Difference between revisions of "Part:BBa K1529151"
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| − | <p style="text-align: center;"><b>Fig.3 | + | <p style="text-align: center;"><b>Fig.3 Distribution of <i>obcA</i> and <i>obcB</i><sup>[1]</sup>.</b></p > |
<span class='h3bb'>Sequence and Features</span> | <span class='h3bb'>Sequence and Features</span> | ||
Revision as of 17:24, 30 September 2022
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.
Usage
CAU_China 2022 used the CDS sequence in their oxalate secretion pathway and the expression product of obcB is one of the main enzyme in this pathway. It can act together with ObcA to catalyze oxaloacetic acid (OAA) and citric acid to form oxalic acid (OA)[1]. When there is only ObcB, it cannot form oxalic acid in our project.
Fig.1 Effects of obcA and obcB, the shade of purple reflects the concentration of oxalic acid[1].
Biology
When producing oxalic acid, obcB turns C6-CoA adduct into CoA, acetoacetate,and oxalic acid
Fig.2 Mechanism of obcA and obcB[2].
Considered the importance of obcA and obcB occur togrther in the biosynthesis of oxalic acid, are in close proximity to each other, and are encoded in the same transcriptional direction, 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.
Fig.3 Distribution of obcA and obcB[1].
Sequence and Features
- 10INCOMPATIBLE WITH RFC[10]Illegal PstI site found at 669
- 12INCOMPATIBLE WITH RFC[12]Illegal PstI site found at 669
Illegal NotI site found at 582
Illegal NotI site found at 687 - 21INCOMPATIBLE WITH RFC[21]Illegal BamHI site found at 650
- 23INCOMPATIBLE WITH RFC[23]Illegal PstI site found at 669
- 25INCOMPATIBLE 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 - 1000COMPATIBLE 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