Inner-membrane quinoprotein glucose dehydrogenase whose periplasm-facing catalytic domain oxidizes D-glucose to D-glucono-1,5-lactone using PQQ and transfers electrons to ubiquinone. The lactone hydrolyzes to gluconate, which can enter either the gluconate kinase route or the 2-ketogluconate loop. Its secretion of gluconic acid also contributes indirectly to mineral phosphate solubilization under low-phosphate conditions.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0008876 quinoprotein glucose dehydrogenase activity | IEA GO_REF:0000120 | ACCEPT | Summary: The EC-supported term precisely describes the PQQ-dependent glucose oxidation reaction. Reason: This is the core molecular function and agrees with KT2440 biochemical evidence. Supporting Evidence: PMID:27287323 which is produced from glucose by a periplasmic glucose dehydrogenase (GDH) that requires pyrroloquinoline quinone (PQQ) as a redox coenzyme. |
| GO:0016020 membrane | IEA GO_REF:0000002 | MODIFY | Summary: Gcd is a bacterial inner-membrane protein, so the source term is too broad. Reason: Replace the generic membrane term with the current bacterial inner-membrane component; obsolete GO:0005887 is replaced by GO:0005886. Proposed replacements: plasma membrane Supporting Evidence: file:PSEPK/gcd/gcd-uniprot.txt FT TRANSMEM 12..35 |
| GO:0016614 oxidoreductase activity, acting on CH-OH group of donors | IEA GO_REF:0000002 | MARK AS OVER ANNOTATED | Summary: This broad parent adds no information beyond GO:0008876. Reason: Retain the exact quinoprotein glucose dehydrogenase term as the core MF. |
| GO:0048038 quinone binding | IEA GO_REF:0000002 | MODIFY | Summary: Gcd binds PQQ specifically rather than an unspecified quinone. Reason: The specific cofactor-binding child term is supported by the enzyme biochemistry. Proposed replacements: pyrroloquinoline quinone binding Supporting Evidence: PMID:27287323 requires pyrroloquinoline quinone (PQQ) as a redox coenzyme |
| GO:0019595 non-phosphorylated glucose catabolic process | IMP | NEW | Summary: KT2440 genetics and flux analysis place Gcd at the start of periplasmic oxidative glucose catabolism. Reason: This is more specific than broad glucose catabolism and covers the non-phosphorylated peripheral routes. Supporting Evidence: PMID:17483213 glucose catabolism in Pseudomonas putida occurs through the simultaneous operation of three pathways that converge at the level of 6-phosphogluconate file:PSEPK/gcd/gcd-deep-research-falcon.md Gluconate generated by Gcd can be further oxidized by the membrane-associated **gluconate 2-dehydrogenase (Gad) complex** |
| GO:0042597 periplasmic space | ISS | NEW | Summary: The membrane-anchored enzyme performs glucose oxidation on the periplasmic side. Reason: Use is_active_in because the catalytic domain faces the periplasm while the protein is membrane-integral. Supporting Evidence: PMID:27287323 periplasmic glucose dehydrogenase (GDH) |
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