Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Combined Automated Annotation using Multiple IEA Methods
Characterisation of D-arabinono-1,4-lactone oxidase from Candida albicans ATCC 10231.
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The C. albicans enzyme was purified from a mitochondrial fraction and characterized as an FAD-linked D-arabinono-1,4-lactone oxidase with alternate L-galactono-, L-gulono-, and L-xylono-1,4-lactone activities.
"D-Arabinono-1,4-lactone oxidase, which catalyses the final step in the biosynthesis of D-erythroascorbic acid, was purified 639-fold from the mitochondrial fraction of C. albicans"
Deficiency of D-erythroascorbic acid attenuates hyphal growth and virulence of Candida albicans.
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Cloning and disruption of ALO1 showed that the gene encodes the enzyme required for D-arabinono-1,4-lactone oxidase activity and cellular D-erythroascorbate production.
"In the alo1/alo1 null mutants, the activity of D-arabinono-1,4-lactone oxidase was completely lost and D-erythroascorbic acid could not be detected"
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C. albicans ALO1 was predicted to encode an integral membrane protein with a covalent-FAD binding site and a single transmembrane segment.
"predicted that the enzyme should be an integral membrane protein with a transmembrane segment"
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Loss and overexpression of ALO1 altered oxidative-stress resistance, and alo1/alo1 mutants had conditional hyphal growth and virulence defects.
"The alo1/alo1 null mutants of C. albicans showed increased sensitivity towards oxidative stress. Overexpression of ALO1 made the cells more resistant to the same stress"
Analysis of Candida albicans plasma membrane proteome.
D-Erythroascorbic acid activates cyanide-resistant respiration in Candida albicans.
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Later C. albicans work connected ALO1-derived D-erythroascorbate to alternative oxidase expression and cyanide-resistant respiration.
"the presence of cyanide in culture medium remarkably retarded the growth of alo1/alo1 mutant of Candida albicans"
A protein interaction map of the myosin Myo2 reveals a role for Alo1 in mitochondrial inheritance in yeast.
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Budding-yeast Alo1 was identified as a Myo2 cargo-binding-domain interactor and implicated in mitochondrial inheritance under oxidative stress.
"using the cargo-binding domain of Myo2, the major organelle transporter in yeast, as bait"
UniProtKB entry O93852 for C. albicans ALO1
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UniProt classifies ALO1 as a PTHR43762:SF1 D-arabinono-1,4-lactone oxidase with EC 1.1.3.37, EC 1.1.3.8, EC 1.3.3.12, ALO_C, and FAD-binding PCMH domains.
"DR PANTHER; PTHR43762:SF1; D-ARABINONO-1,4-LACTONE OXIDASE; 1."
PANTHER PTHR43762 PAINT annotations