ID LIAS_RICCO Reviewed; 348 AA. AC B9RW49; DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot. DT 24-MAR-2009, sequence version 1. DT 24-JAN-2024, entry version 66. DE RecName: Full=Lipoyl synthase, mitochondrial; DE EC=2.8.1.8; DE AltName: Full=Lipoate synthase; DE Short=LS; DE Short=Lip-syn; DE AltName: Full=Lipoic acid synthase; DE Flags: Precursor; GN Name=LIP1; ORFNames=RCOM_1176060; OS Ricinus communis (Castor bean). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae; OC Ricinus. OX NCBI_TaxID=3988; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Hale; RX PubMed=20729833; DOI=10.1038/nbt.1674; RA Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D., RA Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M., RA Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J., RA Rabinowicz P.D.; RT "Draft genome sequence of the oilseed species Ricinus communis."; RL Nat. Biotechnol. 28:951-956(2010). 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:0000250}. 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 -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250}; 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:0000250}; CC -!- PATHWAY: Protein modification; protein lipoylation via endogenous CC pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier- CC protein]: step 2/2. CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. CC -!- SIMILARITY: Belongs to the radical SAM superfamily. Lipoyl synthase CC family. {ECO:0000305}. 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; EQ973822; EEF44486.1; -; Genomic_DNA. DR STRING; 3988.B9RW49; -. DR eggNOG; KOG2672; Eukaryota. DR InParanoid; B9RW49; -. DR UniPathway; UPA00538; UER00593. DR Proteomes; UP000008311; Unassembled WGS sequence. DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule. DR GO; GO:0016992; F:lipoate synthase activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0009107; P:lipoate biosynthetic process; IBA:GO_Central. 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:SF36; LIPOYL SYNTHASE, MITOCHONDRIAL; 1. DR Pfam; PF16881; LIAS_N; 1. DR Pfam; PF04055; Radical_SAM; 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; Mitochondrion; KW Reference proteome; S-adenosyl-L-methionine; Transferase; Transit peptide. FT TRANSIT 1..? FT /note="Mitochondrion" FT /evidence="ECO:0000255" FT CHAIN ?..348 FT /note="Lipoyl synthase, mitochondrial" FT /id="PRO_0000398855" FT DOMAIN 121..341 FT /note="Radical SAM core" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266" FT BINDING 105 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 110 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 116 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 136 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:0000250" FT BINDING 140 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:0000250" FT BINDING 143 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:0000250" SQ SEQUENCE 348 AA; 38584 MW; 05CAF5FBB2772DA3 CRC64; MFQSRFTILI RTLNSSKSRH FSSTIEPTKP QFPQTLAGLR ARLAAESPSL SEFSDLQSNN SYSVEVGTKK KPLPKPKWMR EAIPGGDKYV QIKKKLRELK LHTVCEEAKC PNLGECWSGG ETGTATATIM ILGDTCTRGC RFCNVKTSRT PPPPDPDEPA NVAEAIASWG LDYVVITSVD RDDLPDQGSN HFAQTVQKLK ALKPHMLIEA LVPDFRGDPG CVENVAKSGL DVFAHNIETV EDLQSVIRDH RANFKQSLDV LMMAKDHAPK GTLTKTSIML GCGETPEQVV KTMEKVRAAG VDVMTFGQYM RPSKRHMPVS EYVTPEAFEQ YRTXXLVSYV LFSLLISV //