Protein Name:
NADPH-dependent 3-demethoxyubiquinone 3-hydroxylase, mitochondrial
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UniprotKB/SwissProt ID: P97478 (P97478)
Gene Name:
Coq7
Organism: Mus musculus (Mouse)
Function: Catalyzes the hydroxylation of the 5-methoxy-2-methyl-3-(all-trans-polyprenyl)benzoquinone at the C6 position and participates in the biosynthesis of ubiquinone. Catalyzes the reaction through a substrate-mediated reduction pathway, whereby NADH shuttles electrons to 5-methoxy-2-methyl-3-(all-trans-decaprenyl)benzoquinone, which then transfers the electrons to the two Fe(3+) centers. The binding of 5-methoxy-2-methyl-3-(all-trans-polyprenyl)benzoquinone (DMQn) mediates reduction of the diiron center by nicotinamide adenine dinucleotide (NADH) and initiates oxygen activation for subsequent DMQ hydroxylation. The physiological substrates are 5-methoxy-2-methyl-3-(all-trans-nonaprenyl)benzoquinone (DMQ(9)) and 5-methoxy-2-methyl-3-(all-trans-decaprenyl)benzoquinone (DMQ(10)), however in vitro the enzyme does not have any specificity concerning the length of the polyprenyl tail, and accepts tails of various lengths with similar efficiency (By similarity). Also has a structural role in the COQ enzyme complex, stabilizing other COQ polypeptides (By similarity). Involved in lifespan determination in a ubiquinone-independent manner (PubMed:19478076). Plays a role in modulating mitochondrial stress responses, acting in the nucleus, perhaps via regulating gene expression, independent of its characterized mitochondrial function in ubiquinone biosynthesis (By similarity)
Other Modifications: View all modification sites in dbPTM
Protein Subcellular Localization: Mitochondrion inner membrane
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Graphical Visualization of S-nitrosylation Sites:
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The S-nitrosylation sites of P97478
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| No. |
Position |
S-nitrosylated Peptide |
Secondary Structure of S-nitrosylated Peptide |
Solvent Accessibility of nitrosylated Site |
PubMed ID |
| 1 |
137 |
ALLGKEGAMA C TVAVEESIAN |
CCHHHHHHHH H HHCCCCCCCC |
1.7% |
21278135
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