AC MF_00206; DC Protein; auto c? or TR HAMAP; MF_00206; -; 1; level=0 XX Names: Lipoyl_synth XX ID LIPA DE RecName: Full=Lipoyl synthase; DE EC=2.8.1.8; DE AltName: Full=Lip-syn; DE Short=LS; DE AltName: Full=Lipoate synthase; DE AltName: Full=Lipoic acid synthase; DE AltName: Full=Sulfur insertion protein LipA; GN Name=lipA; XX CC -!- FUNCTION: Catalyzes the radical-mediated insertion of two sulfur atoms CC into the C-6 and C-8 positions of the octanoyl moiety bound to the CC lipoyl domains of lipoate-dependent enzymes, thereby converting the CC octanoylated domains into lipoylated derivatives. CC -!- CATALYTIC ACTIVITY: CC Reaction=[[Fe-S] cluster scaffold protein carrying a second [4Fe- CC 4S](2+) cluster] + 4 H(+) + N(6)-octanoyl-L-lysyl-[protein] + 2 CC oxidized [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2 5'- CC deoxyadenosine + [[Fe-S] cluster scaffold protein] + 4 Fe(3+) + 2 CC hydrogen sulfide + 2 L-methionine + N(6)-[(R)-dihydrolipoyl]-L-lysyl- CC [protein] + 2 reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:16585, CC Rhea:RHEA-COMP:9928, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, CC Rhea:RHEA-COMP:10475, Rhea:RHEA-COMP:14568, Rhea:RHEA-COMP:14569, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17319, ChEBI:CHEBI:29034, CC ChEBI:CHEBI:29919, ChEBI:CHEBI:33722, ChEBI:CHEBI:33737, CC ChEBI:CHEBI:33738, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:78809, ChEBI:CHEBI:83100; EC=2.8.1.8; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Note=Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated CC with 3 cysteines and an exchangeable S-adenosyl-L-methionine.; case CC -!- PATHWAY: Protein modification; protein lipoylation via endogenous CC pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier- CC protein]. else CC -!- PATHWAY: Protein modification; protein lipoylation via endogenous CC pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier- CC protein]: step 2/2. end case CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the radical SAM superfamily. Lipoyl synthase CC family. XX DR Pfam; PF04055; Radical_SAM; 1; trigger=no DR NCBIfam; TIGR00510; LipA; 1; trigger=no XX KW 4Fe-4S KW Cytoplasm KW Iron KW Iron-sulfur KW Metal-binding KW S-adenosyl-L-methionine KW Transferase XX GO GO:0016783; F:sulfurtransferase activity GO GO:0016992; F:lipoate synthase activity GO GO:0051539; F:4 iron, 4 sulfur cluster binding GO GO:0009107; P:lipoate biosynthetic process GO GO:0009249; P:protein lipoylation GO GO:0005737; C:cytoplasm XX FT From: LIPA_MYCTU (P9WK91) FT BINDING 55 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT Condition: C FT BINDING 60 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT Condition: C FT BINDING 66 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT Condition: C FT BINDING 81 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /ligand_note="4Fe-4S-S-AdoMet" FT Condition: C FT BINDING 85 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /ligand_note="4Fe-4S-S-AdoMet" FT Condition: C FT BINDING 88 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /ligand_note="4Fe-4S-S-AdoMet" FT Condition: C FT BINDING 292 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT Condition: S XX Size: 276-373; Related: MF_03128!; MF_03129!; Template: P60716; O32129; P9WK91; Q8DLC2; Q97U63; Scope: Bacteria Archaea Fusion: Nter: None Cter: None Duplicate: in NOSS1, BRADU, GLOVI, PROMA, PROMM, PROMP, THEVB, PARMW, SYNY3 Plasmid: 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). XX # Revision 1.60 2023/09/14 //