Correction for Han et al., “Identification and Predictions Regarding the Biosynthesis Pathway of Polyene Macrolides Produced by Streptomyces roseoflavus Men-myco-93-63”

AUTHOR CORRECTION

Volume 87, no. 10, e03157-20, 2021, https://doi.org/10.1128/AEM.03157-20. Page 7: Figure 4 should appear as shown below, and the legend should include the sentence “The conserved motifs classified as type A and type B in the KR domain are marked with black circles” as indicated.

FIG 4.

Alignment of active-site sequences of AT, DH, and KR domains from RM PKSs. Only the regions containing the proposed active sites are shown. The active-site residues are marked with asterisks. The residue numbers shown in the first row of the AT alignment correspond to the positions in the E. coli FAS acyltransferase (FabD) crystal structure (PDB entry 1MLA). Arg117, which is conserved in all malonate- and methylmalonate-specific AT domains (AT1 to AT17), is the nonpolar amino acid Phe in AT0, which is specific for monocarboxylic substrates. The presence of Gln93 and Ser200 in AT1 and AT17 indicates that their substrate is methylmalonate, whereas Ile93 and Phe200 in AT2 to AT5 and AT7 to AT16 indicate that their substrate is malonate. In AT6, Gln93 indicates that its substrate is methylmalonate, whereas Pro200 indicates that its substrate is malonate; however, considering that position 200 is more selective in terms of amino acid occurrence than position 93, the substrate should be malonate, which also corresponds to the real chemical structure. The unique Ala93 and Ala200 residues in AT0 were not predicted from the key residue comparison. The conserved motifs classified as type A and type B in the KR domain are marked with black circles.