A0A3R6W217 · A0A3R6W217_9CLOT
- ProteinAnthranilate phosphoribosyltransferase
- GenetrpD
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids335 (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 | 79 | 5-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 79 | anthranilate 1 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 82-83 | 5-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI) | ||||
Sequence: GD | ||||||
Binding site | 87 | 5-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 89-92 | 5-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI) | ||||
Sequence: NIST | ||||||
Binding site | 91 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 107-115 | 5-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI) | ||||
Sequence: KHGNRAASS | ||||||
Binding site | 110 | anthranilate 1 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 119 | 5-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 165 | anthranilate 2 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 224 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 225 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 225 | 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
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Clostridia > Eubacteriales > Clostridiaceae > Clostridium
Accessions
- Primary accessionA0A3R6W217
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 3-64 | Glycosyl transferase family 3 N-terminal | ||||
Sequence: KEAINTLVNGKDLTDEVMTQVMEEIMTGEATDAQKASFLTALSIKGETIDEITAAAKVMSSK | ||||||
Domain | 72-322 | Glycosyl transferase family 3 | ||||
Sequence: GDALEIVGTGGDKANSFNISTLSAIVAAAAGVHVAKHGNRAASSKCGTADCLEALGVKIDIEPEHSEKLLKEDGICFLFAQKYHPAMRFVGAVRKEMGIRTMFNVLGPLSNPARANMQLMGVYDEKLVEPLAHVLKNLGLKKLMVVYGMDCLDEISLSAPTKVCEYRDGEVKSYEITPEQFGFTRCKKEDLVGGEPAANAQIAREILDGVEGPKMDAVLLNAGAAIYIATDGITIEQGIEKAKEMITSGKA |
Sequence similarities
Belongs to the anthranilate phosphoribosyltransferase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length335
- Mass (Da)35,983
- Last updated2019-04-10 v1
- ChecksumD75AA59EB5B398F0