Discovery Notes The DOMON domains are involved in heme and sugar recognition.pdf

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Discovery Notes The DOMON domains are involved in heme and sugar recognition.pdf

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Discovery Notes The DOMON domains are involved in heme and sugar recognition

Published by Oxford University Press 2007. The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions@ 1 Discovery Notes The DOMON domains are involved in heme and sugar recognition Lakshminarayan M. Iyer, Vivek Anantharaman and L. Aravind* NCBI, NLM, NIH, Bethesda, MD 20894, USA. *Address for correspondence: aravind@: Telephone (301) 594-2445; Fax: (301) 480-9241. Associate Editor: Prof. John Quackenbush ABSTRACT We expand the functionally uncharacterized DOMON domain super- family to identify several novel families, including the first prokaryotic representatives. Using several computational tools we show that it is involved in ligand-binding--either as heme- or sugar-binding do- mains. We present evidence that the DOMON domain along with the DM13 domain comprises a novel electron-transfer system potentially involved in oxidative modification of animal cell-surface proteins. Other novel versions might function as sugar sensors of histidine kinases of bacterial two component systems. 1 INTRODUCTION The DOMON (dopamine β-monooxygenase N-terminal) domain also called DoH was originally identified in several secreted, or cell surface proteins from plants and animals (Aravind, 2001; Pon- ting, 2001). It usually occurs fused to other domains such as other Cu-ascorbate-dependent mono-oxygenases associated with cate- cholamine metabolism (the eponymous enzyme in which it was found), cytoc