gntZ

UniProt ID: Q88FP6
Organism: Pseudomonas putida KT2440
Review Status: DRAFT
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Gene Description

gntZ (PP_4043) encodes a 6-phosphogluconate dehydrogenase family enzyme in Pseudomonas putida KT2440. UniProt and GOA identify it as a decarboxylating 6-phosphogluconate dehydrogenase (EC 1.1.1.44) with NADP binding, placing it in the pentose phosphate pathway step that oxidatively decarboxylates 6-phosphogluconate to ribulose 5-phosphate while generating NADPH. Current evidence supports Q88FP6 as the single KT2440 6-phosphogluconate dehydrogenase, acting at the 6-phosphogluconate branch point between Entner-Doudoroff flux and the oxidative PPP.

Existing Annotations Review

GO Term Evidence Action Reason
GO:0004616 phosphogluconate dehydrogenase (decarboxylating) activity
IEA
GO_REF:0000120
ACCEPT
Summary: This is the exact catalytic activity for the annotated EC 1.1.1.44 enzyme. UniProt names Q88FP6 as decarboxylating 6-phosphogluconate dehydrogenase, and GOA links the term to InterPro and EC evidence.
Reason: The term captures the core molecular function of gntZ in the oxidative pentose phosphate pathway. Support is family-level: Q88FP6 matches the 6-phosphogluconate dehydrogenase signatures InterPro IPR006183 (Pgluconate_DH), Pfam PF00393 (6PGD C-terminal domain) and the NADP-binding domain IPR006115, and NCBIfam TIGR00872 (gnd_rel, the Gnd-related decarboxylating 6PGDH clade). The submitter-supplied protein name is not used as support, and Q88FP6 has not been assayed directly.
Supporting Evidence:
file:PSEPK/gntZ/gntZ-uniprot.txt
DR InterPro; IPR006183; Pgluconate_DH.
file:PSEPK/gntZ/gntZ-uniprot.txt
DR NCBIfam; TIGR00872; gnd_rel; 1.
file:PSEPK/gntZ/gntZ-uniprot.txt
DR Pfam; PF00393; 6PGD; 1.
GO:0006098 pentose-phosphate shunt
IEA
GO_REF:0000120
KEEP AS NON CORE
Summary: The enzyme catalyzes the oxidative PPP decarboxylation step producing ribulose 5-phosphate, so the broad pentose-phosphate shunt annotation is correct but less informative than the oxidative-branch child term.
Reason: The pathway placement follows both the enzyme chemistry and the UniPathway mapping in the GOA record; GO:0009051 is used for the core process.
Supporting Evidence:
file:PSEPK/gntZ/gntZ-uniprot.txt
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway.
file:PSEPK/gntZ/gntZ-deep-research-openscientist.md
This is the committed oxidative-decarboxylating step of the oxidative pentose phosphate pathway (oxPPP).
GO:0009051 pentose-phosphate shunt, oxidative branch
ISS
file:PSEPK/gntZ/gntZ-deep-research-openscientist.md
NEW
Summary: GntZ performs the oxidative decarboxylation that completes the oxidative pentose-phosphate branch and produces ribulose 5-phosphate and NADPH.
Reason: This child term captures the demonstrated pathway placement more precisely than the existing general pentose-phosphate shunt annotation.
Supporting Evidence:
file:PSEPK/gntZ/gntZ-deep-research-openscientist.md
This is the committed oxidative-decarboxylating step of the oxidative pentose phosphate pathway (oxPPP).
GO:0050661 NADP binding
IEA
GO_REF:0000002
KEEP AS NON CORE
Summary: NADP binding is consistent with the dehydrogenase family and with the NADP-dependent oxidative PPP reaction, but it is a cofactor property rather than the most informative function term.
Reason: Keep as useful catalytic context while treating GO:0004616 as the core molecular function.
Supporting Evidence:
file:PSEPK/gntZ/gntZ-deep-research-openscientist.md
The enzyme catalyzes the NADP⁺-dependent oxidative decarboxylation of 6-phospho-D-gluconate to D-ribulose-5-phosphate, COβ‚‚, and NADPH

Core Functions

Decarboxylating 6-phosphogluconate dehydrogenase that converts 6-phosphogluconate to ribulose 5-phosphate with NADPH production in the oxidative pentose phosphate pathway.

Supporting Evidence:
  • file:PSEPK/gntZ/gntZ-uniprot.txt
    DR InterPro; IPR006183; Pgluconate_DH.
  • file:PSEPK/gntZ/gntZ-uniprot.txt
    DR NCBIfam; TIGR00872; gnd_rel; 1.
  • file:PSEPK/gntZ/gntZ-uniprot.txt
    DR InterPro; IPR006115; 6PGDH_NADP-bd.

References

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Deep Research

OpenScientist

(gntZ-deep-research-openscientist.md)

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