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Missing function
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Suggested candidates
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Criteria for selection
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Comments
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Phosphomevalonate kinase (archaea)
| Family of proteins related to uridylate and acetyl glutamate kinases 3258052_Pyrho Y044_METJA 2621082_Metth 2648231_Arcfu 5105458_Aerpe | Linked to mevalonate kinase in all archaea, similarly to the linkage observed between mevalonate kinase and phosphomevalonate kinase in Borellia and cocci; isolated phylogenetic position. | A more likely candidate. |
| Family of orthologs within galactokinase superfamily 3258263_Pyrho 3024949_Metja 2621655_Metth 2648904_Arcfu 5105835_Aerpe | Sequence similarity and isolated phylogenetic position within the superfamily. |
| Family of orthologs within galactokinase superfamily 2128859_Metja 2621895_Metth 2850101_Arcfu 5105835_Aerpe | Sequence similarity and isolated phylogenetic position within the superfamily. | No orthologs in two of three Pyrococcus species. |
| Family of orthologs within galactokinase superfamily YE27_METJA 3256616_Pyrho 3257645_Pyrho Y830_METTH YK89_ARCFU 5106179_Aerpe 5105197_Aerpe | Sequence similarity and isolated phylogenetic position within the superfamily. |
P. horikoshii andAeropyrum have a set of paralogs, generally not seen for mevalonate pathway enzymes. |
| Family of orthologs within nucleoside monophosphate kinase superfamily 3257422_Pyrho 2128835_Metja 2621499_Metth 2649179_Arcfu | Sequence similarity and isolated phylogenetic position within the superfamily. | Closer to CMP/UMP kinases and may be required for the nucleotide kinase function (judged from the numbers of paralogs with such specificity in bacterial genomes). |
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Diphosphomevalonate decarboxylase (archaea)
| Homologs (probably paralogs) of SAM decarboxylase from E. coli 5103467_Aerpe 2648951_Arcfu 2495908_Metja 3258436_Pyrho | Elimination of other decarboxylases in archaea, either as misannotations, or because they are predicted to have a clearly unrelated biological function. | Related genes in some bacteria, but an internal deletion in archaeal genes suggests that the substrate in archaea may be different. No homolog in M. thermoautotrophicum.
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Isopentenyl pyrophosphate delta-isomerase (archaea, Borrelia,cocci) | FMN-dependent dehydrogenases, including glycolate oxidase (NCBI COG1304) 2688617_Borbu 5105455_Aerpe 2648236_Arcfu 1591547_Metja 2621084_Metth 3257619_Pyrho | In Borrelia,found within an “operon” with all other enzymes of mevalonate pathway; neighbors with relevant functions in some archaea. Consistent phyletic pattern, although paralogs are widespread. | Oxidoreductase activity predicted by sequence similarity. In plants, some oxidoreductases are known to have a desaturase activity, which, in this case, could be exploited to isomerize the double bonds in IPP. |
| Uncharacterized family (NCBI COG1916) 2688316_Borbu 2650316_Arcfu 2129184_Metja 2622291_Metth 3257569_Pyrho | Exceptionally consistent phyletic pattern in microorganisms (Borrelia, Enterococcus, only one additional bacterium, Treponema, and archaea except forAeropyrum). | In Enterococcus, plasmid-borne copy is involved in response to peptide pheromone, which controls conjugation. Orthologs in plants, C. elegans and humans. |
| Uncharacterized family (NCBI COG0327) 2688374_Borbu 2648773_Arcfu Y927_METJA 726074_Metth 3257033_Pyrho | Phyletic pattern (archaea+ Borrelia), although orthologs are found in many bacteria. | Presence of several invariant histidines suggests that this may be a metalloenzyme. |
| Uncharacterized family (NCBI COG0061) 2688218_Borbu 5104774_Aerpe 2650718_Arcfu 2621965_Metth 2826350_Metja 3257490_Pyrho | Phyletic pattern (archaea+ Borrelia), although orthologs are found in many bacteria. | Glycine-rich (phosphate-binding?) motif shared with diacylglycerol kinases and 6- phosphofructokinases. |
| Undecaprenyl diphosphate synthase (NCBI COG0020) UPPS_BORBU 5105068_Aerpe UPPS_ARCFU UPPS_METJA UPPS_PYRHO | Phyletic pattern (archaea+ Bacteria except for Mycoplasmae), note that the DXPS-pathway bacteria may need such activity, too (see text). | Multiple functions in the same pathway would have to be assumed; no biochemical evidence. |