Cloned (Comment) | Organism |
---|---|
- |
Escherichia coli |
Crystallization (Comment) | Organism |
---|---|
crystal structure of a truncated form of UbiI. Residues of the flavin binding pocket of UbiI are important for activity | Escherichia coli |
Protein Variants | Comment | Organism |
---|---|---|
G301A/N303A | mutation of residues form the bottom of the isoalloxazine binding pocket, strongly impairs UbiI activity | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P25535 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-(all-trans-polyprenyl)phenol + NADPH + H+ + O2 | - |
Escherichia coli | 3-(all-trans-polyprenyl)benzene-1,2-diol + NADP+ + H2O | - |
? |
Synonyms | Comment | Organism |
---|---|---|
2-octaprenylphenol hydroxylase | - |
Escherichia coli |
ubiI | - |
Escherichia coli |
visC | - |
Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | - |
Escherichia coli |
General Information | Comment | Organism |
---|---|---|
physiological function | a strain deficient in ubiI has a low level of coenzyme Q and accumulates 3-octaprenyl-4-hydroxyphenol. UbiI is only implicated in aerobic Q biosynthesis. C5-hydroxylation reaction is totally abolished in a strain lacking both UbiF and UbiI. UbiI partially complements the C5-hydroxylation defect of Saccharomyces cerevisiae cells lacking COQ6 | Escherichia coli |