Modified TCA cycles also appear to be critical in the adaptation to a toxic environment. We have recently identified a modified TCA cycle with decreases in NAD-dependent isocitrate dehydrogenase and KGDH activities and an increased NADP-dependent isocitrate dehydrogenase activity. This alternative TCA cycle plays a critical role in the adaptation of the cellular systems to oxidative stress owing to its ability to produce increased amounts of the Lucidenic-acid-L antioxidant NADPH and decreased amounts of the pro-oxidant NADH. Furthermore, a-ketoglutarate also contributes to the detoxification of ROS. The tailoring of the TCA cycle towards an antioxidant defense network appears to be orchestrated by NAD kinase and NADP phosphatase. Although many aspects of this metabolic machinery have been delineated, its regulation, its interaction with other metabolic pathways, the significance of its non-cyclic attributes and its integration into the global molecular networks have yet to be fully elucidated. In this report, we have identified an alternative TCA cycle that enables the soil microbe P.fluorescens exposed to Al to generate ATP by a substrate-level phosphorylation module as oxidative phosphorylation, a process reliant on iron is severely impeded. Al promotes dysfunctional Fe metabolism. This novel ATP-producing module works in tandem with AGODH, SCS, OCT, and ICL to generate oxalate, an Al-sequester. The diversion of succinyl-CoA toward ATP synthesis during Al-toxicity, Fedeprivation, and Lithospermic-acid anaerobiosis is also discussed. We have previously demonstrated that ICL was drastically increased in cells treated with Al compared to control. However, the increased activity of ICL was not coupled to the concomitant increase of MS; this could account for the accumulation of glyoxylate. This glyoxylate appeared to be diverted towards the production of oxalate, a moiety known to render Al innocuous. The amounts of oxalate were dependent on the concentration of Al in the stressed medium. Hence, the two possible enzymes involved in the oxidation of glyoxylate to oxalate, glyoxylate dehydrogenase and AGODH, were probed by in-gel activity staining.