A0A931CTE9 · A0A931CTE9_9BACT
- ProteinAnthranilate phosphoribosyltransferase
- GenetrpD
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids339 (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 | 81 | 5-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 81 | anthranilate 1 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 84-85 | 5-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI) | ||||
Sequence: GD | ||||||
Binding site | 89 | 5-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 91-94 | 5-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI) | ||||
Sequence: NIST | ||||||
Binding site | 93 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 109-117 | 5-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI) | ||||
Sequence: KHGNRSVSS | ||||||
Binding site | 112 | anthranilate 1 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 121 | 5-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 167 | anthranilate 2 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 226 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 227 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 227 | 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 > Thermodesulfobacteriota > Desulfobacteria > Desulfobacterales > Desulfobacteraceae > Desulfotignum
Accessions
- Primary accessionA0A931CTE9
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
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: QYLNQIIRGQDLTQDQAAEMITHIFSGTITPAQTGAFMAALATKGECFEELAGGALAMRRKA | ||||||
Domain | 74-324 | Glycosyl transferase family 3 | ||||
Sequence: QTVIDIVGTGGDGTGTFNISTTASFVVAGAGITVAKHGNRSVSSKCGSADVLEALGVNLAADPEIIEEAINEIGIGFMFAPLYHGSMKHAMTARKECGIRSIFNMLGPLTNPAAASCQVVGVYAPALTEMFANALHLLGVRRAFVVHGHDGMDEITTTDLTRVSELSNGRIKSYDLDPLTYFDDYADPETLQGGDAKENAAILTRILSGEKGAPRDIVLINAGAGLVAANAAADIRQGIQMAADSIDSGRA |
Sequence similarities
Belongs to the anthranilate phosphoribosyltransferase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length339
- Mass (Da)35,787
- Last updated2023-02-22 v1
- Checksum373F6818B2DCF51C