|
|
||
|
|
|
|
|
UniProt functional annotation for Q5SLQ3 | ||
|
|
|
|
|
|
||
| UniProt code: Q5SLQ3. |
|
||
| Organism: | |
Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8). |
| Taxonomy: | |
Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus. |
|
||
|
||
| 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. {ECO:0000255|HAMAP-Rule:MF_00013}. |
|
||
| Catalytic activity: | |
Reaction=L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)- octanoyl-L-lysyl-[protein]; Xref=Rhea:RHEA:17665, Rhea:RHEA- COMP:9636, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9752, Rhea:RHEA- COMP:9928, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:64479, ChEBI:CHEBI:78463, ChEBI:CHEBI:78809; EC=2.3.1.181; Evidence={ECO:0000255|HAMAP-Rule:MF_00013}; |
| Pathway: | |
Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier- protein]: step 1/2. {ECO:0000255|HAMAP-Rule:MF_00013}. |
| Subcellular location: | |
Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00013}. |
| 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. {ECO:0000255|HAMAP-Rule:MF_00013}. |
| Similarity: | |
Belongs to the LipB family. {ECO:0000255|HAMAP- Rule:MF_00013}. |
Annotations taken from UniProtKB at the EBI.