ID LIAS_SCHMA Reviewed; 410 AA. AC C4PZQ3; G4VET5; DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot. DT 07-JUL-2009, sequence version 1. DT 24-JAN-2024, entry version 87. DE RecName: Full=Lipoyl synthase, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03123}; DE EC=2.8.1.8 {ECO:0000255|HAMAP-Rule:MF_03123}; DE AltName: Full=Lipoate synthase {ECO:0000255|HAMAP-Rule:MF_03123}; DE Short=LS {ECO:0000255|HAMAP-Rule:MF_03123}; DE Short=Lip-syn {ECO:0000255|HAMAP-Rule:MF_03123}; DE AltName: Full=Lipoic acid synthase {ECO:0000255|HAMAP-Rule:MF_03123}; GN ORFNames=Smp_010100; OS Schistosoma mansoni (Blood fluke). OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda; OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma. OX NCBI_TaxID=6183; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Puerto Rican; RX PubMed=19606141; DOI=10.1038/nature08160; RA Berriman M., Haas B.J., LoVerde P.T., Wilson R.A., Dillon G.P., RA Cerqueira G.C., Mashiyama S.T., Al-Lazikani B., Andrade L.F., Ashton P.D., RA Aslett M.A., Bartholomeu D.C., Blandin G., Caffrey C.R., Coghlan A., RA Coulson R., Day T.A., Delcher A., DeMarco R., Djikeng A., Eyre T., RA Gamble J.A., Ghedin E., Gu Y., Hertz-Fowler C., Hirai H., Hirai Y., RA Houston R., Ivens A., Johnston D.A., Lacerda D., Macedo C.D., McVeigh P., RA Ning Z., Oliveira G., Overington J.P., Parkhill J., Pertea M., Pierce R.J., RA Protasio A.V., Quail M.A., Rajandream M.A., Rogers J., Sajid M., RA Salzberg S.L., Stanke M., Tivey A.R., White O., Williams D.L., Wortman J., RA Wu W., Zamanian M., Zerlotini A., Fraser-Liggett C.M., Barrell B.G., RA El-Sayed N.M.; RT "The genome of the blood fluke Schistosoma mansoni."; RL Nature 460:352-358(2009). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Puerto Rican; RX PubMed=22253936; DOI=10.1371/journal.pntd.0001455; RA Protasio A.V., Tsai I.J., Babbage A., Nichol S., Hunt M., Aslett M.A., RA De Silva N., Velarde G.S., Anderson T.J., Clark R.C., Davidson C., RA Dillon G.P., Holroyd N.E., LoVerde P.T., Lloyd C., McQuillan J., RA Oliveira G., Otto T.D., Parker-Manuel S.J., Quail M.A., Wilson R.A., RA Zerlotini A., Dunne D.W., Berriman M.; RT "A systematically improved high quality genome and transcriptome of the RT human blood fluke Schistosoma mansoni."; RL PLoS Negl. Trop. Dis. 6:E1455-E1455(2012). 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_03123}. 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_03123}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_03123}; 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_03123}; 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_03123}. CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03123}. 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_03123}. CC -!- SIMILARITY: Belongs to the radical SAM superfamily. Lipoyl synthase CC family. {ECO:0000255|HAMAP-Rule:MF_03123}. 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; HE601626; CCD78443.1; -; Genomic_DNA. DR RefSeq; XP_018651054.1; XM_018799246.1. DR AlphaFoldDB; C4PZQ3; -. DR SMR; C4PZQ3; -. DR STRING; 6183.C4PZQ3; -. DR GeneID; 8353012; -. DR KEGG; smm:Smp_010100; -. DR CTD; 8353012; -. DR eggNOG; KOG2672; Eukaryota. DR HOGENOM; CLU_033144_1_2_1; -. DR InParanoid; C4PZQ3; -. DR OMA; PYCDIDF; -. DR OrthoDB; 575at2759; -. DR PhylomeDB; C4PZQ3; -. DR UniPathway; UPA00538; UER00593. DR Proteomes; UP000008854; Chromosome 3. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell. 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 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:SF0; 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. PE 3: Inferred from homology; KW 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Mitochondrion; KW Reference proteome; S-adenosyl-L-methionine; Transferase. FT CHAIN 1..410 FT /note="Lipoyl synthase, mitochondrial" FT /id="PRO_0000398229" FT DOMAIN 148..379 FT /note="Radical SAM core" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266" FT BINDING 134 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03123" FT BINDING 139 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03123" FT BINDING 145 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03123" FT BINDING 165 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_03123" FT BINDING 169 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_03123" FT BINDING 172 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_03123" FT BINDING 390 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03123" SQ SEQUENCE 410 AA; 45769 MW; 727583BC7ADF758F CRC64; MGLLLPRGSY VFPVLASVSA ATKRRAEWSY IKINITHSYS SNDKSSEFEE DNPTQKLSPE FQKAIAHGPS LSEFIKLSNN NQSTKEDFFS SPSSVNKSGK SLRLPEWLKT EIPCGGSVAR LQKQLRSLNL HTVCEEARCP NISECWTAGK STAATATIMI MGDTCTRGCR FCSVKTSPNP PPLDPDEPVN TAEAISKWDV DYIVITSVDR DDLGDGGARH IAKTIRQIKV RKPSIIVECL VPDFRGCTDS IHTVVRASPE VYAHNIETVE SLQRVVRDHR AGYIQSLRSL ETAKERSNRL VSSGDADFLV VTKSSIMLGL GEKEKEVMIA LKDLRQAGVD CVTIGQYVQP TKRHLKVKEY IHPDKFDYWA KIGNDLGFLY TASGPLVRSS YRAGEYYIKH IIDQRKRKNI //