ID LIPA_PORGI Reviewed; 282 AA. AC Q7MWT4; DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-2003, sequence version 1. DT 27-MAR-2024, entry version 125. DE RecName: Full=Lipoyl synthase {ECO:0000255|HAMAP-Rule:MF_00206}; DE EC=2.8.1.8 {ECO:0000255|HAMAP-Rule:MF_00206}; DE AltName: Full=Lip-syn {ECO:0000255|HAMAP-Rule:MF_00206}; DE Short=LS {ECO:0000255|HAMAP-Rule:MF_00206}; DE AltName: Full=Lipoate synthase {ECO:0000255|HAMAP-Rule:MF_00206}; DE AltName: Full=Lipoic acid synthase {ECO:0000255|HAMAP-Rule:MF_00206}; DE AltName: Full=Sulfur insertion protein LipA {ECO:0000255|HAMAP-Rule:MF_00206}; GN Name=lipA {ECO:0000255|HAMAP-Rule:MF_00206}; GN OrderedLocusNames=PG_0504; OS Porphyromonas gingivalis (strain ATCC BAA-308 / W83). OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae; OC Porphyromonas. OX NCBI_TaxID=242619; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-308 / W83; RX PubMed=12949112; DOI=10.1128/jb.185.18.5591-5601.2003; RA Nelson K.E., Fleischmann R.D., DeBoy R.T., Paulsen I.T., Fouts D.E., RA Eisen J.A., Daugherty S.C., Dodson R.J., Durkin A.S., Gwinn M.L., RA Haft D.H., Kolonay J.F., Nelson W.C., Mason T.M., Tallon L., Gray J., RA Granger D., Tettelin H., Dong H., Galvin J.L., Duncan M.J., Dewhirst F.E., RA Fraser C.M.; RT "Complete genome sequence of the oral pathogenic bacterium Porphyromonas RT gingivalis strain W83."; RL J. Bacteriol. 185:5591-5601(2003). 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_00206}. 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_00206}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00206}; 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_00206}; 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_00206}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00206}. CC -!- SIMILARITY: Belongs to the radical SAM superfamily. Lipoyl synthase CC family. {ECO:0000255|HAMAP-Rule:MF_00206}. 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; AE015924; AAQ65698.1; -; Genomic_DNA. DR RefSeq; WP_010956048.1; NC_002950.2. DR AlphaFoldDB; Q7MWT4; -. DR SMR; Q7MWT4; -. DR STRING; 242619.PG_0504; -. DR EnsemblBacteria; AAQ65698; AAQ65698; PG_0504. DR KEGG; pgi:PG_0504; -. DR PATRIC; fig|242619.8.peg.463; -. DR eggNOG; COG0320; Bacteria. DR HOGENOM; CLU_033144_2_1_10; -. DR BioCyc; PGIN242619:G1G02-465-MONOMER; -. DR UniPathway; UPA00538; UER00593. DR Proteomes; UP000000588; Chromosome. DR GO; GO:0005737; C:cytoplasm; 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; 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; 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; Cytoplasm; Iron; Iron-sulfur; Metal-binding; Reference proteome; KW S-adenosyl-L-methionine; Transferase. FT CHAIN 1..282 FT /note="Lipoyl synthase" FT /id="PRO_0000102335" FT DOMAIN 49..264 FT /note="Radical SAM core" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266" FT BINDING 37 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00206" FT BINDING 42 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00206" FT BINDING 48 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00206" FT BINDING 63 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_00206" FT BINDING 67 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_00206" FT BINDING 70 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_00206" FT BINDING 275 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00206" SQ SEQUENCE 282 AA; 31269 MW; 234D8EFDC11A8626 CRC64; MAQHVKKPEW LKIRLGGNEK FTETKSIVEG HCLHTICTSG KCPNMGECWS RGTATFMIGG DICTRACRFC NTLTGRPKPL NEAEPTHVAL SIKLMGLNHA VVTSVDRDDL PDYGAAHWVK TIQEIRRINS GVTLEVLIPD FKGRMDLVDM IIEASPDVIS HNLETVRRLT PSVRSVATYD TSLAVLRHIA QSGKMPAKTG MMLGLGETEE EILELMDDAL AAGVSVITIG QYLQPSRKNL PVVEYITPEQ FEHLRLVGIE KGFRTIESAP LVRSSYHAER HL //