Gene Ontology annotation through association of InterPro records with GO terms
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
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
A lipA (yutB) mutant, encoding lipoic acid synthase, provides insight into the interplay between branched-chain and unsaturated fatty acid biosynthesis in Bacillus subtilis.
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Identified lipA (yutB) as encoding lipoyl synthase in B. subtilis
"the lipA (yutB) gene, which encodes lipoyl synthase (LipA), the enzyme that catalyzes the final step in the de novo biosynthesis of this cofactor"
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Disruption of lipA causes lipoate auxotrophy and growth defects in minimal medium
"Interrupting lipoate-dependent reactions strongly inhibits growth in minimal medium"
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lipA mutants show impaired branched-chain fatty acid biosynthesis
"impairing the generation of branched-chain fatty acids"
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lipA mutants accumulate straight-chain saturated fatty acids
"leading to accumulation of copious amounts of straight-chain saturated fatty acids in B. subtilis membranes"
Lipoic acid attachment to proteins: stimulating new developments
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Comprehensive 2024 review of lipoate biosynthesis and attachment mechanisms
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Details the radical SAM mechanism with auxiliary [4Fe-4S] cluster as sulfur donor
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Describes the B. subtilis pathway architecture (LipM/LipL/LplJ/GcvH)
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Explains Fe-S carrier protein roles in auxiliary cluster regeneration
Lipoic acid synthesis: a new family of octanoyltransferases generally annotated as lipoate protein ligases
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Identified LipM as the B. subtilis octanoyltransferase (distinct from E. coli LipB)
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LipM transfers octanoyl from ACP to GcvH
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Established the pathway order in B. subtilis de novo lipoate biosynthesis
Deep research on lipA function