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Database: UniProt
Entry: A0A136JR56_9BACT
LinkDB: A0A136JR56_9BACT
Original site: A0A136JR56_9BACT 
ID   A0A136JR56_9BACT        Unreviewed;       301 AA.
AC   A0A136JR56;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 39.
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   ECO:0000313|EMBL:KXJ99593.1};
GN   ORFNames=UZ03_NOB001002991 {ECO:0000313|EMBL:KXJ99593.1};
OS   Nitrospira sp. OLB3.
OC   Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC   Nitrospira.
OX   NCBI_TaxID=1617410 {ECO:0000313|EMBL:KXJ99593.1, ECO:0000313|Proteomes:UP000070691};
RN   [1] {ECO:0000313|EMBL:KXJ99593.1, ECO:0000313|Proteomes:UP000070691}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OLB3 {ECO:0000313|EMBL:KXJ99593.1};
RA   Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT   "Improved understanding of the partial-nitritation anammox process through
RT   23 genomes representing the majority of the microbial community.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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:ARBA00001264, 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:KXJ99593.1}.
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DR   EMBL; JZQY01000062; KXJ99593.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A136JR56; -.
DR   STRING; 1617410.UZ03_NOB001002991; -.
DR   PATRIC; fig|1617410.3.peg.3062; -.
DR   UniPathway; UPA00538; UER00593.
DR   Proteomes; UP000070691; 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};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW   Rule:MF_00206};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00206, ECO:0000313|EMBL:KXJ99593.1}.
FT   DOMAIN          66..280
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
FT   BINDING         54
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         59
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         65
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         80
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         84
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         87
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         291
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   301 AA;  33678 MW;  BCC4B9EC35807FB2 CRC64;
     MSFIPLSTLR PADEAAGATN ARRLPPWFKV RLQTGPDYHD IRKTMDRLNL HTICEEARCP
     NVWECWNART ATFLILGDIC TRRCHYCSVA TGRPHAVDHD EPLRVAEAVQ ALNLRHAVIT
     SVNRDELADG GASVFAETLR QIRRLIPSCT IEVLIPDFEG NEAALATVAA EKPDILNHNI
     ETVRRLFPSI RPQGKYQRSI ELLGRAKQMG MTTKSGLIVG MGESTDEARE VMRDLRAVDC
     DIMTIGQYLQ PTKEHLPVAR FYHPDEFALL KEEGLAMGFR HVESGPLVRS SYHAEQQVAG
     G
//
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