pykA (PP_1362) encodes one of the two pyruvate kinase isozymes of Pseudomonas putida KT2440, the other being pyk (PP_4301). Pyruvate kinase transfers the phosphoryl group of phosphoenolpyruvate to ADP, forming pyruvate and ATP in the final, essentially irreversible step of lower glycolysis. In KT2440, which catabolises glucose almost exclusively through the Entner-Doudoroff route, this reaction sits at the PEP-pyruvate branch point that partitions carbon between pyruvate oxidation and PEP-consuming anaplerotic and biosynthetic reactions.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000287 magnesium ion binding | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: Mg2+ cofactor of pyruvate kinase. Reason: Metal binding is a cofactor property of the catalytic activity. Supporting Evidence: file:PSEPK/pykA/pykA-uniprot.txt DR InterPro; IPR015793; Pyrv_Knase_brl. |
| GO:0004743 pyruvate kinase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Exact pyruvate kinase activity. Reason: Q88N54 carries the TIGR01064 pyruvate kinase and PROSITE PK active-site signatures. Supporting Evidence: file:PSEPK/pykA/pykA-uniprot.txt DR NCBIfam; TIGR01064; pyruv_kin; 1. file:PSEPK/pykA/pykA-uniprot.txt DR PROSITE; PS00110; PYRUVATE_KINASE; 1. file:PSEPK/pykA/pykA-deep-research-openscientist.md encodes a **cytoplasmic pyruvate kinase (EC 2.7.1.40)** |
| GO:0006096 glycolytic process | IEA GO_REF:0000120 | ACCEPT | Summary: Pyruvate kinase catalyses the last step of lower glycolysis. Reason: Even in the ED-dominated KT2440, triose phosphates proceed through the lower glycolytic trunk to PEP, and pyruvate kinase catalyses its final step. Supporting Evidence: PMID:26350459 glycolysis is known to proceed almost exclusively through the Entner-Doudoroff (ED) route file:PSEPK/pykA/pykA-uniprot.txt DR NCBIfam; TIGR01064; pyruv_kin; 1. |
| GO:0030955 potassium ion binding | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: K+ activation is a family property of pyruvate kinases. Reason: Monovalent-cation activation is typical of PKs; cation binding is cofactor context for the activity. Supporting Evidence: file:PSEPK/pykA/pykA-uniprot.txt DR InterPro; IPR001697; Pyr_Knase. |
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Download this section (compressed HTML)Q: Which of the two KT2440 pyruvate kinases carries most PEP-to-pyruvate flux on glucose, and are they regulated like the P. aeruginosa PykA (glucose 6-phosphate activated) and PykF isoforms?
Experiment: Measure growth and PEP/pyruvate pools of single and double pyk mutants of KT2440 on glucose and purify both isozymes for effector screening.
Type: mutant physiology and enzyme kinetics
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Download this section (compressed HTML)Curated by Claude (AI-assisted). Rows that quoted DR GO lines or ARBA-only text were
re-supported with family/domain classification (NCBIfam, PIRSF, HAMAP, PROSITE, InterPro) and,
where useful, orthologue literature. Correct-but-general parent terms are MODIFY to the specific
activity already on the gene. Verdicts were aligned with the experimentally anchored E. coli
(aceE, aceF, ppc, pykF, ppsA) and B. subtilis (pycA) reviews. The KT2440 PDH/OGDH E3 is LpdG
(PP_4187), not Lpd (PP_5366, LPD-3). No KT2440-specific enzymology was found for this gene.
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