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MJ0109 is an enzyme that is both an inositol monophosphatase and the 'missing' archaeal fructose-1,6-bisphosphatase

Nature Structural Biology volume 7, pages 1046–1050 (2000)Cite this article

Abstract

In sequenced genomes, protein coding regions with unassigned function constitute between 10 and 50% of all open reading frames. Often key enzymes cannot be identified using sequence homology searches. For example, despite the fact that methanogens have an apparently functional gluconeogenesis pathway, standard tools have been unable to identify a fructose-1,6-bisphosphatase (FBPase) gene in the sequenced Methanoccocus jannaschii genome. Using a combination of functional and structural tools, we have shown that the protein product of the M. jannaschii gene MJ0109, which had been tentatively annotated as an inositol monophosphatase (IMPase), has both IMPase and FBPase activities. Moreover, several gene products annotated as IMPases from different thermophilic organisms also possess FBPase activity. Thus, we have found the FBPase that was 'missing' in thermophiles and shown that it also functions as an IMPase.

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Figure 1: Stereo views of the M. jannaschii IMPase.
Figure 2: Structural sequence alignments of the metallo-phosphatase family.

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Acknowledgements

B.S. would like to acknowledge the W.M. Keck Center for Computational Biology for financial support. K.A.J. was supported by a Burroughs Wellcome Fund Hitchings-Elion fellowship. This work was also supported by the Department of Energy Biosciences Division.

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Authors and Affiliations

  1. Department of Biochemistry and Cell Biology, W.M. Keck Center for Computational Biology, Rice University, Houston, 77005, Texas, USA

    Boguslaw Stec & Kenneth A. Johnson

  2. Department of Chemistry, Merkert Chemistry Center, Boston College, Chestnut Hill, 02467, Massachussetts, USA

    Hongying Yang, Liangjing Chen & Mary F. Roberts

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  1. Boguslaw Stec
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  2. Hongying Yang
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Correspondence to Boguslaw Stec or Mary F. Roberts.

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Stec, B., Yang, H., Johnson, K. et al. MJ0109 is an enzyme that is both an inositol monophosphatase and the 'missing' archaeal fructose-1,6-bisphosphatase. Nat Struct Mol Biol 7, 1046–1050 (2000). https://doi.org/10.1038/80968

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