Composite

Part:BBa_K1529151

Designed by: Shoko Suzuki   Group: iGEM14_Tokyo_Tech   (2014-09-15)


PT7_obcB

1


Contribution From CAU_China 2022

Group: CAU_China, 2022 https://2022.igem.org/Team:CAU_China

Author: Liu Muhua

Summary: Added information about how this gene catalyze the formation of oxalic acid.

Biology

CAU_China 2022 plan to use the CDS sequence of _obcB_ in this composite part and the expression product of _obcB_ is one of the main enzyme in in the oxalate secretion circuit[1]. It can act together with ObcA to catalyze oxaloacetic acid (OAA) and citric acid to form oxalic acid (OA). When there is only ObcB, it cannot form oxalic acid[2].

CAU-obcAB-pic.jpeg

Fig.1 Effects of obcA and obcB, the shade of purple reflects the concentration of oxalic acid[1].


When producing oxalic acid, obcB turns C6-CoA adduct into CoA, acetoacetate,and oxalic acid


CAU-obcAB-work.jpeg

Fig.2 Mechanism of obcA and obcB[2].

Considering the importance of _obcA_ and _obcB_ occur togrther in the biosynthesis of oxalic acid, the CDS of them are in close proximity to each other, even encoded on a single polycistronic message. The implication of this for our project is that we can make these two genes share the same promoter[2].


CAU-obcAB-gene.jpeg

Fig.3 Distribution of obcA and obcB[1].

Sequence and Features


Assembly Compatibility:
  • 10
    INCOMPATIBLE WITH RFC[10]
    Illegal PstI site found at 669
  • 12
    INCOMPATIBLE WITH RFC[12]
    Illegal PstI site found at 669
    Illegal NotI site found at 582
    Illegal NotI site found at 687
  • 21
    INCOMPATIBLE WITH RFC[21]
    Illegal BamHI site found at 650
  • 23
    INCOMPATIBLE WITH RFC[23]
    Illegal PstI site found at 669
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal PstI site found at 669
    Illegal NgoMIV site found at 460
    Illegal NgoMIV site found at 501
    Illegal NgoMIV site found at 625
  • 1000
    COMPATIBLE WITH RFC[1000]



References

[1]Nakata, Paul A, and Cixin He. “Oxalic acid biosynthesis is encoded by an operon in Burkholderia glumae.” FEMS microbiology letters vol. 304,2 (2010): 177-82. doi:10.1111/j.1574-6968.2010.01895.x

[2]Oh, Juntaek et al. “Structural basis for bacterial quorum sensing-mediated oxalogenesis.” The Journal of biological chemistry vol. 289,16 (2014): 11465-11475. doi:10.1074/jbc.M113.543462


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