Orphan SelD proteins and selenium-dependent molybdenum hydroxylases.
Bacterial and Archaeal cells use selenium structurally in selenouridine-modified tRNAs, in proteins translated with selenocysteine, and in the selenium-dependent molybdenum hydroxylases (SDMH). The first two uses both require the selenophosphate synthetase gene, selD. Examining over 500 complete prokaryotic genomes finds selD in exactly two species lacking both the selenocysteine and selenouridine systems, Enterococcus faecalis and Haloarcula marismortui. Surrounding these orphan selD genes, forming bidirectional best hits between species, and detectable by Partial Phylogenetic Profiling vs. selD, are several candidate molybdenum hydroxylase subunits and accessory proteins. We propose that certain accessory proteins, and orphan selD itself, are markers through which new selenium-dependent molybdenum hydroxylases can be found.
Haft
Daniel H
DH
Department of Bioinformatics, J, Craig Venter Institute, Rockville, MD 20850, USA. haft@jcvi.org
Self
William T
WT
D001105:Archaea / Q000201:enzymology* / Q000235:genetics; D001419:Bacteria / Q000201:enzymology* / Q000235:genetics; D013293:Enterococcus faecalis / Q000201:enzymology / Q000235:genetics; D019614:Haloarcula marismortui / Q000201:enzymology / Q000235:genetics; D006899:Mixed Function Oxygenases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism / Q000502:physiology; D008982:Molybdenum / Q000737:chemistry / Q000378:metabolism*; D012643:Selenium / Q000502:physiology*; D017279:Selenocysteine / Q000235:genetics / Q000502:physiology
D017279:Selenocysteine; D008982:Molybdenum; D006899:Mixed Function Oxygenases; D012643:Selenium