ID A0A1C3FCL4_9BACT Unreviewed; 286 AA. AC A0A1C3FCL4; DT 02-NOV-2016, integrated into UniProtKB/TrEMBL. DT 02-NOV-2016, sequence version 1. DT 22-FEB-2023, entry version 30. DE RecName: Full=Lipoyl synthase {ECO:0000256|HAMAP-Rule:MF_00206}; DE EC=2.8.1.8 {ECO:0000256|HAMAP-Rule:MF_00206}; DE AltName: Full=Lip-syn {ECO:0000256|HAMAP-Rule:MF_00206}; DE Short=LS {ECO:0000256|HAMAP-Rule:MF_00206}; DE AltName: Full=Lipoate synthase {ECO:0000256|HAMAP-Rule:MF_00206}; DE AltName: Full=Lipoic acid synthase {ECO:0000256|HAMAP-Rule:MF_00206}; DE AltName: Full=Sulfur insertion protein LipA {ECO:0000256|HAMAP-Rule:MF_00206}; GN Name=lipA {ECO:0000256|HAMAP-Rule:MF_00206}; GN ORFNames=THER_1997 {ECO:0000313|EMBL:ODA43287.1}; OS Thermodesulfovibrio sp. N1. OC Bacteria; Nitrospirae; Thermodesulfovibrionia; Thermodesulfovibrionales; OC Thermodesulfovibrionaceae; Thermodesulfovibrio. OX NCBI_TaxID=1871110 {ECO:0000313|EMBL:ODA43287.1, ECO:0000313|Proteomes:UP000094295}; RN [1] {ECO:0000313|EMBL:ODA43287.1, ECO:0000313|Proteomes:UP000094295} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=N1 {ECO:0000313|EMBL:ODA43287.1, RC ECO:0000313|Proteomes:UP000094295}; RA Mardanov A.V., Karnachuk O.V., Beletsky A.V., Kadnikov V.V., Ravin N.V.; RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases. 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. {ECO:0000256|HAMAP- CC Rule:MF_00206}. 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 = (R)- CC N(6)-dihydrolipoyl-L-lysyl-[protein] + 2 5'-deoxyadenosine + [[Fe-S] CC cluster scaffold protein] + 4 Fe(3+) + 2 hydrogen sulfide + 2 L- CC methionine + 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 Evidence={ECO:0000256|ARBA:ARBA00001264, ECO:0000256|HAMAP- CC Rule:MF_00206}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00206}; CC Note=Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated CC with 3 cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000256|HAMAP-Rule:MF_00206}; CC -!- PATHWAY: Protein modification; protein lipoylation via endogenous CC pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier- CC protein]: step 2/2. {ECO:0000256|HAMAP-Rule:MF_00206}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00206}. CC -!- SIMILARITY: Belongs to the radical SAM superfamily. Lipoyl synthase CC family. {ECO:0000256|HAMAP-Rule:MF_00206}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:ODA43287.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; MAVV01000083; ODA43287.1; -; Genomic_DNA. DR RefSeq; WP_068861738.1; NZ_MAVV01000083.1. DR AlphaFoldDB; A0A1C3FCL4; -. DR STRING; 1871110.THER_1997; -. DR EnsemblBacteria; ODA43287; ODA43287; THER_1997. DR OrthoDB; 9787898at2; -. DR UniPathway; UPA00538; UER00593. DR Proteomes; UP000094295; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule. DR GO; GO:0016992; F:lipoate synthase activity; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0009249; P:protein lipoylation; IEA:UniProtKB-UniRule. DR CDD; cd01335; Radical_SAM; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR HAMAP; MF_00206; Lipoyl_synth; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM. DR InterPro; IPR003698; Lipoyl_synth. DR InterPro; IPR007197; rSAM. DR PANTHER; PTHR10949; LIPOYL SYNTHASE; 1. DR PANTHER; PTHR10949:SF0; LIPOYL SYNTHASE, MITOCHONDRIAL; 1. DR Pfam; PF04055; Radical_SAM; 1. DR SFLD; SFLDS00029; Radical_SAM; 1. DR SMART; SM00729; Elp3; 1. DR SUPFAM; SSF102114; Radical SAM enzymes; 1. DR TIGRFAMs; TIGR00510; lipA; 1. DR PROSITE; PS51918; RADICAL_SAM; 1. PE 3: Inferred from homology; KW 4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00206}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00206}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00206}; KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP- KW Rule:MF_00206}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00206}; KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP- KW Rule:MF_00206}; Transferase {ECO:0000256|HAMAP-Rule:MF_00206}. FT DOMAIN 42..257 FT /note="Radical SAM core" FT /evidence="ECO:0000259|PROSITE:PS51918" FT BINDING 30 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00206" FT BINDING 35 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00206" FT BINDING 41 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00206" FT BINDING 56 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /ligand_note="4Fe-4S-S-AdoMet" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00206" FT BINDING 60 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /ligand_note="4Fe-4S-S-AdoMet" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00206" FT BINDING 63 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /ligand_note="4Fe-4S-S-AdoMet" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00206" FT BINDING 268 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00206" SQ SEQUENCE 286 AA; 32399 MW; E55490198A6F77A8 CRC64; MPLPEWVKTQ LKELKKTQNF LKHRKLNTVC ETLRCPNRSI CYKEPTATFM ILGNVCTRRC KFCNAKRGNP EPLDFEEPSR IAQAVKELSL KYVVVTSPTR DDIEDGGAEH FVLTIREIRK INHDAQVEVL VPDFKGDINS IEKVINSEIA VFSHNIETVP SLYGYVRDGI YRRSLKVLES AKKLNSEMIT KSGFMVGLGE SLSEIFQTIK DLKNAGCDII TVGQYLQPSK KALPVVEYKK MEFFNQIADF ALKEGIKVVL SSPLIRSSTR AFEAFKAVKE GKYGKL //