Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Combined Automated Annotation using Multiple IEA Methods.
Alternative splicing directs dual localization of Candida albicans 6-phosphogluconate dehydrogenase to cytosol and peroxisomes.
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Gnd1 is one of the two NADPH-producing dehydrogenases of the oxidative PPP in C. albicans; the majority of the protein is cytosolic with a small peroxisome-associated fraction, and dual targeting is achieved by alternative splicing of an intron encoding an N-terminal PTS2.
"dual targeting of Gnd1 is directed by alternative splicing resulting in two Gnd1 isoforms, one without targeting signals localized to the cytosol and one with an N-terminal PTS2 targeted to peroxisomes"
Null mutants of Candida albicans for cell-wall-related genes form fragile biofilms that display an almost identical extracellular matrix proteome.
A response to iron involving carbon metabolism in the opportunistic fungal pathogen Candida albicans.
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Iron limitation in C. albicans causes metabolic remodeling, including induction of ZWF1 and GND1 and increased oxidative PPP NADPH production; a cell-free oxidative PPP assay with NADP+ as acceptor measures the combined Zwf1 plus Gnd1 activity, since Zwf1 supplies the 6-phosphogluconate substrate for Gnd1.
"Since ZWF1 catalysis provides the 6-phosphogluconate substrate for GND1 (see Fig. 6A), the NADPH formed reflects activity from both enzymes"
The Pentose Phosphate Pathway in Yeasts-More Than a Poor Cousin of Glycolysis.
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Review of the yeast PPP; notes that C. albicans Zwf1 and Gnd1 carry functional peroxisomal targeting signals with roughly 10% and 5% of the respective proteins in peroxisomes, proposed to detoxify ROS from fatty-acid degradation.
"In Candida albicans, functional peroxisomal signal sequences were detected in CaZwf1 and also in the 6-phosphogluconate dehydrogenase CaGnd1"
6-Phosphogluconate dehydrogenase and its crystal structures.
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Structural review of 6PGDH (EC 1.1.1.44); coenzyme specificity varies across the family (some bacterial enzymes are NAD+-specific or dual), and NADP+ specificity is conferred by the Asn-Arg-Thr turn that binds the 2'-phosphate, with Asp in place of Asn in NAD+-preferring enzymes.
"Some bacterial 6PGDHs are specific for NAD+, while others can use both NAD+ and NADP+"
Coenzyme-specificity motif check for C. albicans Gnd1 (A0A1D8PFS4)
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C. albicans Gnd1 carries the Gly-X-Ala-X-Met-Gly fingerprint (residues 13-18) and the Asn-Arg-Thr NADP+ 2'-phosphate-binding motif (residues 36-38), both coinciding with UniProt NADP(+) binding features, and lacks the Asp-Arg-Asp motif of NAD+-preferring 6PGDHs; the NADP+-specific term GO:0004616 is the correct cofactor-specific molecular function.
Deep research report on GND1/A0A1D8PFS4 (Falcon/Edison Scientific Literature)
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C. albicans Gnd1 (A0A1D8PFS4, orf19.12491) is the NADP+-dependent 6-phosphogluconate dehydrogenase (EC 1.1.1.44) of the oxidative PPP, generating NADPH and ribulose-5-phosphate.
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Subcellular fractionation of oleate-grown cells shows ~95% of Gnd1 activity in cytosol with ~5-10% in organellar/peroxisomal fractions; an alternatively spliced PTS2-containing transcript is ~1000-fold less abundant than the major cytosolic transcript and yields the peroxisomal isoform, whose import depends on Pex7.
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Iron limitation drives PPP/NADPH remodeling, with GND1 induced as part of compensatory carbon metabolism; the PPP is widely regarded as central to NADPH supply for glutathione/redox homeostasis and oxidative stress defence.