Gene Ontology annotation through association of InterPro records with GO terms

Electronic Gene Ontology annotations created by transferring manual GO annotations between related proteins based on shared sequence features

Combined Automated Annotation using Multiple IEA Methods

Iron-sulfur center of biotin synthase and lipoate synthase.

Escherichia coli LipA is a lipoyl synthase: in vitro biosynthesis of lipoylated pyruvate dehydrogenase complex from octanoyl-acyl carrier protein.

Lipoyl synthase requires two equivalents of S-adenosyl-L-methionine to synthesize one equivalent of lipoic acid.

Escherichia coli lipoyl synthase binds two distinct [4Fe-4S] clusters per polypeptide.

Protein abundance profiling of the Escherichia coli cytosol.

Protein-protein interactions in assembly of lipoic acid on the 2-oxoacid dehydrogenases of aerobic metabolism.

Destruction and reformation of an iron-sulfur cluster during catalysis by lipoyl synthase.

Lipoic acid metabolism in Escherichia coli: sequencing and functional characterization of the lipA and lipB genes.

Assembly of the covalent linkage between lipoic acid and its cognate enzymes.

Mechanistic investigations of lipoic acid biosynthesis in Escherichia coli: both sulfur atoms in lipoic acid are contributed by the same lipoyl synthase polypeptide.

A nucleosidase required for in vivo function of the S-adenosyl-L-methionine radical enzyme, biotin synthase.

UniProtKB reviewed entry for lipA (P60716)