Protein Variants | Comment | Organism |
---|---|---|
additional information | expression of the N-terminal adenylation and thiolation domain | Amycolatopsis mediterranei |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + 3-amino-5-hydroxybenzoate + a holo-[acyl-carrier protein] | Amycolatopsis mediterranei | - |
3-amino-5-hydroxybenzoyl-[acyl-carrier protein] + AMP + diphosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Amycolatopsis mediterranei | O54666 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + 3,5-diaminobenzoate + a holo-[acyl-carrier protein] | - |
Amycolatopsis mediterranei | 3,5-diaminobenzoyl-[acyl-carrier protein] + AMP + diphosphate | - |
? | |
ATP + 3-amino-5-hydroxybenzoate + a holo-[acyl-carrier protein] | - |
Amycolatopsis mediterranei | 3-amino-5-hydroxybenzoyl-[acyl-carrier protein] + AMP + diphosphate | - |
? | |
ATP + 3-aminobenzoate + a holo-[acyl-carrier protein] | - |
Amycolatopsis mediterranei | 3-aminobenzoyl-[acyl-carrier protein] + AMP + diphosphate | - |
? | |
ATP + 3-hydroxybenzoate + a holo-[acyl-carrier protein] | - |
Amycolatopsis mediterranei | 3-hydroxybenzoyl-[acyl-carrier protein] + AMP + diphosphate | - |
? | |
additional information | less than 5% of the activity with 3-amino-5-hydroxybenzoate: 3,5-dihydroxybenzoate, 3-chlorobenzoate, 3-bromobenzoate, benzoate | Amycolatopsis mediterranei | ? | - |
- |
Synonyms | Comment | Organism |
---|---|---|
rifA | - |
Amycolatopsis mediterranei |
General Information | Comment | Organism |
---|---|---|
physiological function | rifamycin synthetase is primed with a 3-amino-5-hydroxybenzoate starter unit by a loading module that contains domains homologous to the adenylation and thiolation domains of nonribosomal peptide synthetases. The thiolation domain requires covalent attachment of the 4'-phosphopantetheine moiety of CoA to a conserved serine to be active. The catalytic models for the mechanism of the adenylation and thiolation didomain involve activation of 3-amino-5-hydroxybenzoate as the aryl-adenylate by the adenylation domain, followed by eventual formation of a covalent aryl thioester enzyme intermediate from attack of either aryl-CoA or the aryl-adenylate by the thiol nucleophile of the phosphopantetheine cofactor of the thiolation domain | Amycolatopsis mediterranei |