ID LIAS_MAIZE Reviewed; 383 AA. AC B8A031; DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot. DT 03-MAR-2009, sequence version 1. DT 24-JAN-2024, entry version 88. DE RecName: Full=Lipoyl synthase, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03128}; DE EC=2.8.1.8 {ECO:0000255|HAMAP-Rule:MF_03128}; 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=Lipoic acid synthase {ECO:0000255|HAMAP-Rule:MF_03128}; GN Name=LIP1 {ECO:0000255|HAMAP-Rule:MF_03128}; OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade; OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea. OX NCBI_TaxID=4577; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=B73; RX PubMed=19936069; DOI=10.1371/journal.pgen.1000740; RA Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J., RA Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J., RA Walbot V., Yu Y.; RT "Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs."; RL PLoS Genet. 5:E1000740-E1000740(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_03128}. 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 -!- 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 -!- 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_03128}. 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; BT054923; ACL53530.1; -; mRNA. DR EMBL; BT061114; ACN25811.1; -; mRNA. DR EMBL; BT086520; ACR36873.1; -; mRNA. DR RefSeq; NP_001146235.1; NM_001152763.1. DR AlphaFoldDB; B8A031; -. DR SMR; B8A031; -. DR STRING; 4577.B8A031; -. DR PaxDb; 4577-GRMZM2G071714_P01; -. DR EnsemblPlants; Zm00001eb081090_T001; Zm00001eb081090_P001; Zm00001eb081090. DR GeneID; 100279807; -. DR Gramene; Zm00001eb081090_T001; Zm00001eb081090_P001; Zm00001eb081090. DR KEGG; zma:100279807; -. DR eggNOG; KOG2672; Eukaryota. DR HOGENOM; CLU_033144_2_0_1; -. DR InParanoid; B8A031; -. DR OMA; PYCDIDF; -. DR OrthoDB; 575at2759; -. DR UniPathway; UPA00538; UER00593. DR Proteomes; UP000007305; Chromosome 2. DR ExpressionAtlas; B8A031; baseline and differential. DR GO; GO:0005759; C:mitochondrial matrix; IEA:EnsemblPlants. 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_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 SFLD; SFLDF00271; lipoyl_synthase; 1. DR SFLD; SFLDS00029; Radical_SAM; 1. DR SMART; SM00729; Elp3; 1. DR SUPFAM; SSF102114; Radical SAM enzymes; 1. DR PROSITE; PS51918; RADICAL_SAM; 1. DR Genevisible; B8A031; ZM. PE 2: Evidence at transcript level; KW 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Mitochondrion; KW Reference proteome; S-adenosyl-L-methionine; Transferase. FT CHAIN 1..383 FT /note="Lipoyl synthase, mitochondrial" FT /id="PRO_0000398846" FT DOMAIN 126..346 FT /note="Radical SAM core" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266" FT REGION 25..44 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 110 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03128" FT BINDING 115 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03128" FT BINDING 121 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-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:0000255|HAMAP-Rule:MF_03128" FT BINDING 145 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_03128" FT BINDING 148 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_03128" FT BINDING 357 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03128" SQ SEQUENCE 383 AA; 41886 MW; D049717212C2F537 CRC64; MHGRRHLAAS LTRALIQAPS RSISSTPSLL QTLDPSVPSP PAAGAGRLAE LRRRLQADAP SLGDFTYSVE VGTRQRPLPK PKWMKETVPG GAKYAAIKAK LRELKLHTVC EEARCPNLGE CWSGGETGTA TATIMILGDT CTRGCRFCNV KTSRTPPPPD PDEPSNVAQA IASWGLEYIV ITSVDRDDLP DQGSGHFAET VQKLKALKPE MLIEALVPDF RGDPSCVEKV ATSGLHVFAH NIETVEELQR NVRDYRANFK QSIDVLEMAK EYAPPGTLTK TSIMLGCGET PDQVIRTMEK VRAADVDVIT FGQYMRPSKR HMPVSEYVTP EAFEKYRALG VEMGFRYVAS GPMVRSSYKA GEFYIKAMIE AERAKGTAAD SSA //