Orphan SeID proteins and selenium-dependent molybdenum hydroxylases

    Authors

    D. H. Haft;W. T. Self

    Comments

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    Abbreviated Journal Title

    Biol. Direct

    Keywords

    XANTHINE DEHYDROGENASE; CLOSTRIDIUM-PURINOLYTICUM; PURINE HYDROXYLASE; GENOME PROPERTIES; ESCHERICHIA-COLI; COFACTOR; SULFUR; ENZYME; EVOLUTION; INSERTION; Biology

    Abstract

    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.

    Journal Title

    Biology Direct

    Volume

    3

    Publication Date

    1-1-2008

    Document Type

    Article

    Language

    English

    First Page

    6

    WOS Identifier

    WOS:000254434500001

    ISSN

    1745-6150

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