ID LIPA_NITV2 Reviewed; 298 AA. AC Q72DM4; DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 04-NOV-2026, entry version 125. DE RecName: Full=Lipoyl synthase {ECO:0000255|HAMAP-Rule:MF_00206}; DE EC=2.8.1.8 {ECO:0000255|HAMAP-Rule:MF_00206}; DE AltName: Full=Lip-syn {ECO:0000255|HAMAP-Rule:MF_00206}; DE Short=LS {ECO:0000255|HAMAP-Rule:MF_00206}; DE AltName: Full=Lipoate synthase {ECO:0000255|HAMAP-Rule:MF_00206}; DE AltName: Full=Lipoic acid synthase {ECO:0000255|HAMAP-Rule:MF_00206}; DE AltName: Full=Sulfur insertion protein LipA {ECO:0000255|HAMAP-Rule:MF_00206}; GN Name=lipA {ECO:0000255|HAMAP-Rule:MF_00206}; GN OrderedLocusNames=DVU_0905; OS Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / OS NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris). OC Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfovibrionia; OC Desulfovibrionales; Desulfovibrionaceae; Nitratidesulfovibrio. OX NCBI_TaxID=882; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / RC Hildenborough; RX PubMed=15077118; DOI=10.1038/nbt959; RA Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T., RA Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M., RA Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R., RA Nelson W.C., Sullivan S.A., Fouts D.E., Haft D.H., Selengut J., RA Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G., RA Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R., Feldblyum T.V., RA Wall J.D., Voordouw G., Fraser C.M.; RT "The genome sequence of the anaerobic, sulfate-reducing bacterium RT Desulfovibrio vulgaris Hildenborough."; RL Nat. Biotechnol. 22:554-559(2004). 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:0000255|HAMAP- CC Rule:MF_00206}. CC -!- CATALYTIC ACTIVITY: CC Reaction=[[Fe-S] cluster scaffold protein carrying a second [4Fe- CC 4S](2+) cluster] + N(6)-octanoyl-L-lysyl-[protein] + 2 oxidized [2Fe- CC 2S]-[ferredoxin] + 2 S-adenosyl-L-methionine + 4 H(+) = [[Fe-S] CC cluster scaffold protein] + N(6)-[(R)-dihydrolipoyl]-L-lysyl- CC [protein] + 4 Fe(3+) + 2 hydrogen sulfide + 2 5'-deoxyadenosine + 2 CC L-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:0000255|HAMAP-Rule:MF_00206}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_00206}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00206}. CC -!- SIMILARITY: Belongs to the radical SAM superfamily. Lipoyl synthase CC family. {ECO:0000255|HAMAP-Rule:MF_00206}. 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; AE017285; AAS95385.1; -; Genomic_DNA. DR RefSeq; WP_010938204.1; NC_002937.3. DR AlphaFoldDB; Q72DM4; -. DR SMR; Q72DM4; -. DR STRING; 882.DVU_0905; -. DR PaxDb; 882-DVU_0905; -. DR EnsemblBacteria; AAS95385; AAS95385; DVU_0905. DR KEGG; dvu:DVU_0905; -. DR PATRIC; fig|882.5.peg.849; -. DR eggNOG; COG0320; Bacteria. DR HOGENOM; CLU_033144_2_1_7; -. DR OMA; AACPNIW; -. DR OrthoDB; 9787898at2; -. DR PhylomeDB; Q72DM4; -. DR UniPathway; UPA00538; UER00593. DR Proteomes; UP000002194; Chromosome. 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:0009249; P:protein lipoylation; IEA:UniProtKB-UniRule. DR CDD; cd01335; Radical_SAM; 1. DR FunFam; 3.20.20.70:FF:000186; Lipoyl synthase; 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 InterPro; IPR058240; rSAM_sf. DR NCBIfam; TIGR00510; lipA; 1. DR NCBIfam; NF004019; PRK05481.1; 1. DR NCBIfam; NF009544; PRK12928.1; 1. DR PANTHER; PTHR10949; LIPOYL SYNTHASE; 1. DR PANTHER; PTHR10949:SF0; LIPOYL SYNTHASE, MITOCHONDRIAL; 1. DR Pfam; PF04055; Radical_SAM; 1. DR PIRSF; PIRSF005963; Lipoyl_synth; 1. DR SFLD; SFLDF00271; lipoyl_synthase; 1. DR SFLD; SFLDG01058; lipoyl_synthase_like; 1. DR SFLD; SFLDS00029; Radical_SAM; 1. DR SMART; SM00729; Elp3; 1. DR SUPFAM; SSF102114; Radical SAM enzymes; 1. DR PROSITE; PS51918; RADICAL_SAM; 1. PE 3: Inferred from homology; KW 4Fe-4S; Cytoplasm; Iron; Iron-sulfur; Metal-binding; Reference proteome; KW S-adenosyl-L-methionine; Transferase. FT CHAIN 1..298 FT /note="Lipoyl synthase" FT /id="PRO_0000325247" FT DOMAIN 55..269 FT /note="Radical SAM core" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266" FT BINDING 43 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00206" FT BINDING 48 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00206" FT BINDING 54 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00206" FT BINDING 69 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:0000255|HAMAP-Rule:MF_00206" FT BINDING 73 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:0000255|HAMAP-Rule:MF_00206" FT BINDING 76 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:0000255|HAMAP-Rule:MF_00206" FT BINDING 280 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00206" SQ SEQUENCE 298 AA; 32017 MW; 566B03D04879200B CRC64; MSSPDNSSPS LRIPPWLRVK LPCSHTFADT RALVEGLGLN TVCNSAKCPN MFECFSSGTA TFLILGNVCT RNCAFCNITP GHVSPPDPDE PRRVAEAAAR LALRHVVVTS VTRDDLDDGG AAHFAATITR LRAALPAATV EVLIPDFRGD HAALRTVMAA APHIVNHNVE TPPAHYARIR PQADYRQSLE LLRRVKAAGG VAKSGLMVGL GENDTEVEGV LADLADCGCD IVTIGQYMRP SRQHPPVERY VHPDTFESFA ACGRGMGIPF VFSAPLVRSS YNAESAYNAL CTLRTEPA //