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A0A101FL26 · A0A101FL26_9BACT

Function

function

Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
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 )

Note: Binds 2 magnesium ions per monomer.

Pathway

Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 2/5.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site805-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI)
Binding site80anthranilate 1 (UniProtKB | ChEBI)
Binding site83-845-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI)
Binding site885-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI)
Binding site90-935-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI)
Binding site92Mg2+ 1 (UniProtKB | ChEBI)
Binding site108-1165-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI)
Binding site111anthranilate 1 (UniProtKB | ChEBI)
Binding site1205-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI)
Binding site166anthranilate 2 (UniProtKB | ChEBI)
Binding site225Mg2+ 2 (UniProtKB | ChEBI)
Binding site226Mg2+ 1 (UniProtKB | ChEBI)
Binding site226Mg2+ 2 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Functionanthranilate phosphoribosyltransferase activity
Molecular Functionmagnesium ion binding
Biological Processtryptophan biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Anthranilate phosphoribosyltransferase
  • EC number

Gene names

    • Name
      trpD
    • ORF names
      XD68_1451

Organism names

Accessions

  • Primary accession
    A0A101FL26

Proteomes

Subcellular Location

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain4-65Glycosyl transferase family 3 N-terminal
Domain74-324Glycosyl transferase family 3

Sequence similarities

Belongs to the anthranilate phosphoribosyltransferase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    343
  • Mass (Da)
    36,252
  • Last updated
    2016-04-13 v1
  • MD5 Checksum
    4A3641C19059FC72B558BF79F707260C
MLRHYIEKVTGRKSLSFDEMAKAMEIIMDGQATEIQSAGLLIGLKAKVESVEEITAAAFVMREKALRVETDAPILMDTCGTGGDGKGTFNISTAVAFIVASAGIPVAKHGNRSVSSRCGSADVLEALDIPIFSSPEQVKASIESVGFGFCFAPYFHQATKNVARPRKELGVRTIFNILGPLTNPAGANYQLLGVYDPNLVLPIAEALENLGTKGAIVVHGSGGMDEFSLCGPNKVALLRDGKIKELMVAPEDAGLARASLEDVAGYSPEDNARILAAVLSGERGPKRDVVVFNAAAAFVATDMAKTFKEGAHLAEDLIDSGKAMDKLLQVKAFAHSLVEVAQC

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LGFQ01000086
EMBL· GenBank· DDBJ
KUK38992.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

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.
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