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UniProt functional annotation for Q5SKN9 | ||
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| UniProt code: Q5SKN9. |
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| Organism: | |
Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8). |
| Taxonomy: | |
Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus. |
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| Function: | |
Catalyzes the esterification of a number of long chain fatty acids with CoA, resulting in the formation of long-chain fatty acyl- CoA. Myristate (C14) is the most efficiently processed fatty acid, followed by palmitate (C16). Also catalyzes the esterification of stearate (C18) and laurate (C12), but at lower efficiency. Does not catalyze the esterification of the unsaturated fatty acids mysteroleic and palmitoleic acids in vitro. {ECO:0000269|PubMed:15145952}. |
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| Catalytic activity: | |
Reaction=a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl- CoA + AMP + diphosphate; Xref=Rhea:RHEA:15421, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57560, ChEBI:CHEBI:83139, ChEBI:CHEBI:456215; EC=6.2.1.3; Evidence={ECO:0000269|PubMed:15145952}; |
| Cofactor: | |
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:15145952}; |
| Pathway: | |
Lipid metabolism; fatty acid metabolism. |
| Subunit: | |
Forms a domain swapped homodimer. {ECO:0000269|PubMed:15145952}. |
| Miscellaneous: | |
Upon ATP binding, the fatty acid-binding tunnel gated by the aromatic residue Trp-234 opens to the ATP-binding site. The acylation reaction proceeds in two steps, via the formation of a fatty acyl-AMP intermediate, and is proposed to follow a unidirectional Bi Uni Uni Bi ping-pong mechanism. |
| Similarity: | |
Belongs to the ATP-dependent AMP-binding enzyme family. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.