Q7JQW6 · LIAS_DROME
- ProteinLipoyl synthase, mitochondrial
- GeneLas
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids377 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
Function
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.
Miscellaneous
This protein may be expected to contain an N-terminal transit peptide but none has been predicted.
Catalytic activity
- [[Fe-S] cluster scaffold protein carrying a second [4Fe-4S]2+ cluster] + 4 H+ + N6-octanoyl-L-lysyl-[protein] + 2 oxidized [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine + [[Fe-S] cluster scaffold protein] + 4 Fe3+ + 2 hydrogen sulfide + 2 L-methionine + N6-[(R)-dihydrolipoyl]-L-lysyl-[protein] + 2 reduced [2Fe-2S]-[ferredoxin]
RHEA-COMP:14568 CHEBI:33722 Position: ACHEBI:33722 Position: B+ 4 CHEBI:15378 + RHEA-COMP:9928 + 2 RHEA-COMP:10000 + 2 CHEBI:59789 = 2 CHEBI:17319 + RHEA-COMP:14569 CHEBI:33722 Position: A+ 4 CHEBI:29034 + 2 CHEBI:29919 + 2 CHEBI:57844 + RHEA-COMP:10475 + 2 RHEA-COMP:10001
Cofactor
Note: Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Pathway
Protein modification; protein lipoylation via endogenous pathway; protein N6-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 2/2.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 103 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 108 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 114 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 134 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 138 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 141 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 349 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: S |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrion | |
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | lipoate synthase activity | |
Molecular Function | metal ion binding | |
Biological Process | lipoate biosynthetic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameLipoyl synthase, mitochondrial
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionQ7JQW6
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000398219 | 1-377 | Lipoyl synthase, mitochondrial | |||
Sequence: MLRALKTHAEAPIVVATRAASTNAEKLEEIRERLAKGPNFHDFVQNPDNTRNEWEQYDGKLRREKGEEQRLRLPPWLKTTIPVGKNYAKIKAQMRELKLSTVCEEARCPNIGECWGGGEHGTQTATIMLMGDTCTRGCRFCSVKTARKPPPLDVNEPVNTATAIASWGLDYIVLTSVDRDDLPDGGSEHIAETVREIKARNSNIFVECLVPDFRGNLECVKTIANSGLDVYAHNIETVEKLTPYVRDRRAHYRQTLQVLTEAKRFNPNLITKSSIMLGLGETDEEIENTLKDLREAGVDCVTLGQYMQPTNKHLKVIEYVTPEKFKHWEERGNELGFLYTASGPLVRSSYKAGEFFITSILENRKKRQNDTEVPKKQ |
Proteomic databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 119-338 | Radical SAM core | ||||
Sequence: EHGTQTATIMLMGDTCTRGCRFCSVKTARKPPPLDVNEPVNTATAIASWGLDYIVLTSVDRDDLPDGGSEHIAETVREIKARNSNIFVECLVPDFRGNLECVKTIANSGLDVYAHNIETVEKLTPYVRDRRAHYRQTLQVLTEAKRFNPNLITKSSIMLGLGETDEEIENTLKDLREAGVDCVTLGQYMQPTNKHLKVIEYVTPEKFKHWEERGNELGFL |
Sequence similarities
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length377
- Mass (Da)42,734
- Last updated2010-10-05 v2
- ChecksumE702B1AB55DD5DC3
Sequence caution
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE014296 EMBL· GenBank· DDBJ | AAF51596.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY058557 EMBL· GenBank· DDBJ | AAL13786.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BT003750 EMBL· GenBank· DDBJ | AAO41414.1 EMBL· GenBank· DDBJ | mRNA | Different initiation |