AC   MF_03123;
DC   Protein; auto
c?   <OC:Eukaryota> or <OG:Plastid>
TR   HAMAP; MF_00206; -; 1; level=0
XX
Names: Lipoyl_synth_euk
XX
case <OC:Metazoa>
ID   LIAS
else
ID   LIPA
end case
case <OG:Organellar chromatophore>
DE   RecName: Full=Lipoyl synthase, organellar chromatophore;
DE            EC=2.8.1.8;
DE   AltName: Full=Lipoate synthase;
DE            Short=Lip-syn;
DE            Short=LS;
DE   AltName: Full=Lipoic acid synthase;
else case <OC:Apicomplexa>
DE   RecName: Full=Lipoyl synthase, apicoplast;
DE            EC=2.8.1.8;
DE   AltName: Full=Lipoate synthase;
DE            Short=Lip-syn;
DE            Short=LS;
DE   AltName: Full=Lipoic acid synthase;
else
DE   RecName: Full=Lipoyl synthase, mitochondrial;
DE            EC=2.8.1.8;
DE   AltName: Full=Lipoate synthase;
DE            Short=Lip-syn;
DE            Short=LS;
DE   AltName: Full=Lipoic acid synthase;
end case
case <OC:Vertebrata>
GN   Name=LIAS;
else case <OC:Drosophilidae>
GN   Name=Las;
else case <OC:Apicomplexa>
GN   Name=lipA;
else case <OC:Saccharomyces>
GN   Name=LIP5;
end case
XX
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.
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   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
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   -!- PATHWAY: Protein modification; protein lipoylation via endogenous
CC       pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-
CC       protein]: step 2/2.
case <OG:Organellar chromatophore>
CC   -!- SUBCELLULAR LOCATION: Plastid, organellar chromatophore.
else case <OC:Apicomplexa>
CC   -!- SUBCELLULAR LOCATION: Plastid, apicoplast.
else
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
end case
case not <OC:Apicomplexa> and not <OG:Organellar chromatophore> and not <AnyFeature:TransitM>
CC   -!- MISCELLANEOUS: This protein may be expected to contain an N-terminal
CC       transit peptide but none has been predicted.
end case
CC   -!- SIMILARITY: Belongs to the radical SAM superfamily. Lipoyl synthase
CC       family.
XX
DR   Pfam; PF04055; Radical_SAM; 1; trigger=no
DR   NCBIfam; TIGR00510; lipA; 1; trigger=no
DR   PIRSF; PIRSF005963; Lipoyl_synth; 1; trigger=no
case <OC:Apicomplexa>
DR   General; Signal; -; 1; trigger=yes
else case not <OG:Organellar chromatophore>
DR   General; TransitM; -; 0-1; trigger=yes
end case
XX
KW   4Fe-4S
KW   Iron
KW   Iron-sulfur
KW   Metal-binding
case <OG:Organellar chromatophore>
KW   Organellar chromatophore
KW   Plastid
else case <OC:Apicomplexa>
KW   Apicoplast
KW   Plastid
KW   Signal
else
KW   Mitochondrion
end case
KW   S-adenosyl-L-methionine
KW   Transferase
XX
GO   GO:0016783; F:sulfurtransferase activity
GO   GO:0016992; F:lipoate synthase activity
GO   GO:0051539; F:4 iron, 4 sulfur cluster binding
GO   GO:0009107; P:lipoate biosynthetic process
GO   GO:0009249; P:protein lipoylation
case <OG:Organellar chromatophore>
GO   GO:0070111; C:organellar chromatophore
else case <OC:Apicomplexa>
GO   GO:0020011; C:apicoplast
else
GO   GO:0005739; C:mitochondrion
end case
XX
FT   From: LIPA_YEAST (P32875)
FT   BINDING         150
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT   Condition: C
FT   BINDING         155
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT   Condition: C
FT   BINDING         161
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT   Condition: C
FT   BINDING         181
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT   Condition: C
FT   BINDING         185
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT   Condition: C
FT   BINDING         188
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT   Condition: C
FT   BINDING         396
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT   Condition: S
XX
Size: 291-502;
Related: MF_03128!; MF_03129!;
Template: P32875; Q8IDQ0;
Scope:
 Eukaryota
 Plastid
Fusion:
 Nter: None
 Cter: None
Duplicate: in DROYA, PHATR, TRYCR
Plasmid: None
Comments: None
XX
# Revision 1.17 2023/09/14
//