A0A1X9YAA4 · A0A1X9YAA4_9SPHN
- ProteinAnthranilate phosphoribosyltransferase
- GenetrpD
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids331 (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
- diphosphate + N-(5-phospho-beta-D-ribosyl)anthranilate = 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 | 78 | 5-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 78 | anthranilate 1 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 81-82 | 5-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI) | ||||
Sequence: GD | ||||||
Binding site | 86 | 5-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 88-91 | 5-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI) | ||||
Sequence: NVST | ||||||
Binding site | 90 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 106-114 | 5-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI) | ||||
Sequence: KHGNRAASS | ||||||
Binding site | 109 | anthranilate 1 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 118 | 5-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 164 | anthranilate 2 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 223 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 224 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 224 | Mg2+ 1 (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
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Sphingomonadales > Sphingomonadaceae > Sphingomonas
Accessions
- Primary accessionA0A1X9YAA4
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 13-63 | Glycosyl transferase family 3 N-terminal | ||||
Sequence: PLDQATAHAAFADMLDGRANEAEAQAFLTVMAERDETSVEIAAAAMALRER | ||||||
Domain | 73-321 | Glycosyl transferase family 3 | ||||
Sequence: AIDVCGTGGDGAHSLNVSTAVAIVVAACGVPVAKHGNRAASSKAGSSDTLEALGLDLDRASARAEASLNDLGIAFLFAQLHHPSLKRLAAVRRAIGRRTIFNLIGPIANPARVTRQLIGVARPDYLPVYADALRLIGTESAMMVAGDEPLDELSIAGPSSAIRIGACGEGAIRIVPEDAGLTRHPLEALRGGDAVYNADALRRLLLGEQGAYRDAVLLNAAAALIVAGHATDLHAGVEEAAETIDKGLA |
Sequence similarities
Belongs to the anthranilate phosphoribosyltransferase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length331
- Mass (Da)34,234
- Last updated2017-08-30 v1
- ChecksumDA2515DE118E3172
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP016306 EMBL· GenBank· DDBJ | ARS25743.1 EMBL· GenBank· DDBJ | Genomic DNA |