ID B4D740_9BACT Unreviewed; 295 AA.
AC B4D740;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=Lipoyl synthase {ECO:0000256|HAMAP-Rule:MF_00206};
DE EC=2.8.1.8 {ECO:0000256|HAMAP-Rule:MF_00206};
DE AltName: Full=Lip-syn {ECO:0000256|HAMAP-Rule:MF_00206};
DE Short=LS {ECO:0000256|HAMAP-Rule:MF_00206};
DE AltName: Full=Lipoate synthase {ECO:0000256|HAMAP-Rule:MF_00206};
DE AltName: Full=Lipoic acid synthase {ECO:0000256|HAMAP-Rule:MF_00206};
DE AltName: Full=Sulfur insertion protein LipA {ECO:0000256|HAMAP-Rule:MF_00206};
GN Name=lipA {ECO:0000256|HAMAP-Rule:MF_00206};
GN ORFNames=CfE428DRAFT_4730 {ECO:0000313|EMBL:EDY17691.1};
OS Chthoniobacter flavus Ellin428.
OC Bacteria; Verrucomicrobiota; Spartobacteria; Chthoniobacterales;
OC Chthoniobacteraceae; Chthoniobacter.
OX NCBI_TaxID=497964 {ECO:0000313|EMBL:EDY17691.1, ECO:0000313|Proteomes:UP000005824};
RN [1] {ECO:0000313|EMBL:EDY17691.1, ECO:0000313|Proteomes:UP000005824}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ellin428 {ECO:0000313|EMBL:EDY17691.1,
RC ECO:0000313|Proteomes:UP000005824};
RX PubMed=21460085; DOI=10.1128/JB.00295-11;
RA Kant R., van Passel M.W., Palva A., Lucas S., Lapidus A.,
RA Glavina Del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S.,
RA Larimer F.W., Land M.L., Hauser L., Sangwan P., de Vos W.M., Janssen P.H.,
RA Smidt H.;
RT "Genome sequence of Chthoniobacter flavus Ellin428, an aerobic
RT heterotrophic soil bacterium.";
RL J. Bacteriol. 193:2902-2903(2011).
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:0000256|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:0000256|ARBA:ARBA00043709, ECO:0000256|HAMAP-
CC Rule:MF_00206};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00206}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00206}.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. Lipoyl synthase
CC family. {ECO:0000256|HAMAP-Rule:MF_00206}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EDY17691.1}.
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DR EMBL; ABVL01000017; EDY17691.1; -; Genomic_DNA.
DR RefSeq; WP_006982051.1; NZ_ABVL01000017.1.
DR AlphaFoldDB; B4D740; -.
DR STRING; 497964.CfE428DRAFT_4730; -.
DR GeneID; 78186990; -.
DR eggNOG; COG0320; Bacteria.
DR InParanoid; B4D740; -.
DR UniPathway; UPA00538; UER00593.
DR Proteomes; UP000005824; Unassembled WGS sequence.
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; 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 {ECO:0000256|HAMAP-Rule:MF_00206};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00206};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00206};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW Rule:MF_00206};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00206}; Reference proteome {ECO:0000313|Proteomes:UP000005824};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_00206}; Transferase {ECO:0000256|HAMAP-Rule:MF_00206}.
FT DOMAIN 57..273
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT BINDING 45
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00206"
FT BINDING 50
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00206"
FT BINDING 56
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00206"
FT BINDING 71
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:0000256|HAMAP-Rule:MF_00206"
FT BINDING 75
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:0000256|HAMAP-Rule:MF_00206"
FT BINDING 78
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:0000256|HAMAP-Rule:MF_00206"
FT BINDING 284
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00206"
SQ SEQUENCE 295 AA; 33200 MW; 857A57B830A321BF CRC64;
MSCSKIDPAL HQAKKPDWIK VRLPTNPVFF STKALISDLR LHTVCEEAQC PNRWECWSAG
TATFMIAGER CTRACGFCAV TTAKPFALEV DEPERVAEAV KRMKLKHVVV TAVARDDLKD
GGAEHFARTI EAIRAAQPDM AIEVLTPDFH AKEECLRMVA DAKPHIFNHN VETVERLTPL
VRSRAKYRVS LQVLRRMKDI APEIVTKSGI MLGLGETEPE IFQTMDDLRE AGVQVLTMGQ
YLRPTPQHLP VVEYVHPDTF KLYKEIAEKK GFEHVASGPL VRSSYHAADF NPLKR
//
