Part:BBa_K5051001
PPTase
PPTase from Aureobasidium pullulans EXF-150 is critical for post-translational modifications (PTMs) of PKS1. The conserved mechanism is that the PPTase transfers a 4'-phosphopantetheinyl (4'-PP) group from Coenzyme A (CoA) to a conserved serine in the acyl carrier (ACP) domains of polyketide synthases (PKS) (Sunbul et al., 2009).
This modification converts PKS1 from the inactive apo-form to the active holo-form, enabling them to participate in downstream reactions. The 4′-PP group acts as a flexible arm that facilitates the transport of acyl or aminoacyl intermediates between the active sites. Without PPTase, PKS1 would be hindered from maximum enzymatic activity (Venkitasubramanian et al., 2006; Xue et al., 2018).
Fig 1. Structure predicted by ESMFold, coloured by pLDDT (Lin et al., 2023)
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12INCOMPATIBLE WITH RFC[12]Illegal NheI site found at 924
- 21INCOMPATIBLE WITH RFC[21]Illegal BglII site found at 981
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
None |