LIAS_ARATH
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 03-AUG-2022, entry version 137.
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 = (R)-
CC N(6)-dihydrolipoyl-L-lysyl-[protein] + 2 5'-deoxyadenosine + [[Fe-S]
CC cluster scaffold protein] + 4 Fe(3+) + 2 hydrogen sulfide + 2 L-
CC methionine + 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.AT2G20860.1; -.
DR PaxDb; Q9ZWT1; -.
DR PRIDE; Q9ZWT1; -.
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; locus:2051384; AT2G20860.
DR eggNOG; KOG2672; Eukaryota.
DR HOGENOM; CLU_033144_1_0_1; -.
DR OMA; PYCDIDF; -.
DR OrthoDB; 610833at2759; -.
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 Genevisible; Q9ZWT1; AT.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:TAIR.
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:0102552; F:lipoyl synthase activity (acting on glycine-cleavage complex H protein; IEA:UniProtKB-EC.
DR GO; GO:0102553; F:lipoyl synthase activity (acting on pyruvate dehydrogenase E2 protein); IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006546; P:glycine catabolic process; TAS:TAIR.
DR GO; GO:0009107; P:lipoate biosynthetic process; IBA:GO_Central.
DR GO; GO:0009249; P:protein lipoylation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.20.20.70; -; 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/MiaB/NifB.
DR InterPro; IPR031691; LIAS_N.
DR InterPro; IPR003698; Lipoyl_synth.
DR InterPro; IPR027527; Lipoyl_synth_mt.
DR InterPro; IPR007197; rSAM.
DR PANTHER; PTHR10949; PTHR10949; 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 SMART; SM00729; Elp3; 1.
DR TIGRFAMs; TIGR00510; lipA; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
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
