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
Automatic Gene Ontology annotation based on Rhea mapping
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
YeastPathways to GO-CAM conversion
Yeast mitochondrial dehydrogenases are associated in a supramolecular complex.
Yeast AMID homologue Ndi1p displays respiration-restricted apoptotic activity and is involved in chronological aging.
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Overexpression of NDI1, but not NDE1, causes ROS-associated apoptosis-like death that is suppressed by increased respiration and by interrupting downstream ETC components; deletion lowers ROS and extends chronological lifespan.
"internal NADH dehydrogenase (NDI1), but not external NADH dehydrogenase (NDE1),"
Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics.
Isolation and inactivation of the nuclear gene encoding the rotenone-insensitive internal NADH: ubiquinone oxidoreductase of mitochondria from Saccharomyces cerevisiae.
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Cloning and disruption of NDI1; mitochondria from null mutants show Ndi1 oxidizes intramitochondrial NADH; null mutants are impaired on lactate, pyruvate and acetate.
"that this NADH dehydrogenase catalyzes the oxidation of NADH generated inside"
The structure of the yeast NADH dehydrogenase (Ndi1) reveals overlapping binding sites for water- and lipid-soluble substrates.
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Crystal structures of Ndi1 alone and with NAD+ or UQ2 show a peripheral, monotopic, matrix-directed homodimer with overlapping NAD+ and quinone sites.
"protein forming an intimate dimer, in which packing of the monomeric units"
Structural insight into the type-II mitochondrial NADH dehydrogenases.
Quantitative variations of the mitochondrial proteome and phosphoproteome during fermentative and respiratory growth in Saccharomyces cerevisiae.
Purification and characterization of a rotenone-insensitive NADH:Q6 oxidoreductase from mitochondria of Saccharomyces cerevisiae.
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Purification of a 53 kDa single-subunit, FAD-containing, rotenone-insensitive NADH:Q6 oxidoreductase. The authors provisionally assigned it as the external enzyme; their 1991 gene disruption paper showed it is the internal enzyme Ndi1.
"The enzyme contains FAD, non-covalently linked, as the sole"
Molecular remedy of complex I defects: rotenone-insensitive internal NADH-quinone oxidoreductase of Saccharomyces cerevisiae mitochondria restores the NADH oxidase activity of complex I-deficient mammalian cells.
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Ndi1 expressed in complex I-deficient hamster cells localizes to the matrix side of the inner membrane and restores rotenone-insensitive NADH oxidation and respiratory growth.
"catalyzed electron transfer from NADH in the matrix to ubiquinone-10 in the inner mitochondrial membranes"
Lack of complex I activity in human cells carrying a mutation in MtDNA-encoded ND4 subunit is corrected by the Saccharomyces cerevisiae NADH-quinone oxidoreductase (NDI1) gene.
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Ndi1 restores NADH-dependent respiration in ND4-mutant human cells with a P:O ratio about two-thirds of wild type, consistent with no proton pumping by Ndi1.
"wild-type 143B.TK(-) cells, as expected from the lack of proton pumping activity"
The Saccharomyces cerevisiae NDE1 and NDE2 genes encode separate mitochondrial NADH dehydrogenases catalyzing the oxidation of cytosolic NADH.
Stoichiometry and compartmentation of NADH metabolism in Saccharomyces cerevisiae.
Comparative analysis of mitochondrial proteomes across the tree of life.
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Comparative proteomics reconstructs NDH2 in ancestral mitochondria; retained in yeast, lost in humans; NDH2 recovered as a candidate pathogen drug target.
"mitochondria inherited NDH2, amino acid and cofactor biosynthetic pathways"
SGD gene description for NDI1 (yeast)