ID LIAS_ARATH Reviewed; 374 AA. AC Q9ZWT1; DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 24-JAN-2024, entry version 144. DE RecName: Full=Lipoyl synthase, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03128}; DE EC=2.8.1.8 {ECO:0000255|HAMAP-Rule:MF_03128, ECO:0000269|PubMed:24872381, ECO:0000269|PubMed:9808738}; DE AltName: Full=Lipoate synthase {ECO:0000255|HAMAP-Rule:MF_03128}; DE Short=LS {ECO:0000255|HAMAP-Rule:MF_03128}; DE Short=Lip-syn {ECO:0000255|HAMAP-Rule:MF_03128}; DE AltName: Full=Lipoate-protein ligase {ECO:0000303|PubMed:24872381}; DE Short=AtLPLA {ECO:0000303|PubMed:24872381}; DE AltName: Full=Lipoic acid synthase {ECO:0000255|HAMAP-Rule:MF_03128}; DE Flags: Precursor; GN Name=LIP1 {ECO:0000255|HAMAP-Rule:MF_03128}; GN Synonyms=LPLA {ECO:0000303|PubMed:24872381}; GN OrderedLocusNames=At2g20860 {ECO:0000312|Araport:AT2G20860}; GN ORFNames=F5H14.17 {ECO:0000312|EMBL:AAD20909.1}; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE RP SPECIFICITY, AND SUBCELLULAR LOCATION. RX PubMed=9808738; DOI=10.1104/pp.118.3.935; RA Yasuno R., Wada H.; RT "Biosynthesis of lipoic acid in Arabidopsis: cloning and characterization RT of the cDNA for lipoic acid synthase."; RL Plant Physiol. 118:935-943(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=10617197; DOI=10.1038/45471; RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.; RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."; RL Nature 402:761-768(1999). RN [3] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RX PubMed=27862469; DOI=10.1111/tpj.13415; RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S., RA Town C.D.; RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference RT genome."; RL Plant J. 89:789-804(2017). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., RA Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [5] RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND RP DISRUPTION PHENOTYPE. RX PubMed=24872381; DOI=10.1104/pp.114.238311; RA Ewald R., Hoffmann C., Florian A., Neuhaus E., Fernie A.R., Bauwe H.; RT "Lipoate-protein ligase and octanoyltransferase are essential for protein RT lipoylation in mitochondria of Arabidopsis."; RL Plant Physiol. 165:978-990(2014). 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 (PubMed:9808738, CC PubMed:24872381) (By similarity). Together with LIP2 is essential for CC mitochondrial protein lipoylation during seed development. Required for CC the lipoylation of mitochondrial pyruvate dehydrogenase component E2 CC proteins in leaves and roots (PubMed:24872381). {ECO:0000255|HAMAP- CC Rule:MF_03128, ECO:0000269|PubMed:24872381, CC ECO:0000269|PubMed:9808738}. 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_03128, CC ECO:0000269|PubMed:24872381, ECO:0000269|PubMed:9808738}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_03128}; 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_03128}; 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_03128}. CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03128, CC ECO:0000269|PubMed:24872381, ECO:0000269|PubMed:9808738}. CC -!- TISSUE SPECIFICITY: Expressed in leaves and flowers, but not in roots CC (PubMed:9808738). Expressed in roots, rosette leaves, cauline leaves, CC stems, flowers and siliques (PubMed:24872381). CC {ECO:0000269|PubMed:24872381, ECO:0000269|PubMed:9808738}. CC -!- DISRUPTION PHENOTYPE: Embryonic lethality. CC {ECO:0000269|PubMed:24872381}. CC -!- SIMILARITY: Belongs to the radical SAM superfamily. Lipoyl synthase CC family. {ECO:0000255|HAMAP-Rule:MF_03128}. 