InterPro domain: IPR005801

This domain superfamily is characteristic of ADC synthases, including:

• Anthranilate synthase aminodeoxyisochorismate synthase/lyase subunit, TrpE, which catalyses the formation of anthranilate (o-aminobenzoate) and pyruvic acid from chorismate and glutamine [ 1 , 2 ].
• P-aminobenzoate synthase component I (Aminodeoxychorismate synthase), which catalyses the two-step biosynthesis of 4-amino-4-deoxychorismate (ADC), a precursor of p-aminobenzoate and folate in microorganisms [ 3 ].
• Menaquinone-specific isochorismate synthase MenF, which catalyses the conversion of chorismate to isochorismate [ 4 ].
• Salicylate synthetase Irp9, which is involved in the biosynthesis of the siderophore yersiniabactin in Yersinia enterocolitica [ 5 ].
• Salicylate synthase MbtI (Mycobactin synthetase protein I), which is involved in salicylate production [ 6 ].

1. Structure of the cooperative allosteric anthranilate synthase from Salmonella typhimurium. Nat. Struct. Biol. 8, 243-7
2. The structures of anthranilate synthase of Serratia marcescens crystallized in the presence of (i) its substrates, chorismate and glutamine, and a product, glutamate, and (ii) its end-product inhibitor, L-tryptophan. Proc. Natl. Acad. Sci. U.S.A. 98, 6021-6
3. Structure of Escherichia coli aminodeoxychorismate synthase: architectural conservation and diversity in chorismate-utilizing enzymes. Biochemistry 41, 2198-208
4. Lysine 190 is the catalytic base in MenF, the menaquinone-specific isochorismate synthase from Escherichia coli: implications for an enzyme family. Biochemistry 46, 946-53
5. Crystal structures of Yersinia enterocolitica salicylate synthase and its complex with the reaction products salicylate and pyruvate. J. Mol. Biol. 357, 524-34
6. The structure of MbtI from Mycobacterium tuberculosis, the first enzyme in the biosynthesis of the siderophore mycobactin, reveals it to be a salicylate synthase. J. Bacteriol. 188, 6081-91