ID LIPA_EHRRW Reviewed; 292 AA. AC Q5HB02; Q5FEQ5; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-FEB-2005, sequence version 1. DT 27-MAR-2024, entry version 113. 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=Erum5290, ERWE_CDS_05550; OS Ehrlichia ruminantium (strain Welgevonden). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales; OC Anaplasmataceae; Ehrlichia. OX NCBI_TaxID=254945; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Welgevonden; RX PubMed=15637156; DOI=10.1073/pnas.0406633102; RA Collins N.E., Liebenberg J., de Villiers E.P., Brayton K.A., Louw E., RA Pretorius A., Faber F.E., van Heerden H., Josemans A., van Kleef M., RA Steyn H.C., van Strijp M.F., Zweygarth E., Jongejan F., Maillard J.C., RA Berthier D., Botha M., Joubert F., Corton C.H., Thomson N.R., Allsopp M.T., RA Allsopp B.A.; RT "The genome of the heartwater agent Ehrlichia ruminantium contains multiple RT tandem repeats of actively variable copy number."; RL Proc. Natl. Acad. Sci. U.S.A. 102:838-843(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Welgevonden; RX PubMed=16547041; DOI=10.1128/jb.188.7.2533-2542.2006; RA Frutos R., Viari A., Ferraz C., Morgat A., Eychenie S., Kandassamy Y., RA Chantal I., Bensaid A., Coissac E., Vachiery N., Demaille J., Martinez D.; RT "Comparative genomic analysis of three strains of Ehrlichia ruminantium RT reveals an active process of genome size plasticity."; RL J. Bacteriol. 188:2533-2542(2006). 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] + 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 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; CR767821; CAH58258.1; -; Genomic_DNA. DR EMBL; CR925678; CAI27049.1; -; Genomic_DNA. DR RefSeq; WP_011155209.1; NC_006832.1. DR AlphaFoldDB; Q5HB02; -. DR SMR; Q5HB02; -. DR KEGG; eru:Erum5290; -. DR KEGG; erw:ERWE_CDS_05550; -. DR eggNOG; COG0320; Bacteria. DR HOGENOM; CLU_033144_2_1_5; -. DR UniPathway; UPA00538; UER00593. DR Proteomes; UP000001021; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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; IPR031691; LIAS_N. DR InterPro; IPR003698; Lipoyl_synth. DR InterPro; IPR007197; rSAM. DR NCBIfam; TIGR00510; lipA; 1. DR PANTHER; PTHR10949; LIPOYL SYNTHASE; 1. DR PANTHER; PTHR10949:SF0; LIPOYL SYNTHASE, MITOCHONDRIAL; 1. DR Pfam; PF16881; LIAS_N; 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 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; KW S-adenosyl-L-methionine; Transferase. FT CHAIN 1..292 FT /note="Lipoyl synthase" FT /id="PRO_1000012219" FT DOMAIN 46..262 FT /note="Radical SAM core" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266" FT BINDING 34 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 39 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 45 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 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:0000255|HAMAP-Rule:MF_00206" FT BINDING 64 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 67 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 273 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 292 AA; 33219 MW; 0255F7BAF478899C CRC64; MKSKPDWLKV KMPTGSAFYE MRNLMKLHKL NTVCEEAACP NIGECWNKKH ATVMILGSTC TRACAFCNVA SGIPDKLDPH EPQSLAKAVS SLKLQHVVIT SVDRDDLEDG GAGHFVECIE EIRKRDSNVT IEILTPDFLN KHDAIDKIAK AFPDVYNHNV ETVPRLYAKI RPKARYFHSL YLLKTIKQKN PRIFTKSGIM VGLGELKEEI YQVMDDLRSA DVDFIVIGQY LQPTSKHAVV DRYVTPEEFD HYKYVAYSKG FLMVASGPLV RSSYHAEEDF QRLKKNRAAM YT //