A0A4R5WAM9 · A0A4R5WAM9_MYCMU

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.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Pathway

Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 1/5.

GO annotations

AspectTerm
Molecular Functionanthranilate synthase activity
Molecular Functionmetal ion binding
Biological Processtryptophan biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Anthranilate synthase component 1
  • EC number

Gene names

    • Name
      trpE
    • ORF names
      EUA03_20280

Organism names

Accessions

  • Primary accession
    A0A4R5WAM9

Proteomes

Interaction

Subunit

Heterotetramer consisting of two non-identical subunits: a beta subunit (TrpG) and a large alpha subunit (TrpE).

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain28-169Anthranilate synthase component I N-terminal
Domain226-484Chorismate-utilising enzyme C-terminal

Sequence similarities

Belongs to the anthranilate synthase component I family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    501
  • Mass (Da)
    54,067
  • Last updated
    2019-07-31 v1
  • Checksum
    BCF0170310BADC4E
MKTTSREEFQALAAEHRVVPVTRKVLADSETPLSAYRKLAANRPGTFLLESAENGRSWSRWSFIGAGAPSALTVRDGEAVWLGNTPQDAPSGGDPLQAVRDTLALLQTAPVPGLPPLSSGLVGYFAYDMVRRLERLPELAVDDLKLPDMVLLLATDMAAVDHHEGTITLIANAVNWNGTDERVDWAYDDAVARLDVMTKALGEPLPSSIATFSRPQPQPRQQRTVEEYTAIVEKLVGDIEAGEAFQVVPSQRFEMDTAADPIDVYRVLRVTNPSPYMYLLNVPNAEGGLDFSVVGSSPEALVTVKDGVATTHPIAGTRWRGATEEDDILLEKELLADDKERSEHLMLVDLGRNDLGRVCKPGTVRVEDYSHIERYSHVMHLVSTVTGHLADDKTALDAVTACFPAGTLSGAPKVRAMELIEEVELTRRGLYGGVLGYLDFAGNADFAIAIRTALMRAGTAYVQAGGGVVADSNGPYEYNESSNKAKAVLAAIAAAETLSEP

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
SDLO01000019
EMBL· GenBank· DDBJ
TDK86327.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp