A0A2S7IXU2 · A0A2S7IXU2_9HYPH
- ProteinXanthine-guanine phosphoribosyltransferase
- Genegpt
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids165 (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
- diphosphate + GMP = 5-phospho-alpha-D-ribose 1-diphosphate + guanine
- diphosphate + IMP = 5-phospho-alpha-D-ribose 1-diphosphate + hypoxanthine
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 | 41-42 | 5-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI) | ||||
Sequence: RG | ||||||
Binding site | 98-106 | 5-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI) | ||||
Sequence: DDLTDTGKT | ||||||
Binding site | 99 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 102 | guanine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 102 | xanthine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 102-106 | GMP (UniProtKB | ChEBI) | ||||
Sequence: DTGKT | ||||||
Binding site | 144-145 | GMP (UniProtKB | ChEBI) | ||||
Sequence: WI | ||||||
Binding site | 145 | guanine (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 145 | xanthine (UniProtKB | ChEBI) | ||||
Sequence: I |
GO annotations
Aspect | Term | |
---|---|---|
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 | 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
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Brucellaceae > Brucella/Ochrobactrum group > Brucella
Accessions
- Primary accessionA0A2S7IXU2
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Peripheral membrane protein
Keywords
- Cellular component
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 11-154 | Phosphoribosyltransferase | ||||
Sequence: SWDQFHRDARALAWRISGMGREWHAIVAITRGGLVPAAIVCRELGIRLIETVCIASYHDYTSQGEMQVLKGVSETLLDNGGEGVIVVDDLTDTGKTAAIVREMMPKAHFATVYAKPKGRPLIDTFVTEVSQDTWIYFPWDMGFT |
Sequence similarities
Belongs to the purine/pyrimidine phosphoribosyltransferase family. XGPT subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length165
- Mass (Da)18,346
- Last updated2018-07-18 v1
- Checksum5580356A779A5D7F