E9GMP1 · E9GMP1_DAPPU
- ProteinLipoyl synthase, mitochondrial
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids385 (go to sequence)
- Protein existenceInferred from homology
- 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.
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 | 119 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 124 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 130 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 150 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 154 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 157 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 365 | [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
- Organism
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Crustacea > Branchiopoda > Diplostraca > Cladocera > Anomopoda > Daphniidae > Daphnia
Accessions
- Primary accessionE9GMP1
Proteomes
Subcellular Location
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 133-354 | Radical SAM core | ||||
Sequence: GGPDATATATIMLMGDTCTRGCRFCSVKTSKAPPPLDPNEPVNTAIAIAAWGLDYVVLTSVDRDDLPDQGSNHLSQTVSELKQRKPELLVECLTPDFRGDRDCVERIVLSGLDVFAHNIETVEELTWLVRDPRAKYQQSMDVLRYAKQVRPDVVTKSSIMLGLGETDDQVRKTLEDLRAANVDCVTLGQYMQPTKRHLKVTEYVTPEKFAQWESVGKELGFL |
Sequence similarities
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length385
- Mass (Da)42,905
- Last updated2011-04-05 v1
- ChecksumF1C2CC657A667CCD
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
GL732553 EMBL· GenBank· DDBJ | EFX79130.1 EMBL· GenBank· DDBJ | Genomic DNA |