aroF-I

UniProt ID: Q88KG6
Organism: Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)
Review Status: DRAFT
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Gene Description

aroF-I (PP_2324) encodes a predicted class-I 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase (DAHP synthase; EC 2.5.1.54) in Pseudomonas putida KT2440. DAHP synthase catalyzes the aldol-like condensation of phosphoenolpyruvate and D-erythrose 4-phosphate to form DAHP, the first committed step of the shikimate pathway. That pathway produces chorismate, the branch-point precursor for phenylalanine, tyrosine, tryptophan, folate, ubiquinone, and other aromatic metabolites. KT2440 has multiple DAHP synthase paralogs, including aroH, aroF-I, and aroF-II, whose feedback regulation and relative in vivo flux contributions remain unresolved.

Existing Annotations Review

GO Term Evidence Action Reason
GO:0003849 3-deoxy-7-phosphoheptulonate synthase activity
IEA
GO_REF:0000120
ACCEPT
Summary: aroF-I is a class-I DAHP synthase family protein with EC 2.5.1.54 annotation, matching condensation of phosphoenolpyruvate and erythrose 4-phosphate to DAHP.
Reason: This is the core molecular function and is supported by PIRNR/Pfam/InterPro family evidence. Direct biochemical data for this specific paralog were not found in this first pass.
GO:0005737 cytoplasm
IEA
GO_REF:0000118
ACCEPT
Summary: DAHP synthase is a soluble central-metabolism enzyme acting on cytoplasmic substrates.
Reason: Cytoplasmic localization is appropriate for a bacterial shikimate-pathway enzyme and no secretion or membrane features are indicated.
GO:0009073 aromatic amino acid biosynthetic process
IEA
GO_REF:0000120
ACCEPT
Summary: DAHP synthase initiates the shikimate pathway that supplies chorismate for all three aromatic amino acid branches.
Reason: Correct biological process for this enzyme class. The specific aromatic amino-acid branch affected by this paralog's feedback regulation is not resolved.
GO:0042802 identical protein binding
IEA
GO_REF:0000117
MARK AS OVER ANNOTATED
Summary: Class-I DAHP synthases are commonly oligomeric, but identical protein binding is a generic structural interaction term rather than the informative biochemical function.
Reason: The annotation adds little beyond the catalytic DAHP synthase activity and appears electronically propagated. Generic protein-binding-style terms are not useful as core molecular functions here.
GO:0009423 chorismate biosynthetic process
IEA
GO_REF:0000041
ACCEPT
Summary: DAHP synthase catalyzes the entry reaction into the shikimate pathway, upstream of chorismate.
Reason: This is the most specific pathway-process annotation available in GOA for the anabolic role of aroF-I.

Core Functions

Predicted class-I DAHP synthase catalyzing condensation of phosphoenolpyruvate and D-erythrose 4-phosphate to DAHP, the entry reaction of the shikimate pathway leading to chorismate.

Supporting Evidence:

References

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Suggested Questions for Experts

Q: What are the feedback-inhibition properties and relative in vivo contributions of aroH, aroF-I, and aroF-II in KT2440 aromatic amino acid biosynthesis?

Deep Research

Asta

(aroF-I-deep-research-asta.md)

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