Q44697 · TRPE_BUCDN
- ProteinAnthranilate synthase component 1
- GenetrpE
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids519 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia (By similarity).
Catalytic activity
- chorismate + L-glutamine = anthranilate + H+ + L-glutamate + pyruvate
Cofactor
Note: Binds 1 Mg2+ ion per subunit.
Activity regulation
Feedback inhibited by tryptophan.
Pathway
Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 1/5.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 40 | L-tryptophan (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 293-295 | L-tryptophan (UniProtKB | ChEBI) | ||||
Sequence: PYM | ||||||
Binding site | 330-331 | chorismate (UniProtKB | ChEBI) | ||||
Sequence: GT | ||||||
Binding site | 363 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 451 | chorismate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 471 | chorismate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 485-487 | chorismate (UniProtKB | ChEBI) | ||||
Sequence: GSG | ||||||
Binding site | 487 | chorismate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 500 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | anthranilate synthase activity | |
Molecular Function | metal ion binding | |
Biological Process | tryptophan biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAnthranilate synthase component 1
- EC number
- Short namesAS; ASI
Gene names
Encoded on
- Plasmid pBDn
Organism names
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Erwiniaceae > Buchnera
Accessions
- Primary accessionQ44697
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000154083 | 1-519 | Anthranilate synthase component 1 | |||
Sequence: MEKKPYEIKIIQKKAKYHPDPTIVFNHICGSQKQTLLLETAEINKKNDLESIMIIDAALRISSERNHSVQLTALSKNGENILSILKSNLKQKVQMFIQDTSIRLEFPHFQKNLDEDKKIFSLSIFDTFRFIMKFFKNRNKVQKAMFFGGLFSYDLISNFELLPKLKKTQKCPHFCFYLAETLLIVDHQKKTCLIQNSLFTKNSHEQMRVEKRGREIQKKLEASLNSIPVRQEVKNSMLTANMSDEQYCSIIKKLQILIRKGEIFQVVPSRKFFLPCSNPLSAYQKLKKSNPSPYMFFMQDKDFTLFGASPESSLKYDDTTRQVELYPIAGTRPRGRNMDGTLNLDLDSRIELEMRTNHKELAEHLMLVDLARNDLARICEPGSRYVSDLVRVDKYPHVMHLVSRVVGTLKPELDALHAYAACMNMGTLTGAPKIRAMELIAEYEMEQRGSYGGAIGYFTDLGNLDTCITIRSAYVEDNIATIQSGSGIVYNSIPEDEVKEGINKAKRVINAIQHAHHLV |
Interaction
Subunit
Heterotetramer consisting of two non-identical subunits: a beta subunit (TrpG) and a large alpha subunit (TrpE).
Structure
Sequence
- Sequence statusComplete
- Length519
- Mass (Da)59,521
- Last updated1996-11-01 v1
- ChecksumC04B205AD8D74ECB
Keywords
- Technical term