Title

Orphan SeID proteins and selenium-dependent molybdenum hydroxylases

Authors

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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