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UbiD protein domain
In molecular biology this protein domain, refers to UbiD, which is found in prokaryotes, archaea and fungi, with two members in ''Archaeoglobus fulgidus''. They are related to UbiD, a 3-octaprenyl-4-hydroxybenzoate carboxy-lyase from ''Escherichia coli'' that is involved in ubiquinone biosynthesis. The member from ''Helicobacter pylori'' has a C-terminal extension of just over 100 residues that is shared, in part, by the ''Aquifex aeolicus'' homologue.
==Function==
Ubiquinone is an essential electron carrier in prokaryotes. In ''Escherichia coli'', the Ubiquinone biosynthesis pathway involves at least nine reactions whereby 3-octaprenyl4-hydroxybenzoate
decarboxylase (UbiD) is an enzyme on the pathway which catalyses the conversion of the substrate 3-octaprenyl-4-hydroxybenzoate to the product, 2-octaprenyl phenol. 〔 〕''E. coli'' ubiD- mutants have defects in Q8 biosynthesis, accumulate 4-hydroxy-3-octaprenylbenzoicacid (HP8B), and lack decarboxylase activity ''in vitro''.However, ''E. coli'' ubiD- mutants retained the ability to produce about 20–25% of the normal levels of Q 4-hydroxy-3-octaprenylbenzoic acid 〔 〕 In essence, the protein domain, UbiD, is vital to creating ubiquinone, an essential electron carrier in the creation on energy.
抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』
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