ID LISC_SORBI Reviewed; 368 AA. AC C5XKZ1; DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot. DT 01-SEP-2009, sequence version 1. DT 24-JAN-2024, entry version 78. 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}; GN OrderedLocusNames=Sb03g035760; OS Sorghum bicolor (Sorghum) (Sorghum vulgare). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade; OC Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum. OX NCBI_TaxID=4558; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. BTx623; RX PubMed=19189423; DOI=10.1038/nature07723; RA Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J., RA Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J., RA Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J., RA Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M., RA Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L., RA Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P., RA Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman M., RA Ware D., Westhoff P., Mayer K.F.X., Messing J., Rokhsar D.S.; RT "The Sorghum bicolor genome and the diversification of grasses."; RL Nature 457:551-556(2009). 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; CM000762; EES01528.1; -; Genomic_DNA. DR RefSeq; XP_002456408.1; XM_002456363.1. DR AlphaFoldDB; C5XKZ1; -. DR SMR; C5XKZ1; -. DR STRING; 4558.C5XKZ1; -. DR EnsemblPlants; EES01528; EES01528; SORBI_3003G309300. DR GeneID; 8072124; -. DR Gramene; EES01528; EES01528; SORBI_3003G309300. DR KEGG; sbi:8072124; -. DR eggNOG; KOG2672; Eukaryota. DR HOGENOM; CLU_033144_2_0_1; -. DR InParanoid; C5XKZ1; -. DR OMA; RSCAFCQ; -. DR OrthoDB; 575at2759; -. DR UniPathway; UPA00538; UER00593. DR Proteomes; UP000000768; Chromosome 3. DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell. 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 HAMAP; MF_03129; Lipoyl_synth_plantC; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM. 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:SF31; LIPOYL SYNTHASE 1, CHLOROPLASTIC; 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; Chloroplast; Iron; Iron-sulfur; Metal-binding; Plastid; KW Reference proteome; S-adenosyl-L-methionine; Transferase. FT CHAIN 1..368 FT /note="Lipoyl synthase, chloroplastic" FT /id="PRO_0000398870" FT DOMAIN 114..335 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 REGION 42..61 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 94 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 99 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 105 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 131 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 135 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 138 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 346 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 368 AA; 39528 MW; B63753E5085C935C CRC64; MQSSLARPLR PPVLAGCGGR RGHGAPRGSV SVARCRAEAA PPTVGTASRA PAGPYTGRDP EVKKPAWLRQ RAAQGDKYAR LRESIGELKL NTVCVEAQCP NIGECWNGGG GAGGEGDGIA TATIMVLGDT CTRGCRFCAV KTSNKPPPPD PLEPLNTALA VASWGVDYVV LTSVDRDDLP DGGSSHFAQT VRALKELKPG ILVECLTSDF RGDLEAVSSL ANSGLDVYAH NIETVRSLQR IVRDPRAGYD QSLAVLKHAK DCREGMITKS SIMLGLGETD EEVKQAMIDL RAIGVDILTL GQYLQPTERH LTVREYVTPE KFQFWKEYGE SVGFRYVASG PLVRSSYRAG ELFVQNLVRN NKTGSSSS //