A0A9C7B299 · A0A9C7B299_9THEO
- ProteinOctanoyltransferase
- GenelipB
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids225 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Miscellaneous
In the reaction, the free carboxyl group of octanoic acid is attached via an amide linkage to the epsilon-amino group of a specific lysine residue of lipoyl domains of lipoate-dependent enzymes.
Catalytic activity
- octanoyl-[ACP] + L-lysyl-[protein] = N6-octanoyl-L-lysyl-[protein] + holo-[ACP] + H+
Pathway
Protein modification; protein lipoylation via endogenous pathway; protein N6-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2.
Features
Showing features for binding site, site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 75-82 | substrate | ||||
Sequence: RGGDVTYH | ||||||
Site | 139 | Lowers pKa of active site Cys | ||||
Sequence: K | ||||||
Binding site | 142-144 | substrate | ||||
Sequence: AIG | ||||||
Binding site | 155-157 | substrate | ||||
Sequence: GFA | ||||||
Active site | 173 | Acyl-thioester intermediate | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | lipoyl(octanoyl) transferase activity | |
Biological Process | protein lipoylation |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameOctanoyltransferase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Clostridia > Thermoanaerobacterales > Thermoanaerobacteraceae > Gelria
Accessions
- Primary accessionA0A9C7B299
Proteomes
Subcellular Location
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 30-212 | BPL/LPL catalytic | ||||
Sequence: GEEPDTLLLVEHDPVITLGRTAKREHLLFKEAALAEQGISVFAVERGGDVTYHGPGQLVGYPILNLNRHGRDLHLLLRNYEEVLIRALADFGVAGRRFPPYTGVWVGEEKVAAIGVAVEHWVSFHGFAFNVDPNLDHFGLIVPCGISQYGVTSLARLLGRPVELFEVIPHVVHHFADVFGLTL |
Sequence similarities
Belongs to the LipB family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length225
- Mass (Da)24,715
- Last updated2023-05-03 v1
- Checksum0A093C9266808A32
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AP024619 EMBL· GenBank· DDBJ | BCV23466.1 EMBL· GenBank· DDBJ | Genomic DNA |