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; AB007987; BAA34701.1; -; mRNA. DR EMBL; AC006234; AAD20909.1; -; Genomic_DNA. DR EMBL; CP002685; AEC07088.1; -; Genomic_DNA. DR EMBL; CP002685; ANM61393.1; -; Genomic_DNA. DR EMBL; CP002685; ANM61394.1; -; Genomic_DNA. DR EMBL; AY035143; AAK59647.1; -; mRNA. DR EMBL; AF424583; AAL11577.1; -; mRNA. DR EMBL; AY059077; AAL15183.1; -; mRNA. DR PIR; T44259; T44259. DR RefSeq; NP_001318257.1; NM_001335714.1. DR RefSeq; NP_001323612.1; NM_001335715.1. DR RefSeq; NP_179682.1; NM_127655.4. DR AlphaFoldDB; Q9ZWT1; -. DR SMR; Q9ZWT1; -. DR STRING; 3702.Q9ZWT1; -. DR iPTMnet; Q9ZWT1; -. DR PaxDb; 3702-AT2G20860-1; -. DR ProteomicsDB; 238459; -. DR EnsemblPlants; AT2G20860.1; AT2G20860.1; AT2G20860. DR EnsemblPlants; AT2G20860.2; AT2G20860.2; AT2G20860. DR EnsemblPlants; AT2G20860.3; AT2G20860.3; AT2G20860. DR GeneID; 816619; -. DR Gramene; AT2G20860.1; AT2G20860.1; AT2G20860. DR Gramene; AT2G20860.2; AT2G20860.2; AT2G20860. DR Gramene; AT2G20860.3; AT2G20860.3; AT2G20860. DR KEGG; ath:AT2G20860; -. DR Araport; AT2G20860; -. DR TAIR; AT2G20860; LIP1. DR eggNOG; KOG2672; Eukaryota. DR HOGENOM; CLU_033144_1_0_1; -. DR InParanoid; Q9ZWT1; -. DR OMA; PYCDIDF; -. DR OrthoDB; 575at2759; -. DR PhylomeDB; Q9ZWT1; -. DR BRENDA; 2.8.1.8; 399. DR UniPathway; UPA00538; UER00593. DR PRO; PR:Q9ZWT1; -. DR Proteomes; UP000006548; Chromosome 2. DR ExpressionAtlas; Q9ZWT1; baseline and differential. DR GO; GO:0005759; C:mitochondrial matrix; IDA:TAIR. 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 GO; GO:0006546; P:glycine catabolic process; TAS:TAIR. 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_03128; Lipoyl_synth_plantM; 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; IPR027527; Lipoyl_synth_mt. 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 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. DR Genevisible; Q9ZWT1; AT. PE 1: Evidence at protein level; KW 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Mitochondrion; KW Reference proteome; S-adenosyl-L-methionine; Transferase; Transit peptide. FT TRANSIT 1..19 FT /note="Mitochondrion" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03128" FT CHAIN 20..374 FT /note="Lipoyl synthase, mitochondrial" FT /id="PRO_0000398844" FT DOMAIN 119..339 FT /note="Radical SAM core" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266" FT BINDING 103 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P9WK91, ECO:0000255|HAMAP- FT Rule:MF_03128" FT BINDING 108 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P9WK91, ECO:0000255|HAMAP- FT Rule:MF_03128" FT BINDING 114 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P9WK91, ECO:0000255|HAMAP- FT Rule:MF_03128" FT BINDING 134 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|UniProtKB:P9WK91, ECO:0000255|HAMAP- FT Rule:MF_03128" 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:0000250|UniProtKB:P9WK91, ECO:0000255|HAMAP- FT Rule:MF_03128" FT BINDING 141 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|UniProtKB:P9WK91, ECO:0000255|HAMAP- FT Rule:MF_03128" FT BINDING 350 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P9WK91, ECO:0000255|HAMAP- FT Rule:MF_03128" SQ SEQUENCE 374 AA; 41344 MW; 9527359AA5E9AF6A CRC64; MHSRSALLYR FLRPASRCFS SSSAVTPVTV TQSPKSLEAL RARLANESPS LTDFIHGDTY SVEVGTKKKP LPKPKWMKES IPGGERYVQI KKKLRDLKLH TVCEEAKCPN LGECWSGGET GTATATIMIL GDTCTRGCRF CNVKTSRTPP PPDPNEPNNV AEAIASWGVD YVVITSVDRD DLPDQGSGHF AETVQRLKFL KPEMLIEALV PDFRGDGGCV EKVSKSGLDV LAHNIETVEE LQSFVRDHRA NFKQSLDVLR MAKEYAPAGT LTKTSVMLGC GETPDQVVKT MEKVRAAGVD VMTFGQYMRP SKRHMPVAEY VTPDAFERYR LLGMEMGFRY VASGPMVRSS YKAGEYYIKS MIEADRVASP STSP //