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.[1] 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.
UbiD | |||||||||
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Identifiers | |||||||||
Symbol | UbiD | ||||||||
Pfam | PF01977 | ||||||||
InterPro | IPR002830 | ||||||||
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Function
editUbiquinone 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.[2] 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.[3] In essence, the protein domain, UbiD, is vital to creating ubiquinone, an essential electron carrier in the creation on energy.
References
edit- ^ Zhang H, Javor GT (November 2000). "Identification of the ubiD gene on the Escherichia coli chromosome". J. Bacteriol. 182 (21): 6243–6. doi:10.1128/jb.182.21.6243-6246.2000. PMC 94763. PMID 11029449.
- ^ Liu J, Liu JH (2006). "Ubiquinone (coenzyme Q) biosynthesis in Chlamydophila pneumoniae AR39: identification of the ubiD gene". Acta Biochim Biophys Sin (Shanghai). 38 (10): 725–30. doi:10.1111/j.1745-7270.2006.00214.x. PMID 17033719.
- ^ Gulmezian M, Hyman KR, Marbois BN, Clarke CF, Javor GT (2007). "The role of UbiX in Escherichia coli coenzyme Q biosynthesis". Arch Biochem Biophys. 467 (2): 144–53. doi:10.1016/j.abb.2007.08.009. PMC 2475804. PMID 17889824.