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. 2017 Apr 14;292(22):9117–9135. doi: 10.1074/jbc.M117.778977

Figure 2.

Figure 2.

Comparison of the primary sequences of ADS, AQS, and other type III PKSs. The secondary structures of ADS are delineated as follows: α-helices (rectangles) and β-strands (arrows). The Cys, His, and Asn catalytic triad and the residues lining the active-site cavity of CHS are colored red and blue, respectively. Tyr-215 in AQS and the corresponding residues in other type III PKSs are highlighted in green. GenBankTM accession numbers are as follows: MsCHS, L02902; CmQNS, AB823730; ClDCS, AB535216; ClCURS1, AB495007; OsCUS, BAC79571; RpBAS, AF326911; RdORS, LC133082. The sequence of HsPKS3 has not yet been released from GenBankTM.