Part:BBa_K5226007
TD-glyA
Sequence and Features
- 10INCOMPATIBLE WITH RFC[10]Illegal PstI site found at 626
Illegal PstI site found at 754 - 12INCOMPATIBLE WITH RFC[12]Illegal NheI site found at 480
Illegal PstI site found at 626
Illegal PstI site found at 754 - 21COMPATIBLE WITH RFC[21]
- 23INCOMPATIBLE WITH RFC[23]Illegal PstI site found at 626
Illegal PstI site found at 754 - 25INCOMPATIBLE WITH RFC[25]Illegal PstI site found at 626
Illegal PstI site found at 754
Illegal AgeI site found at 985 - 1000COMPATIBLE WITH RFC[1000]
Introduction
One of the goals of iGEM24-SCUT-China-A is to use synthetic biology tools to obtain Halomonas TD strains that can metabolize formate. We chose to introduce the formate assimilation pathway to enable it to utilize formate, a difficult-to-recover product in CDE. For the first method, based on previous studies obtained from literature research, we selected the tetrahydrofolate (THF) cycle imported from Methylobacterium extorquens AM1 and strengthened the endogenous C2 and C3 modules of Halomonas TD.
Usage and Biology
TD-GlyA is Serine hydroxymethyltransferase .The protein sequence is from Halomonas sp. TD01 strain.This protein catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
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