HAMAP

Accession	MF_00206
Dates	1-JUN-2001 (Created) 12-AUG-2011 (Last updated, Version 38)

Data class

Protein

Predictors

HAMAP; MF_00206; [distribution of match scores in UniProtKB];[seed alignment for MF_00206]

Names

Lipoyl_synth

Identifier

LIPA

Protein name

RecName: Full=Lipoyl synthase; EC=2.8.1.8; AltName: Full=Lip-syn; Short=LS; AltName: Full=Lipoate synthase; AltName: Full=Lipoic acid synthase; AltName: Full=Sulfur insertion protein LipA;

Protein name

RecName: Full=Probable lipoyl synthase; EC=2.8.1.8; AltName: Full=Lip-syn; Short=LS; AltName: Full=Lipoate synthase; AltName: Full=Lipoic acid synthase; AltName: Full=Sulfur insertion protein LipA;

Gene name

lipA

FUNCTION: Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives (By similarity).

CATALYTIC ACTIVITY: Protein N(6)-(octanoyl)lysine + 2 sulfur + 2 S-adenosyl-L-methionine = protein N(6)-(lipoyl)lysine + 2 L-methionine + 2 5'-deoxyadenosine.

COFACTOR: Binds 2 4Fe-4S clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine (By similarity).

PATHWAY: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein].

PATHWAY: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 2/2.

SUBCELLULAR LOCATION: Cytoplasm (Potential).

SIMILARITY: Belongs to the radical SAM superfamily. Lipoyl synthase family.

Pfam	PF04055; Radical_SAM; 1;
TIGRFAMs	TIGR00510; LipA; 1;

4Fe-4S, Cytoplasm, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine, Transferase.

GO:0016783; Molecular function: sulfurtransferase activity.
GO:0016992; Molecular function: lipoate synthase activity.
GO:0051539; Molecular function: 4 iron, 4 sulfur cluster binding.
GO:0009107; Biological process: lipoate biosynthetic process.
GO:0009249; Biological process: protein lipoylation.
GO:0005737; Cellular component: cytoplasm.

From: LIPA_ECOLI (P60716)
Key		From		To		Description		Condition		FTGroup
METAL		68		68		Iron-sulfur 1 (4Fe-4S) (By similarity)		C
METAL		73		73		Iron-sulfur 1 (4Fe-4S) (By similarity)		C
METAL		79		79		Iron-sulfur 1 (4Fe-4S) (By similarity)		C
METAL		94		94		Iron-sulfur 2 (4Fe-4S-S-AdoMet) (By similarity)		C
METAL		98		98		Iron-sulfur 2 (4Fe-4S-S-AdoMet) (By similarity)		C
METAL		101		101		Iron-sulfur 2 (4Fe-4S-S-AdoMet) (By similarity)		C

Size range:	276-373 amino acids
Related UniRules:	MF_04128 (LIAS (supersedes the current rule)); MF_04129 (LISC (supersedes the current rule)); MF_04123 (LIAS)
Template:	P60716 (LIPA_ECOLI); O32129 (LIPA_BACSU): [Recover all]
Scope:	Bacteria Archaea
Fusion:	Nter: None; Cter: None
Duplicate:	in NOSS1, BRAJA, GLOVI, PROMA, PROMM, PROMP, THEEB, SYNPX, SYNY3
Plasmid encoded:	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 Firmicutes) requires 3 enzymes: LipM (MF_02118), LipL (MF_02119) and LipA (MF_00206).