ID A0A1C3FCL4_9BACT Unreviewed; 286 AA. AC A0A1C3FCL4; DT 02-NOV-2016, integrated into UniProtKB/TrEMBL. DT 02-NOV-2016, sequence version 1. DT 28-FEB-2018, entry version 11. 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; Nitrospirales; Nitrospiraceae; OC 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 Florea S., Webb J.S., Jaromczyk J., Schardl C.L.; RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the radical-mediated insertion of two sulfur CC atoms into the C-6 and C-8 positions of the octanoyl moiety bound CC to the lipoyl domains of lipoate-dependent enzymes, thereby CC converting the octanoylated domains into lipoylated derivatives. CC {ECO:0000256|HAMAP-Rule:MF_00206}. CC -!- CATALYTIC ACTIVITY: Protein N(6)-(octanoyl)lysine + 2 sulfur- CC (sulfur carrier) + 2 S-adenosyl-L-methionine + 2 reduced [2Fe-2S] CC ferredoxin = protein N(6)-(lipoyl)lysine + 2 (sulfur carrier) + 2 CC L-methionine + 2 5'-deoxyadenosine + 2 oxidized [2Fe-2S] CC ferredoxin. {ECO:0000256|HAMAP-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 CC coordinated with 3 cysteines and an exchangeable S-adenosyl-L- CC methionine. {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 ECO:0000256|SAAS:SAAS00921108}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00206}. CC -!- SIMILARITY: Belongs to the radical SAM superfamily. Lipoyl CC synthase family. {ECO:0000256|HAMAP-Rule:MF_00206}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 EnsemblBacteria; ODA43287; ODA43287; THER_1997. 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 Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00206; Lipoyl_synth; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR003698; Lipoyl_synth. DR InterPro; IPR007197; rSAM. DR Pfam; PF04055; Radical_SAM; 1. DR SFLD; SFLDS00029; Radical_SAM; 1. DR SMART; SM00729; Elp3; 1. DR TIGRFAMs; TIGR00510; lipA; 1. PE 3: Inferred from homology; KW 4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00206}; KW Complete proteome {ECO:0000313|Proteomes:UP000094295}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00206}; KW Iron {ECO:0000256|HAMAP-Rule:MF_00206}; KW Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00206}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00206}; KW Reference proteome {ECO:0000313|Proteomes:UP000094295}; KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00206}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00206}. FT DOMAIN 46 249 Elp3. {ECO:0000259|SMART:SM00729}. FT METAL 30 30 Iron-sulfur 1 (4Fe-4S). FT {ECO:0000256|HAMAP-Rule:MF_00206}. FT METAL 35 35 Iron-sulfur 1 (4Fe-4S). FT {ECO:0000256|HAMAP-Rule:MF_00206}. FT METAL 41 41 Iron-sulfur 1 (4Fe-4S). FT {ECO:0000256|HAMAP-Rule:MF_00206}. FT METAL 56 56 Iron-sulfur 2 (4Fe-4S-S-AdoMet). FT {ECO:0000256|HAMAP-Rule:MF_00206}. FT METAL 60 60 Iron-sulfur 2 (4Fe-4S-S-AdoMet). FT {ECO:0000256|HAMAP-Rule:MF_00206}. FT METAL 63 63 Iron-sulfur 2 (4Fe-4S-S-AdoMet). FT {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 //