Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Gene Ontology annotation based on curation of intracellular localizations of expressed fusion proteins in living cells
Electronic Gene Ontology annotations created by transferring manual GO annotations between related proteins based on shared sequence features
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Combined Automated Annotation using Multiple IEA Methods
Aging-associated enzyme human clock-1: substrate-mediated reduction of the diiron center for 5-demethoxyubiquinone hydroxylation.
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Purified human CLK-1/COQ7 is a 5-demethoxyubiquinone hydroxylase that uses a carboxylate-bridged diiron center; substrate (DMQ) binding mediates NADH reduction of the diiron center and initiates O2 activation for hydroxylation.
"GB1-hCLK-1 functions as a 5-demethoxyubiquinone-hydroxylase, utilizing its carboxylate-bridged diiron center."
Mitochondrial COQ9 is a lipid-binding protein that associates with COQ7 to enable coenzyme Q biosynthesis.
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COQ9 is a lipid-binding protein that specifically interacts with COQ7 through conserved residues around its lipid-binding site, and is proposed to present its bound lipid (DMQ) substrate to COQ7 to enable CoQ biosynthesis.
"COQ9 specifically interacts with COQ7 through a series of conserved residues."
A nuclear role for the respiratory enzyme CLK-1 in regulating mitochondrial stress responses and longevity.
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A distinct uncleaved pool of COQ7/CLK-1 localizes to the nucleus and chromatin and regulates ROS metabolism, the UPRmt, and longevity independently of its mitochondrial ubiquinone-biosynthetic function.
"COQ7 has a biologically relevant nuclear role that is independent of its characterised mitochondrial function in ubiquinone biosynthesis."
Mitochondrial Protein Interaction Mapping Identifies Regulators of Respiratory Chain Function.
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Systematic mitochondrial protein interaction mapping identified a dynamic human CoQ biosynthetic complex, placing COQ7 within the CoQ synthome at the inner mitochondrial membrane.
"we identified a dynamic human CoQ biosynthetic complex involving"
Pathogenicity of two COQ7 mutations and responses to 2,4-dihydroxybenzoate bypass treatment.
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Pathogenic COQ7 variants (V141E, L111P) reduce protein stability and ubiquinone levels; 2,4-dihydroxybenzoate can restore ubiquinone synthesis in cells lacking COQ7 activity, confirming COQ7's requirement in ubiquinone biosynthesis.
"mutations in the ubiquinone biosynthetic gene COQ7"
Biochemistry of Mitochondrial Coenzyme Q Biosynthesis.
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Review of mitochondrial CoQ biosynthesis and the CoQ biosynthetic complex, within which COQ7 catalyzes a hydroxylation step.
"questions framed by the recently discovered CoQ biosynthetic complex"
An Isoprene Lipid-Binding Protein Promotes Eukaryotic Coenzyme Q Biosynthesis.
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Structural/biochemical study of the COQ9 isoprene-lipid-binding protein and its interface with COQ7, supporting a lipid-presentation role in CoQ biosynthesis.
"COQ9 interaction and interface with COQ7 suggest a lipid presentation role"
Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context.
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High-confidence human mitochondrial proteome (MitoCoP) that includes COQ7 among mitochondrial proteins.
"defined a mitochondrial high-confidence proteome of >1,100 proteins (MitoCoP)"
In vitro construction of the COQ metabolon unveils the molecular determinants of coenzyme Q biosynthesis.
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In vitro reconstitution of the animal COQ metabolon shows COQ7 is an NADH-dependent, carboxylate-bridged-diiron hydroxylase performing the C6 step, with COQ9 enhancing its catalytic efficiency, within a COQ3/4/5/6/7/9 complex.
"COQ7 is an NADH-dependent hydroxylase that possesses a carboxylate-bridged diiron centre and converts 5 to 6"
UniProt entry Q99807 (COQ7_HUMAN)
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COQ7 is an NADPH-dependent 3-demethoxyubiquinone 3-hydroxylase that binds two iron ions per subunit and localizes as a peripheral protein to the matrix side of the mitochondrial inner membrane.
"Note=Binds 2 iron ions per subunit."
COQ7:COQ9 octamer hydroxylates DMQ10H2