Entry
Name
3-amino-5-hydroxybenzoate---[acyl-carrier protein] ligase;
rifA (gene name);
mitE (gene name)
Class
Ligases;
Forming carbon-sulfur bonds;
Acid-thiol ligases
BRITE hierarchy
Sysname
3-amino-5-hydroxybenzoate:[acyl carrier protein] ligase (AMP-forming)
Reaction(IUBMB)
ATP + 3-amino-5-hydroxybenzoate + a holo-[acyl-carrier protein] = 3-amino-5-hydroxybenzoyl-[acyl-carrier protein] + AMP + diphosphate [RN:
R12789 ]
Reaction(KEGG)
Substrate
ATP [CPD:
C00002 ];
3-amino-5-hydroxybenzoate [CPD:
C12107 ];
holo-[acyl-carrier protein] [CPD:
C00229 ]
Product
3-amino-5-hydroxybenzoyl-[acyl-carrier protein] [CPD:
C22389 ];
AMP [CPD:
C00020 ];
diphosphate [CPD:
C00013 ]
Comment
During the biosynthesis of most ansamycin antibiotics such as rifamycins, streptovaricins, naphthomycins, and chaxamycins, the activity is catalysed by the loading domain of the respective polyketide synthase (PKS), which transfers the substrate to the acyl-carrier protein domain of the first extension module of the PKS. During the biosynthesis of the mitomycins the reaction is catalysed by the MitE protein, which transfers the substrate to a dedicated acyl-carrier protein (MmcB).
History
EC 6.2.1.74 created 2021
Pathway
Orthology
K15670 rifamycin polyketide synthase modules 1, 2 and 3
Genes
SSOI : I1A49_05870 I1A49_10320
» show all
Taxonomy
Reference
Authors
Admiraal SJ, Walsh CT, Khosla C.
Title
The loading module of rifamycin synthetase is an adenylation-thiolation didomain with substrate tolerance for substituted benzoates.
Journal
Sequence
Reference
Authors
Admiraal SJ, Khosla C, Walsh CT.
Title
The loading and initial elongation modules of rifamycin synthetase collaborate to produce mixed aryl ketide products.
Journal
Sequence
Reference
Authors
Admiraal SJ, Khosla C, Walsh CT.
Title
A Switch for the transfer of substrate between nonribosomal peptide and polyketide modules of the rifamycin synthetase assembly line.
Journal
Reference
Authors
Chamberland S, Gruschow S, Sherman DH, Williams RM.
Title
Synthesis of potential early-stage intermediates in the biosynthesis of FR900482 and mitomycin C.
Journal
Other DBs
ExplorEnz - The Enzyme Database: 6.2.1.74
ExPASy - ENZYME nomenclature database: 6.2.1.74
LinkDB
All DBs