ID LISC_OSTLU Reviewed; 324 AA. AC A4RW69; DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot. DT 15-MAY-2007, sequence version 1. DT 24-JAN-2024, entry version 89. DE RecName: Full=Lipoyl synthase, chloroplastic {ECO:0000255|HAMAP-Rule:MF_03129}; DE EC=2.8.1.8 {ECO:0000255|HAMAP-Rule:MF_03129}; DE AltName: Full=Lipoate synthase {ECO:0000255|HAMAP-Rule:MF_03129}; DE Short=LS {ECO:0000255|HAMAP-Rule:MF_03129}; DE Short=Lip-syn {ECO:0000255|HAMAP-Rule:MF_03129}; DE AltName: Full=Lipoate synthase, plastidial {ECO:0000255|HAMAP-Rule:MF_03129}; DE Short=LIP1p {ECO:0000255|HAMAP-Rule:MF_03129}; DE AltName: Full=Lipoic acid synthase {ECO:0000255|HAMAP-Rule:MF_03129}; GN Name=LIP1P {ECO:0000255|HAMAP-Rule:MF_03129}; ORFNames=OSTLU_31232; OS Ostreococcus lucimarinus (strain CCE9901). OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales; OC Bathycoccaceae; Ostreococcus. OX NCBI_TaxID=436017; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCE9901; RX PubMed=17460045; DOI=10.1073/pnas.0611046104; RA Palenik B., Grimwood J., Aerts A., Rouze P., Salamov A., Putnam N., RA Dupont C., Jorgensen R., Derelle E., Rombauts S., Zhou K., Otillar R., RA Merchant S.S., Podell S., Gaasterland T., Napoli C., Gendler K., RA Manuell A., Tai V., Vallon O., Piganeau G., Jancek S., Heijde M., RA Jabbari K., Bowler C., Lohr M., Robbens S., Werner G., Dubchak I., RA Pazour G.J., Ren Q., Paulsen I., Delwiche C., Schmutz J., Rokhsar D., RA Van de Peer Y., Moreau H., Grigoriev I.V.; RT "The tiny eukaryote Ostreococcus provides genomic insights into the paradox RT of plankton speciation."; RL Proc. Natl. Acad. Sci. U.S.A. 104:7705-7710(2007). 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_03129}. 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_03129}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_03129}; 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_03129}; 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_03129}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast. CC -!- MISCELLANEOUS: This protein may be expected to contain an N-terminal CC transit peptide but none has been predicted. {ECO:0000255|HAMAP- CC Rule:MF_03129}. CC -!- SIMILARITY: Belongs to the radical SAM superfamily. Lipoyl synthase CC family. {ECO:0000255|HAMAP-Rule:MF_03129}. 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; CP000584; ABO95567.1; -; Genomic_DNA. DR RefSeq; XP_001417274.1; XM_001417237.1. DR AlphaFoldDB; A4RW69; -. DR SMR; A4RW69; -. DR STRING; 436017.A4RW69; -. DR EnsemblPlants; ABO95567; ABO95567; OSTLU_31232. DR GeneID; 5001263; -. DR Gramene; ABO95567; ABO95567; OSTLU_31232. DR KEGG; olu:OSTLU_31232; -. DR eggNOG; KOG2672; Eukaryota. DR HOGENOM; CLU_033144_1_1_1; -. DR OMA; RSCAFCQ; -. DR OrthoDB; 575at2759; -. DR UniPathway; UPA00538; UER00593. DR Proteomes; UP000001568; Chromosome 4. DR GO; GO:0009507; C:chloroplast; 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 HAMAP; MF_03129; Lipoyl_synth_plantC; 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; IPR027526; Lipoyl_synth_chlpt. 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; 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; Chloroplast; Iron; Iron-sulfur; Metal-binding; Plastid; KW Reference proteome; S-adenosyl-L-methionine; Transferase. FT CHAIN 1..324 FT /note="Lipoyl synthase, chloroplastic" FT /id="PRO_0000398866" FT DOMAIN 72..291 FT /note="Radical SAM core" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266" FT REGION 1..30 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 58 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03129" FT BINDING 63 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03129" FT BINDING 69 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03129" FT BINDING 86 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_03129" FT BINDING 90 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_03129" FT BINDING 93 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_03129" FT BINDING 302 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03129" SQ SEQUENCE 324 AA; 35487 MW; A494F5444E1D46E5 CRC64; MCGPTATTVA NAGTGGETIK GLPPGLKKPP WLRQRAPSGE RFDYLSESLT GLKLNTVCEE AMCPNVGECW NGDTGTATVM LLGDTCTRGC RFCAVNTSQT PPPPDENEPE NTAHAIAEWG VGYIVLTSVD RDDIPDGGSE HFARTVRTLK TIKSSVLVEA LTPDFQGDMN AVAHLARSGL DVFAHNVETV ERLQKRVRDP RANYEQSLAV LRHAKASKEG LVTKTSIMLG LGEEDEEIKQ CMRACKEAGV DIFTLGQYLQ PTPQHLPVKE FVTPEKFDFW KAYGEEVIGF RYVASGPLVR SSYKAGEFFI ESMLRKDALD RGET //