A0A285NKT0 · A0A285NKT0_9PSED
- ProteinAnthranilate phosphoribosyltransferase
- GenetrpD
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids349 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
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 | 82 | 5-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 82 | anthranilate 1 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 85-86 | 5-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI) | ||||
Sequence: GD | ||||||
Binding site | 92-95 | 5-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI) | ||||
Sequence: NVST | ||||||
Binding site | 94 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 110-118 | 5-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI) | ||||
Sequence: KHGNRAVSG | ||||||
Binding site | 113 | anthranilate 1 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 122 | 5-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 168 | anthranilate 2 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 227 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 228 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 228 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
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 > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas
Accessions
- Primary accessionA0A285NKT0
Proteomes
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 5-66 | Glycosyl transferase family 3 N-terminal | ||||
Sequence: AALARVVDHLDLSTDEMRDVMRLIMTGQCTDAQIGAFLMGLRMKSESIDEIVGAVSAMRELA | ||||||
Domain | 76-329 | Glycosyl transferase family 3 | ||||
Sequence: RVVDIVGTGGDGANIFNVSTAASLVVAAAGCTVAKHGNRAVSGKSGSADLLEAAGVYLNLTPVQVARCIDSVGIGFMFAQSHHGAMKHAAGPRRDLGLRTLFNMIGPLTNPAGVVHQVVGVFSQALCRPVAEVLARLGSKHVLVVHSKDGLDEFSLAAPTFVAELRHGEITEYWVQPETLGIQSQSLYGLEVESPQASLQLIRDAITRRKTAQGQKAAEMIVLNAGAALYAADHASSLKEGVALAHDALHTGLA |
Sequence similarities
Belongs to the anthranilate phosphoribosyltransferase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length349
- Mass (Da)36,897
- Last updated2017-11-22 v1
- Checksum3A85F65450189539
Keywords
- Technical term