A2SLH5 · TRPD_METPP
- ProteinAnthranilate phosphoribosyltransferase
- GenetrpD
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids344 (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 | 83 | 5-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 83 | anthranilate 1 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 86-87 | 5-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI) | ||||
Sequence: GD | ||||||
Binding site | 91 | 5-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 93-96 | 5-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI) | ||||
Sequence: NIST | ||||||
Binding site | 95 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 111-119 | 5-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI) | ||||
Sequence: KHGGRSVSS | ||||||
Binding site | 123 | 5-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 169 | anthranilate 2 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 228 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 229 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 229 | Mg2+ 2 (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
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Sphaerotilaceae > Methylibium
Accessions
- Primary accessionA2SLH5
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000325434 | 1-344 | Anthranilate phosphoribosyltransferase | |||
Sequence: MITDTAALQRTIEHREIFHDEMLHLMRRIMSGEMSPVMIAALAVGLRVKKESIGEIAAAATVMREFATPVPVADTEHLVDLCGTGGDAAHTFNISTTAMFVAAAAGARVAKHGGRSVSSTSGSADVLEALGASIDLAPAQVAECLAESGIGFMFAPNHHPAMKHAGPVRKELGVRTIFNILGPLTNPAGAPNQLMGVFHPDLVGIQVRVLQRLGSRHVLVVYGMNGMDEISLSGETLIGELKDGEVREYTVHPSDFGLPVYDTRGLKVASKDESVGCIRRALADEAGPVRDIVLLNAGAALYAADVAPSIGEGVRQAREAVASGAAAKTLERFVATTRRLKGAA |
Interaction
Structure
Sequence
- Sequence statusComplete
- Length344
- Mass (Da)36,128
- Last updated2007-03-06 v1
- Checksum97CD552D30CF91A1
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000555 EMBL· GenBank· DDBJ | ABM96414.1 EMBL· GenBank· DDBJ | Genomic DNA |