Q73YM4 · TRPD_MYCPA
- ProteinAnthranilate phosphoribosyltransferase
- GenetrpD
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids367 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
Catalytic activity
- N-(5-phospho-beta-D-ribosyl)anthranilate + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + anthranilate
Cofactor
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 104 | 5-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 104 | anthranilate 1 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 107-108 | 5-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI) | ||||
Sequence: GD | ||||||
Binding site | 112 | 5-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 114-117 | 5-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI) | ||||
Sequence: NLST | ||||||
Binding site | 116 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 132-140 | 5-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI) | ||||
Sequence: KHGNRAASS | ||||||
Binding site | 135 | anthranilate 1 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 144 | 5-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 190 | anthranilate 2 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 248 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 249 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 249 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | anthranilate phosphoribosyltransferase activity | |
Molecular Function | magnesium ion binding | |
Biological Process | tryptophan biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAnthranilate phosphoribosyltransferase
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Mycobacteriaceae > Mycobacterium > Mycobacterium avium complex (MAC)
Accessions
- Primary accessionQ73YM4
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000227169 | 1-367 | Anthranilate phosphoribosyltransferase | |||
Sequence: MALSSESSAASAARRPSGGPATSWRQVLARLTGGDDLARGQAAWAMDQIMTGEASPAQIAAFAVAMQVKVPTSAEVIELAEVMLNHALPFPAGAIRDDTVDIVGTGGDGVNTLNLSTMAAIVAAAAGVPVVKHGNRAASSLSGGADTLEELGVRIDLGPEQVARSVAEVGIGFCFAPLFHPSYRHTSAVRREIGVPTVFNLLGPLTNPARPRAGLIGCAFAELAEVMAGVFAARRSSVLVVHGDDGLDELTTTTTSTIWRVQAGTVDRLTFDPAGFGFPRAELDDLLGGDAQTNAAEVRAVLAGGQGPVRDAVVLNAAGAIVAHAGLSSRAEWLPAWEDGLARASAAIDSGAAEQLLARWVRFGQQL |
Interaction
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-24 | Disordered | ||||
Sequence: MALSSESSAASAARRPSGGPATSW |
Sequence similarities
Belongs to the anthranilate phosphoribosyltransferase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length367
- Mass (Da)37,729
- Last updated2004-07-05 v1
- Checksum05F73559DB6DAEFE
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE016958 EMBL· GenBank· DDBJ | AAS04248.1 EMBL· GenBank· DDBJ | Genomic DNA |