B5FJW9 · XGPT_SALDC
- ProteinXanthine-guanine phosphoribosyltransferase
- Genegpt
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids152 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Purine salvage pathway enzyme that catalyzes the transfer of the ribosyl-5-phosphate group from 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to the N9 position of the 6-oxopurines guanine and xanthine to form the corresponding ribonucleotides GMP (guanosine 5'-monophosphate) and XMP (xanthosine 5'-monophosphate), with the release of PPi. To a lesser extent, also acts on hypoxanthine.
Catalytic activity
- GMP + diphosphate = guanine + 5-phospho-alpha-D-ribose 1-diphosphateThis reaction proceeds in the backward direction.
- IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphateThis reaction proceeds in the backward direction.
Cofactor
Pathway
Purine metabolism; GMP biosynthesis via salvage pathway; GMP from guanine: step 1/1.
Purine metabolism; XMP biosynthesis via salvage pathway; XMP from xanthine: step 1/1.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 37-38 | 5-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI) | ||||
Sequence: RG | ||||||
Binding site | 69 | 5-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 69 | GMP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 88-96 | 5-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI) | ||||
Sequence: DDLVDTGGT | ||||||
Binding site | 89 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 92 | guanine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 92 | xanthine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 92-96 | GMP (UniProtKB | ChEBI) | ||||
Sequence: DTGGT | ||||||
Binding site | 134-135 | GMP (UniProtKB | ChEBI) | ||||
Sequence: WI | ||||||
Binding site | 135 | guanine (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 135 | xanthine (UniProtKB | ChEBI) | ||||
Sequence: I |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | plasma membrane | |
Molecular Function | guanine phosphoribosyltransferase activity | |
Molecular Function | hypoxanthine phosphoribosyltransferase activity | |
Molecular Function | magnesium ion binding | |
Molecular Function | xanthine phosphoribosyltransferase activity | |
Biological Process | GMP salvage | |
Biological Process | IMP salvage | |
Biological Process | purine ribonucleoside salvage | |
Biological Process | XMP salvage |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameXanthine-guanine phosphoribosyltransferase
- EC number
- Short namesXGPRT
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Salmonella
Accessions
- Primary accessionB5FJW9
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell inner membrane ; Peripheral membrane protein
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000188753 | 1-152 | Xanthine-guanine phosphoribosyltransferase | |||
Sequence: MSEKYVVTWDMLQIHARKLASRLMPSEQWKGIIAVSRGGLVPGALLARELGIRHVDTVCISSYDHDNQRELKVLKRAEGDGEGFIVIDDLVDTGGTAVAIREMYPKAHFVTIFAKPAGRPLVDDYVIDIPQNTWIEQPWDMGVVFVPPISGR |
Interaction
Subunit
Homotetramer.
Structure
Sequence
- Sequence statusComplete
- Length152
- Mass (Da)16,970
- Last updated2008-10-14 v1
- ChecksumEE42974303E6900D
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP001144 EMBL· GenBank· DDBJ | ACH77185.1 EMBL· GenBank· DDBJ | Genomic DNA |