Literature summary for 6.2.1.74 extracted from

Admiraal, S.; Khosla, C.; Walsh, C.
A Switch for the transfer of substrate between nonribosomal peptide and polyketide modules of the rifamycin synthetase assembly line (2003), J. Am. Chem. Soc., 125, 13664-13665.

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Organism

Organism	UniProt	Comment	Textmining
Amycolatopsis mediterranei	O54666	-	-

Synonyms

Synonyms	Comment	Organism
rifA	-	Amycolatopsis mediterranei

General Information

General Information	Comment	Organism
metabolism	the loading module (LM) of Rif synthetase activates 3-amino-5-hydroxybenzoate (AHB) as AHB-AMP and links it to the phosphopantetheine arm of its thiolation domain (T1). AHB is then transferred across the non-ribosomal peptide synthase interface to the active-site cysteine of the ketosynthase domain of PKS module 1 (M1), and this second intermediate reacts with a methylmalonyl moiety to form an aryl ketide covalently bound to the M1 thiolation domain (T2). Occupancy of the T2 domain of LM-M1 by a methylmalonyl moiety triggers intermodular transfer of benzoate from the T1 domain to the KS domain, and this transthiolation event is fast relative to the initial loading of benzoate onto the T1 domain	Amycolatopsis mediterranei

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Release 2026.1 (March 2026)