trpE

UniProt ID: Q88QS1
Organism: Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)
Review Status: DRAFT
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Gene Description

Anthranilate synthase component I (TrpE, locus PP_0417), the large alpha subunit of anthranilate synthase (EC 4.1.3.27). Together with the glutamine amidotransferase beta subunit TrpG, it forms a heterotetrameric complex that catalyzes the first committed step of L-tryptophan biosynthesis, the conversion of chorismate to anthranilate. TrpE binds chorismate and performs the amination/lyase chemistry, using ammonia supplied by TrpG from hydrolysis of L-glutamine; the products are anthranilate, pyruvate and L-glutamate. In the absence of TrpG, TrpE alone can produce anthranilate directly from chorismate when free ammonia is abundant. The enzyme requires Mg2+ and is a soluble, cytoplasmic enzyme of aromatic amino acid primary metabolism. Anthranilate synthase is typically feedback-inhibited by L-tryptophan, the pathway end product. In P. putida KT2440, loss of trpE causes tryptophan auxotrophy that is rescued by anthranilate, indole or tryptophan, confirming its placement at the anthranilate-forming step.

Existing Annotations Review

GO Term Evidence Action Reason
GO:0000162 L-tryptophan biosynthetic process
IEA
GO_REF:0000120
ACCEPT
Summary: TrpE catalyzes the first committed step (chorismate to anthranilate) of de novo L-tryptophan biosynthesis. This is the correct, well-supported biological process for this enzyme.
Reason: Anthranilate synthase component I is the entry enzyme of the tryptophan branch of aromatic amino acid biosynthesis. The IEA assignment (InterPro IPR005256, UniPathway UPA00035) is corroborated by experimental genetics in KT2440, where a trpE (PP_0417) insertion mutant is a tryptophan auxotroph rescued by anthranilate, indole or tryptophan (PMID:21261884; see file:PSEPK/trpE/trpE-deep-research-falcon.md).
GO:0004049 anthranilate synthase activity
IEA
GO_REF:0000120
ACCEPT
Summary: TrpE is the synthase (alpha) component of anthranilate synthase (EC 4.1.3.27), catalyzing chorismate + L-glutamine to anthranilate + pyruvate + L-glutamate (RHEA:21732). This is the core molecular function and is correct.
Reason: Assigned from InterPro IPR005256, RHEA:21732 and EC 4.1.3.27, consistent with the protein family (anthranilate synthase component I), the Pfam chorismate-binding domain, and the UniProt catalytic activity annotation. GO:0004049 is the precise molecular function term.

Core Functions

Anthranilate synthase component I activity - binds chorismate and, using ammonia supplied by the TrpG glutaminase subunit (or free ammonia at high concentration), converts chorismate to anthranilate with release of pyruvate, the first committed step of L-tryptophan biosynthesis.

Supporting Evidence:
  • GO_REF:0000120
    Anthranilate synthase component 1; EC 4.1.3.27; Reaction=chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate + H(+); Rhea:RHEA:21732.
  • PMID:21261884
    A trpE mutant did not grow on minimal medium but growth was restored by anthranilate, indole, or tryptophan supplementation, placing TrpE (PP_0417) at the anthranilate-forming step of tryptophan biosynthesis.

References

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Deep Research

Asta

(trpE-deep-research-asta.md)

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Falcon

(trpE-deep-research-falcon.md)

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