aroH

UniProt ID: Q88LR3
Organism: Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)
Review Status: DRAFT
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Gene Description

aroH (PP_1866) encodes a class-II (type-II) 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase (DAHP synthase / DAH7PS; EC 2.5.1.54) in Pseudomonas putida KT2440. The enzyme catalyzes the aldol-like condensation of phosphoenolpyruvate (PEP) and D-erythrose 4-phosphate (E4P), with release of phosphate, to form 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP). This is the first committed step of the shikimate pathway, which ultimately produces chorismate, the branch-point precursor for the aromatic amino acids (phenylalanine, tyrosine, tryptophan) and many other aromatic metabolites. Class-II DAH7PS enzymes adopt a (beta/alpha)8 TIM-barrel fold and require a divalent metal cation for catalysis; the UniProt record for this protein indicates activity with manganese, cobalt or cadmium ions, with one cation bound per subunit. In bacterial DAHP-synthase nomenclature, AroH is conventionally the tryptophan-sensitive isoenzyme, although the regulatory properties of this specific P. putida protein have not been characterized experimentally. As a soluble central-metabolism enzyme acting on cytosolic substrates, AroH is expected to function in the cytoplasm.

Existing Annotations Review

GO Term Evidence Action Reason
GO:0003849 3-deoxy-7-phosphoheptulonate synthase activity
IEA
GO_REF:0000120
ACCEPT
Summary: Core molecular function. The protein belongs to the class-II DAHP synthase family (RuleBase RU363071; InterPro IPR002480/PF01474; TIGR01358 DAHP_synth_II) and the UniProt catalytic-activity record (Rhea:14717, EC 2.5.1.54) describes condensation of PEP + E4P + H2O to DAHP + phosphate, exactly matching this GO term.
Reason: This term precisely captures the enzymatic activity of a class-II DAHP synthase. The assignment is strongly supported by sequence/family evidence (InterPro, RuleBase, NCBIfam TIGR01358) and conserved PEP- and metal-binding residues annotated in UniProt. This is the gene's core molecular function.
Supporting Evidence:
file:PSEPK/aroH/aroH-deep-research-falcon.md
AroH is a DAH7PS catalyzing PEP + E4P -> DAHP/DAH7P and feeding the shikimate pathway; best-supported assignment is class-II / type-II DAH7PS (TIM-barrel fold, conserved metal-binding site), compatible with the UniProt/InterPro/Pfam context for Q88LR3 (PF01474 / DAHP_synth_2). No direct biochemical characterization of P. putida KT2440 AroH was found, so this is family/sequence-level inference.
GO:0009073 aromatic amino acid family biosynthetic process
IEA
GO_REF:0000002
ACCEPT
Summary: Correct biological process. DAHP synthase catalyzes the first committed step of the shikimate pathway, which feeds chorismate biosynthesis and the downstream aromatic amino acid (Phe/Tyr/Trp) biosynthetic branches.
Reason: This is the canonical pathway role of a DAHP synthase and is consistent with the molecular function annotation. The term is appropriate and represents a core biological process for this gene. (The GOA stub used the label "aromatic amino acid biosynthetic process"; the current GO label for GO:0009073 is "aromatic amino acid family biosynthetic process" and is used here.)

Core Functions

Catalyzes the first committed step of the shikimate pathway, the condensation of phosphoenolpyruvate and D-erythrose 4-phosphate to form 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP), as a class-II DAHP synthase.

Supporting Evidence:
  • GO_REF:0000120
    3-deoxy-7-phosphoheptulonate synthase activity (GO:0003849); EC 2.5.1.54; Rhea:14717 PEP + E4P + H2O = DAHP + phosphate.

References

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Deep Research

Asta

(aroH-deep-research-asta.md)

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Falcon

(aroH-deep-research-falcon.md)

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