HAMAP rule MF_00206
General rule information
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Accession | MF_00206 |
Dates | 1-JUN-2001 (Created)
2-SEP-2024 (Last updated, Version 61) |
Name | Lipoyl_synth |
Scope(s) |
Bacteria Archaea |
Template(s) | P60716 (LIPA_ECOLI); O32129 (LIPA_BACSU); P9WK91 (LIPA_MYCTU); Q8DLC2 (LIPA2_THEVB); Q97U63 (LIPA_SACS2); [ Recover all ] |
Triggered by |
case c? <OC:Bacteria> or <OC:Archaea>
HAMAP; MF_00206 (Get profile general information and statistics) end case
|
Propagated annotation
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Identifier, protein and gene names
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Identifier | LIPA |
Protein name | RecName: Full=Lipoyl synthase; EC=2.8.1.8; AltName: Full=Lip-syn; Short=LS; AltName: Full=Lipoate synthase; AltName: Full=Lipoic acid synthase; AltName: Full=Sulfur insertion protein LipA; |
Gene name | Name=lipA; |
Comments
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FUNCTION | Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. |
CATALYTIC ACTIVITY | Reaction=[[Fe-S] cluster scaffold protein carrying a second [4Fe- 4S](2+) cluster] + N(6)-octanoyl-L-lysyl-[protein] + 2 oxidized [2Fe- 2S]-[ferredoxin] + 2 S-adenosyl-L-methionine + 4 H(+) = [[Fe-S] cluster scaffold protein] + N(6)-[(R)-dihydrolipoyl]-L-lysyl- [protein] + 4 Fe(3+) + 2 hydrogen sulfide + 2 5'-deoxyadenosine + 2 L-methionine + 2 reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:16585, Rhea:RHEA-COMP:9928, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, Rhea:RHEA-COMP:10475, Rhea:RHEA-COMP:14568, Rhea:RHEA-COMP:14569, ChEBI:CHEBI:15378, ChEBI:CHEBI:17319, ChEBI:CHEBI:29034, ChEBI:CHEBI:29919, ChEBI:CHEBI:33722, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789, ChEBI:CHEBI:78809, ChEBI:CHEBI:83100; EC=2.8.1.8; |
COFACTOR | Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Note=Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.; |
case <OC:Bacillales> | |
PATHWAY | Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier- protein]. |
else | |
PATHWAY | Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier- protein]: step 2/2. |
end case | |
SUBCELLULAR LOCATION | Cytoplasm. |
SIMILARITY | Belongs to the radical SAM superfamily. Lipoyl synthase family. |
Keywords
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Gene Ontology
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GO:0016783; Molecular function:sulfurtransferase activity |
GO:0016992; Molecular function:lipoate synthase activity |
GO:0051539; Molecular function:4 iron, 4 sulfur cluster binding |
GO:0009107; Biological process:lipoate biosynthetic process |
GO:0009249; Biological process:protein lipoylation |
GO:0005737; Cellular component:cytoplasm |
Cross-references
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Features
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From: LIPA_MYCTU (P9WK91) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
BINDING | 55 | 55 | /ligand="[4Fe-4S] cluster" /ligand_id="ChEBI:CHEBI:49883" /ligand_label="1" |
C | ||||||||
BINDING | 60 | 60 | /ligand="[4Fe-4S] cluster" /ligand_id="ChEBI:CHEBI:49883" /ligand_label="1" |
C | ||||||||
BINDING | 66 | 66 | /ligand="[4Fe-4S] cluster" /ligand_id="ChEBI:CHEBI:49883" /ligand_label="1" |
C | ||||||||
BINDING | 81 | 81 | /ligand="[4Fe-4S] cluster" /ligand_id="ChEBI:CHEBI:49883" /ligand_label="2" /ligand_note="4Fe-4S-S-AdoMet" |
C | ||||||||
BINDING | 85 | 85 | /ligand="[4Fe-4S] cluster" /ligand_id="ChEBI:CHEBI:49883" /ligand_label="2" /ligand_note="4Fe-4S-S-AdoMet" |
C | ||||||||
BINDING | 88 | 88 | /ligand="[4Fe-4S] cluster" /ligand_id="ChEBI:CHEBI:49883" /ligand_label="2" /ligand_note="4Fe-4S-S-AdoMet" |
C | ||||||||
BINDING | 292 | 292 | /ligand="[4Fe-4S] cluster" /ligand_id="ChEBI:CHEBI:49883" /ligand_label="1" |
S |
Additional information
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Size range | 276-373 amino acids |
Related rules |
MF_03128 MF_03129 |
Fusion | Nter: None Cter: None |
Comments | E.coli requires only 2 proteins for the endogenous pathway of protein lipoylation, LipB (MF_00013) and LipA (MF_00206), whereas B.subtilis (and probably many Bacillota) requires 3 enzymes: LipM (MF_02118), LipL (MF_02119) and LipA (MF_00206). |