7.63; AltName: Full=Lipoate--protein ligase;

Gene name

lplA

FUNCTION: Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes (By similarity).

CATALYTIC ACTIVITY: ATP + lipoate = diphosphate + lipoyl-AMP.

CATALYTIC ACTIVITY: Lipoyl-AMP + protein = protein N(6)-(lipoyl)lysine + AMP.

PATHWAY: Protein modification; protein lipoylation via exogenous pathway; protein N(6)-(lipoyl)lysine from lipoate: step 1/2.

PATHWAY: Protein modification; protein lipoylation via exogenous pathway; protein N(6)-(lipoyl)lysine from lipoate: step 2/2.

SUBUNIT: Monomer (By similarity).

SUBCELLULAR LOCATION: Cytoplasm (By similarity).

MISCELLANEOUS: In the transfer reaction, the free carboxyl group of lipoic acid is attached via an amide linkage to the epsilon-amino group of a specific lysine residue of lipoyl domains of lipoate-dependent enzymes (By similarity).

SIMILARITY: Belongs to the lplA family.

Pfam	PF03099; BPL_LipA_LipB; 1;
TIGRFAMs	TIGR00545; lipoyltrans; 1;

ATP-binding, Cytoplasm, Nucleotide-binding, Transferase.

GO:0016979; Molecular function: lipoate-protein ligase activity.
GO:0018055; Biological process: peptidyl-lysine lipoylation.
GO:0005737; Cellular component: cytoplasm.

From: LPLA_ECOLI (P32099)
Key		From		To		Description		Condition		FTGroup
NP_BIND		76		79		ATP (By similarity)		G-A-V-[FY]
BINDING		71		71		ATP (By similarity)		R
BINDING		134		134		ATP (By similarity)		K
BINDING		134		134		Lipoate (By similarity)		K

Size range:	337-339 amino acids
Related UniRules:	None
Template:	P32099 (LPLA_ECOLI); Q9HKT1 (LPLA_THEAC): [Recover all]
Scope:	Bacteria; Proteobacteria
Fusion:	Nter: None; Cter: None
Duplicate:	None
Plasmid encoded:	None