Part:BBa_K3841010
Particulate methane monooxygenase alpha subunit (PmoB)
Methane monooxygenases catalyses the initial oxygenation of methane to methanol in methanotrophic bacteria [1].
The bacterium Methylococcus capsulatus has two forms of methane monooxygenase, a soluble (sMMO) and a membrane-bound (particulate) type (pMMO). The particulate type is a cupper-dependent [2] nonamer composed of three alpha:beta:gamma heterotrimeric protomers assembled into a cylindrical structure; the beta and gamma subunits comprise the bulk of the membrane-spanning regions and the soluble regions are derived primarily from alpha subunits which form two antiparallel beta-barrel-like structures each [3].
BBa_K3841010 is the alpha subunit of pMMO and has been codon-optimized for the methylotropich yeast, Komagataella phaffii.
Sequence and Features
- 10INCOMPATIBLE WITH RFC[10]Illegal XbaI site found at 619
Illegal XbaI site found at 1153 - 12COMPATIBLE WITH RFC[12]
- 21INCOMPATIBLE WITH RFC[21]Illegal BglII site found at 334
- 23INCOMPATIBLE WITH RFC[23]Illegal XbaI site found at 619
Illegal XbaI site found at 1153 - 25INCOMPATIBLE WITH RFC[25]Illegal XbaI site found at 619
Illegal XbaI site found at 1153 - 1000COMPATIBLE WITH RFC[1000]
References
[1] Hanson, Richard S., and Thomas E. Hanson. “Methanotrophic Bacteria.†Microbiological Reviews, vol. 60, no. 2, American Society for Microbiology, 1996, pp. 439–71, doi:10.1128/mmbr.60.2.439-471.1996.
[2] Basu, Piku, et al. “The Membrane-Associated Form of Methane Mono-Oxygenase from Methylococcus Capsulatus (Bath) Is a Copper/Iron Protein.†Biochemical Journal, vol. 369, no. 2, PORTLAND PRESS LTD, 2003, pp. 417–27, doi:10.1042/BJ20020823.
[3] Lieberman, Raquel L., and Amy C. Rosenzweig. “Crystal Structure of a Membrane-Bound Metalloenzyme That Catalyses the Biological Oxidation of Methane.†Nature, vol. 434, no. 7030, NATURE PUBLISHING GROUP, 2005, pp. 177–82, doi:10.1038/nature03311.
[4] Cramer, Patrick. “AlphaFold2 And the Future of Structural Biology.†Nature Structural and Molecular Biology, vol. 28, no. 9, Nature Research, 2021, pp. 704–05, doi:10.1038/s41594-021-00650-1.
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