TreeGrafter-generated GO annotations
Combined Automated Annotation using Multiple IEA Methods
Pseudomonas putida KT2440 Strain Metabolizes Glucose through a Cycle Formed by Enzymes of the Entner-Doudoroff, Embden-Meyerhof-Parnas, and Pentose Phosphate Pathways
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Deletion of tpiA (PP_4715, triose phosphate isomerase) abolishes growth of KT2440 on both glucose and succinate, demonstrating an essential role in triose-phosphate interconversion under glycolytic and gluconeogenic conditions. TpiA activity is present (equally active) in both glucose- and succinate-grown cells.
Deep research report (falcon) for tpiA / Q88DV4
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TIM/TPI catalyzes the reversible, stereospecific, cofactor-independent isomerization of DHAP and D-glyceraldehyde 3-phosphate; the enzyme is a near-perfect diffusion-limited homodimer with the canonical (beta/alpha)8 TIM-barrel fold, conserved catalytic His95 electrophile and Glu167 proton acceptor.
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In KT2440, deletion of tpiA (PP_4715) abolishes growth on both glucose and succinate, an unexpectedly strong requirement given the ED-dominated glucose catabolism, demonstrating that triose-phosphate interconversion is indispensable under both glycolytic and gluconeogenic conditions.