ID LIPA_PAUCH Reviewed; 291 AA. AC B1X4X1; DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot. DT 20-MAY-2008, sequence version 1. DT 24-JAN-2024, entry version 65. DE RecName: Full=Lipoyl synthase, organellar chromatophore {ECO:0000255|HAMAP-Rule:MF_03123}; DE EC=2.8.1.8 {ECO:0000255|HAMAP-Rule:MF_03123}; DE AltName: Full=Lipoate synthase {ECO:0000255|HAMAP-Rule:MF_03123}; DE Short=LS {ECO:0000255|HAMAP-Rule:MF_03123}; DE Short=Lip-syn {ECO:0000255|HAMAP-Rule:MF_03123}; DE AltName: Full=Lipoic acid synthase {ECO:0000255|HAMAP-Rule:MF_03123}; GN OrderedLocusNames=PCC_0559; OS Paulinella chromatophora. OG Plastid; Organellar chromatophore. OC Eukaryota; Sar; Rhizaria; Cercozoa; Imbricatea; Silicofilosea; Euglyphida; OC Paulinellidae; Paulinella. OX NCBI_TaxID=39717; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=18356055; DOI=10.1016/j.cub.2008.02.051; RA Nowack E.C.M., Melkonian M., Gloeckner G.; RT "Chromatophore genome sequence of Paulinella sheds light on acquisition of RT photosynthesis by eukaryotes."; RL Curr. Biol. 18:410-418(2008). 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_03123}. 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_03123}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_03123}; 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_03123}; 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_03123}. CC -!- SUBCELLULAR LOCATION: Plastid, organellar chromatophore. CC -!- SIMILARITY: Belongs to the radical SAM superfamily. Lipoyl synthase CC family. {ECO:0000255|HAMAP-Rule:MF_03123}. 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; CP000815; ACB42990.1; -; Genomic_DNA. DR RefSeq; YP_002049200.1; NC_011087.1. DR AlphaFoldDB; B1X4X1; -. DR SMR; B1X4X1; -. DR GeneID; 6481678; -. DR UniPathway; UPA00538; UER00593. DR GO; GO:0070111; C:organellar chromatophore; IEA:UniProtKB-SubCell. DR GO; GO:0009536; C:plastid; IEA:UniProtKB-KW. 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; 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; 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; Iron; Iron-sulfur; Metal-binding; Organellar chromatophore; KW Plastid; S-adenosyl-L-methionine; Transferase. FT CHAIN 1..291 FT /note="Lipoyl synthase, organellar chromatophore" FT /id="PRO_0000398235" FT DOMAIN 45..263 FT /note="Radical SAM core" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266" FT BINDING 33 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03123" FT BINDING 38 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03123" FT BINDING 44 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03123" FT BINDING 59 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_03123" 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:0000255|HAMAP-Rule:MF_03123" FT BINDING 66 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_03123" FT BINDING 274 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03123" SQ SEQUENCE 291 AA; 32395 MW; C3D08984BC910713 CRC64; MLKPTWLRVK APQKERIGTI NRLLTDLKLN TVCEEASCPN IGECFAGGTA TFLIMGPGCT RACPYCDIDF DKSIRTVDHT EPTRIGEAVS RMRLKHVVIT SVNRDDLADG GASHFVACIA AVRAASPTTT IEVLIPDFCG NLNSIDKVLA AKPEIINHNI ETVPRIYNRV RPQGVYQRSL YLLDWIKSND KNLYTKSGLM VGLGEIDAEV LEVMADLRAI QVDVVTIGQY LSPGSKHLPI DRFVTPTQFD NYKAIGELEM NFLQVVSTPL TRSSYHSGEF RNLMRDNPRQ N //