C5PIN8 · LIPA_COCP7
- ProteinLipoyl synthase, mitochondrial
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids419 (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 | 136 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 141 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 147 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 167 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 171 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 174 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 382 | [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 |
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 > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Onygenales > Onygenaceae > Coccidioides
Accessions
- Primary accessionC5PIN8
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for transit peptide, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-26 | Mitochondrion | ||||
Sequence: MAVCAGRLKCFGNPAVSLRTAASRAY | ||||||
Chain | PRO_0000398263 | 27-419 | Lipoyl synthase, mitochondrial | |||
Sequence: ATTTSPDPAIPSSSSASSSSALPKRPQTSFRDKLNAGPSFSDFLSGGNRDDARILDPNEAYALKTALVGPKGKKKEITRLPSWLKTSIPDSNNYKRIKNDLRGLGLHTVCEEARCPNISECWGGSSKSAATATIMLMGDTCTRACRFCSVKTSKTPPPLDPHEPENTAEALSRWGLGYVVLTTVDRDDLIDGGARHFAETVIRIKQKAPNILVECLTGDYAGDLEMVALMAKSGLDVYAHNVETVEALTPHVRDRRANFQTSLRVLKAAKAAVPSLITKTSMMLGLGETEEQMWDALRQLRAANVDVVTFGQYMRPTKRHMPVHEYVRPDVFELWKDRALEMGFLYCASGPLVRSSYKAGEAFIENVLKKRRAESTGPESTNVPNVTPDAIVR |
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 28-52 | Polar residues | ||||
Sequence: TTTSPDPAIPSSSSASSSSALPKRP | ||||||
Region | 28-61 | Disordered | ||||
Sequence: TTTSPDPAIPSSSSASSSSALPKRPQTSFRDKLN | ||||||
Domain | 150-371 | Radical SAM core | ||||
Sequence: GSSKSAATATIMLMGDTCTRACRFCSVKTSKTPPPLDPHEPENTAEALSRWGLGYVVLTTVDRDDLIDGGARHFAETVIRIKQKAPNILVECLTGDYAGDLEMVALMAKSGLDVYAHNVETVEALTPHVRDRRANFQTSLRVLKAAKAAVPSLITKTSMMLGLGETEEQMWDALRQLRAANVDVVTFGQYMRPTKRHMPVHEYVRPDVFELWKDRALEMGFL | ||||||
Region | 399-419 | Disordered | ||||
Sequence: AESTGPESTNVPNVTPDAIVR |
Sequence similarities
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length419
- Mass (Da)45,766
- Last updated2009-09-01 v1
- ChecksumE41CAE42605B6DEF
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 28-52 | Polar residues | ||||
Sequence: TTTSPDPAIPSSSSASSSSALPKRP |
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
ACFW01000049 EMBL· GenBank· DDBJ | EER24391.1 EMBL· GenBank· DDBJ | Genomic DNA |