Gene Ontology annotation through association of InterPro records with GO terms
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniPathway vocabulary mapping
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Biochemical characterization of human 3-methylglutaconyl-CoA hydratase and its role in leucine metabolism.
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Purified recombinant AUH is the major human 3-methylglutaconyl-CoA hydratase, with (E)-3-methylglutaconyl-CoA and (E)-glutaconyl-CoA as its best substrates, acting in the leucine degradation pathway.
"giving strong evidence that the AUH gene encodes for the major human 3-MG-CoA hydratase in leucine degradation."
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The MGCA1-associated A240V missense variant retains only ~9% of wild-type 3-MG-CoA hydratase activity.
"leading to the amino acid exchange A240V, produces an enzyme with only 9% of the wild-type 3-MG-CoA hydratase activity."
The Human Knockout Gene CLYBL Connects Itaconate to Vitamin B(12).
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Itaconate can be converted to itaconyl-CoA and citramalyl-CoA via a reversible hydration reaction catalyzed by methylglutaconyl-CoA hydratase (AUH), placing AUH in the C5-dicarboxylate / itaconate detoxification pathway.
"reaction catalyzed by methylglutaconyl-CoA hydratase (AUH)"
Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context.
AUH, a gene encoding an AU-specific RNA binding protein with intrinsic enoyl-CoA hydratase activity.
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AUH was identified by affinity purification on an AUUUA matrix as a protein that binds specifically to AU-rich 3'UTR transcripts of lymphokines and proto-oncogenes (IL-3, GM-CSF, c-fos, c-myc).
"In vitro, the recombinant protein bound specifically to AU-rich transcripts, including those for interleukin 3, granulocyte/macrophage colony-stimulating factor, c-fos, and c-myc."
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AUH has intrinsic (low) enoyl-CoA hydratase activity, and the hydratase and AU-binding functions reside on distinct domains within a single polypeptide.
"suggesting that hydratase and AU-binding functions are located on distinct domains within a single polypeptide."
beta-methylglutaconyl-CoA + H2O <=> beta-hydroxy-beta-methylglutaryl-CoA
AUH mutants don't synthesize 3-hydroxy-methylglutaryl-CoA