| Category | Identifier / finding | Evidence details | Source URL / year | Key citations |
|---|---|---|---|---|
| User-specified target identity | **UniProt:** A0A1D8PFS4; **gene:** GND1; **aliases:** orf19.12491, CAALFM_C113860CA; **organism:** *Candida albicans* SC5314 / ATCC MYA-2876 | User-provided record describes a **6-phosphogluconate dehydrogenase, decarboxylating** family protein with EC **1.1.1.44** and 6PGDH/NADP-binding domains; retrieved literature independently supports that *C. albicans* has a protein named **CaGnd1** with this enzyme activity, though the papers did not explicitly print the full accession-to-locus crosswalk. | UniProt accession supplied by user; supporting literature 2021 review and 2009 to 2012 primary studies | (pqac-00000000, pqac-00000029, pqac-00000030) |
| Enzyme identity | **CaGnd1 = 6-phosphogluconate dehydrogenase (6PGD or 6PGDH)** | Primary *Candida* studies explicitly identify **Gnd1** as the 6-phosphogluconate dehydrogenase of the oxidative PPP; assays monitored NADP+ reduction at 340 nm using **6-phosphogluconate** substrate. | https://doi.org/10.1111/j.1567-1364.2011.00761.x (2012); earlier primary study retrieved as 2009 report | (pqac-00000025, pqac-00000031, pqac-00000032) |
| EC number and cofactor | **EC 1.1.1.44; NADP+-dependent** | Authoritative reviews describe 6PGDH as catalyzing oxidative decarboxylation in the oxidative PPP and, in fungal yeasts, list **NADP+** as the cofactor, generating **NADPH**. | https://doi.org/10.1107/S2053230X22001091 (2022); https://doi.org/10.3390/biom11050725 (2021) | (pqac-00000012, pqac-00000017, pqac-00000019) |
| Pathway assignment | **Oxidative pentose phosphate pathway** | Gnd1 is one of the two NADPH-producing dehydrogenases in the oxidative PPP, alongside Zwf1; pathway diagrams and gene-expression analyses in *C. albicans* place **ZWF1 to 6-phosphogluconate to GND1** as the NADPH-generating branch. | https://doi.org/10.1128/msphere.00040-25 (2025); https://doi.org/10.3390/biom11050725 (2021) | (pqac-00000006, pqac-00000010, pqac-00000022) |
| Catalyzed reaction | **6-phosphogluconate + NADP+ to ribulose-5-phosphate + CO2 + NADPH** | Reviews describe 6PGDH as catalyzing the oxidative decarboxylation of **6-phosphogluconate** to **ribulose-5-phosphate**, producing the **second NADPH** of the oxidative PPP; *Candida* primary literature specifically states that Gnd1 converts 6-phosphogluconate to ribulose-5-phosphate. | https://doi.org/10.1107/S2053230X22001091 (2022); https://doi.org/10.3390/biom11050725 (2021); *Candida* primary studies from 2009 and 2012 | (pqac-00000012, pqac-00000018, pqac-00000032) |
| Functional importance | **NADPH production and redox homeostasis** | Gnd1 supplies reducing power needed for biosynthesis and oxidative stress defense; in *C. albicans* iron limitation induces PPP genes including **GND1** and increases oxidative PPP NADPH production. | https://doi.org/10.1128/msphere.00040-25 (2025) | (pqac-00000006, pqac-00000008, pqac-00000022) |
| Predominant subcellular localization | **Mostly cytosolic** | Fractionation of oleate-grown cells showed about **95% of Gnd1 activity in the cytosolic S fraction**; the majority of tagged Gnd1 signal was cytosolic by microscopy and immunoblot. | https://doi.org/10.1111/j.1567-1364.2011.00761.x (2012); earlier primary study retrieved as 2009 report | (pqac-00000025, pqac-00000029, pqac-00000031) |
| Minor subcellular localization | **Small peroxisomal pool** | Biochemical fractionation and Nycodenz gradients found a **small Gnd1 activity peak** in organellar fractions co-migrating with peroxisomal markers; the 2009 study reports the remaining **5 to 10 percent** of Zwf1 and Gnd1 activity in the organellar fraction, with Gnd1 only partially co-localizing with the peroxisomal marker. | 2009 primary study retrieved; https://doi.org/10.3390/biom11050725 (2021) | (pqac-00000027, pqac-00000031, pqac-00000020) |
| Mechanism of dual localization | **Alternative splicing generates a peroxisomal isoform** | GND1 contains an intron encoding an in-frame **PTS2** motif; the **spliced transcript** encodes the cytosolic isoform, whereas an **alternatively spliced or unspliced transcript** yields a PTS2-containing isoform targeted to peroxisomes. qPCR showed the alternatively spliced transcript is about **1000-fold less abundant** than the spliced transcript. | https://doi.org/10.1111/j.1567-1364.2011.00761.x (2012) | (pqac-00000026, pqac-00000029, pqac-00000032) |
| Peroxisomal import machinery | **PTS2 and Pex7 dependent** | Deletion of **PEX7**, the PTS2 receptor, abolished or strongly reduced the peroxisomal Gnd1 signal and activity peak, showing that import of the minor peroxisomal isoform depends on **Pex7**. | https://doi.org/10.1111/j.1567-1364.2011.00761.x (2012); earlier primary study retrieved as 2009 report | (pqac-00000026, pqac-00000027, pqac-00000028) |
| Carbon-source dependence of isoforms | **Peroxisomal isoform more evident on oleate** | In glucose-grown cells immunoblots showed mainly one about **60 kDa** Gnd1 band, whereas **oleate-grown** cells showed a second minor band near **63 kDa** consistent with the low-abundance PTS2-containing isoform; peroxisome-inducing conditions using oleate and maltose were used to visualize targeting. | https://doi.org/10.1111/j.1567-1364.2011.00761.x (2012) | (pqac-00000026, pqac-00000029) |
| Expert interpretation and annotation confidence | **High confidence for enzyme function; moderate confidence for exact accession to locus mapping from retrieved texts** | The combined evidence strongly supports that *C. albicans* **Gnd1** is the NADP+-dependent 6PGDH of the oxidative PPP and is dual localized to cytosol and peroxisomes. The exact mapping from the retrieved literature to **A0A1D8PFS4 equals orf19.12491 equals CAALFM_C113860CA** relies on the user-provided UniProt record because most papers use the protein name **Gnd1** rather than the ORF or accession. | User-supplied UniProt context plus 2009 and 2012 primary studies plus 2021 review | (pqac-00000000, pqac-00000025, pqac-00000030) |


*Table: This table consolidates the user-provided identifiers for the *Candida albicans* target with literature-supported functional annotation and localization evidence. It is useful for checking that the inferred annotation matches experimentally studied CaGnd1 while keeping track of where the exact accession mapping is direct versus inferred.*