Literature summary for 1.14.99.60 extracted from

Stenmark, P.; Gruenler, J.; Mattsson, J.; Sindelar, P.J.; Nordlund, P.; Berthold, D.A.
A new member of the family of di-iron carboxylate proteins. Coq7 (clk-1), a membrane-bound hydroxylase involved in ubiquinone biosynthesis (2001), J. Biol. Chem., 276, 33297-33300 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
homology moldeing based on the Escherichia coli bacterioferritin structure. In the structural model, 14 of the 15 completely conserved residues in Coq7 cluster in a region surrounding the active site	Pseudomonas aeruginosa

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
membrane	-	Pseudomonas aeruginosa	16020	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Iron	active site of the Coq7 model shows a typical di-iron center, with each Fe atom chelated by one histidine and one terminal carboxylate ligand	Pseudomonas aeruginosa

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas aeruginosa	Q9I5R6	-	-

Synonyms

Synonyms	Comment	Organism
2-nonaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase	-	Pseudomonas aeruginosa
COQ7	-	Pseudomonas aeruginosa

General Information

General Information	Comment	Organism
physiological function	the gene complements an Escherichia coli mutant that lacks 5-demethoxyubiquinone hydroxylase UbiF	Pseudomonas aeruginosa

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Release 2023.1 (January 2023)