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HAMAP rule MF_00206

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General rule information [?]

Accession MF_00206
Dates 1-JUN-2001 (Created)
14-SEP-2023 (Last updated, Version 60)
Name Lipoyl_synth
Scope(s) Bacteria
Template(s) P60716 (LIPA_ECOLI); O32129 (LIPA_BACSU); P9WK91 (LIPA_MYCTU); Q8DLC2 (LIPA2_THEVB); Q97U63 (LIPA_SACS2); [ Recover all ]
Triggered by
case c? <OC:Bacteria> or <OC:Archaea>
HAMAP; MF_00206 (Get profile general information and statistics)
end case

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier LIPA
Protein name RecName: Full=Lipoyl synthase;
AltName: Full=Lip-syn;
AltName: Full=Lipoate synthase;
AltName: Full=Lipoic acid synthase;
AltName: Full=Sulfur insertion protein LipA;
Gene name Name=lipA;

Comments [?]

FUNCTIONCatalyzes 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.
CATALYTIC ACTIVITY Reaction=[[Fe-S] cluster scaffold protein carrying a second [4Fe- 4S](2+) cluster] + 4 H(+) + N(6)-octanoyl-L-lysyl-[protein] + 2 oxidized [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2 5'- deoxyadenosine + [[Fe-S] cluster scaffold protein] + 4 Fe(3+) + 2 hydrogen sulfide + 2 L-methionine + N(6)-[(R)-dihydrolipoyl]-L-lysyl- [protein] + 2 reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:16585, Rhea:RHEA-COMP:9928, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, Rhea:RHEA-COMP:10475, Rhea:RHEA-COMP:14568, Rhea:RHEA-COMP:14569, ChEBI:CHEBI:15378, ChEBI:CHEBI:17319, ChEBI:CHEBI:29034, ChEBI:CHEBI:29919, ChEBI:CHEBI:33722, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789, ChEBI:CHEBI:78809, ChEBI:CHEBI:83100; EC=;
COFACTOR Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Note=Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.;
case <OC:Bacillales>
PATHWAYProtein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier- protein].
PATHWAYProtein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier- protein]: step 2/2.
end case
SIMILARITYBelongs to the radical SAM superfamily. Lipoyl synthase family.

Keywords [?]

Gene Ontology [?]

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

Cross-references [?]

Pfam PF04055; Radical_SAM; 1;
NCBIfam TIGR00510; LipA; 1;

Features [?]

Key From To Description Tag Condition FTGroup
BINDING 55 55 /ligand="[4Fe-4S] cluster"
BINDING 60 60 /ligand="[4Fe-4S] cluster"
BINDING 66 66 /ligand="[4Fe-4S] cluster"
BINDING 81 81 /ligand="[4Fe-4S] cluster"
BINDING 85 85 /ligand="[4Fe-4S] cluster"
BINDING 88 88 /ligand="[4Fe-4S] cluster"
BINDING 292 292 /ligand="[4Fe-4S] cluster"

Additional information [?]

Size range 276-373 amino acids
Related rules MF_03128
Fusion Nter: None Cter: 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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