PRPS2
entrez
5634
canonical
uniprot
P11908
canonical
ensembl
ENSG00000101911
resolver
ensp
ENSP00000370043
resolver
ensp
ENSP00000381504
resolver
genesymbol
PRPS2
resolver
hgnc
HGNC:9465
resolver
uniprot
A0A140VK41
resolver
uniprot
Q0VDH9
resolver
uniprot
Q0VDI0
resolver
uniprot
Q15245
resolver
uniprot
Q2TAK7
resolver
uniprot_entry
A0A140VK41_HUMAN
resolver
uniprot_entry
PRPS2_HUMAN
resolver
uniprot_sec
Q0VDH9
resolver
uniprot_sec
Q0VDI0
resolver
uniprot_sec
Q15245
resolver
uniprot_sec
Q2TAK7
resolver
activity_regulation
ACTIVITY REGULATION: Activated by magnesium (PubMed:8387514). Activated by inorganic phosphate (Pi) that binds D-ribose 5-phosphate binding site (PubMed:37248548, PubMed:8387514). Inhibited by GDP (PubMed:8387514). Feedback inhibition by purine nucleotides is less sensitive than inhibition by 2,3-diphosphoglycerate (PubMed:8387514). ADP can regulate enzyme activity through competitive inhibition and allosteric inhibition by affecting the conformation of regulatory flexible (RF) loop (PubMed:37248548). The ADP of allosteric site can interact with RF loop, leading to the regulation of ATP conformation in active site (PubMed:37248548). Competitive inhibition of ADP by binding to the ATP active site in the hexamer where also binds magnesium (PubMed:37248548). Thermal inactivation at 55 degrees Celsius (PubMed:8387514). {ECO:0000269|PubMed:37248548, ECO:0000269|PubMed:8387514}.
uniprot
proteins
amino_acid_sequence
MPNIVLFSGSSHQDLSQRVADRLGLELGKVVTKKFSNQETSVEIGESVRGEDVYIIQSGCGEINDNLMELLIMINACKIASSSRVTAVIPCFPYARQDKKDKSRAPISAKLVANMLSVAGADHIITMDLHASQIQGFFDIPVDNLYAEPAVLQWIRENIAEWKNCIIVSPDAGGAKRVTSIADRLNVEFALIHKERKKANEVDRMVLVGDVKDRVAILVDDMADTCGTICHAADKLLSAGATKVYAILTHGIFSGPAISRINNAAFEAVVVTNTIPQEDKMKHCTKIQVIDISMILAEAIRRTHNGESVSYLFSHVPL
uniprot
proteins
ec_number
2.7.6.1
uniprot
proteins
function
FUNCTION: Catalyzes the transfer of the pyrophosphoryl group from ATP to the 1-hydroxyl of ribose-5-phosphate to form 5-phospho-ribosyl-1-pyrophosphate (PRPP), a key intermediate in the biosynthesis of several metabolites including nucleotides, dinucleotides and some amino acids (PubMed:37248548, PubMed:40295500, PubMed:8387514). Involved in the production of newly synthesized ATP/GTP through the purine biosynthesis pathway (PubMed:40295500). {ECO:0000269|PubMed:37248548, ECO:0000269|PubMed:40295500, ECO:0000269|PubMed:8387514}.
uniprot
proteins
mass_dalton
34769
uniprot
proteins
mutagenesis
MUTAGEN 99; /note="K->A: Loss of 5-phosphate ribose-1-pyrophosphate (PRPP) synthase activity's inhibition by ADP. Decreases 5-phosphate ribose-1-pyrophosphate (PRPP) synthase activity."; /evidence="ECO:0000269|PubMed:37248548"; MUTAGEN 301; /note="R->A: Loss of its filament-forming ability. Loss of 5-phosphate ribose-1-pyrophosphate (PRPP) synthase activity."; /evidence="ECO:0000269|PubMed:37248548"; MUTAGEN 302; /note="R->A: Loss of its filament-forming ability. Loss of 5-phosphate ribose-1-pyrophosphate (PRPP) synthase activity."; /evidence="ECO:0000269|PubMed:37248548
uniprot
proteins
pathway_participation
PATHWAY: Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route I): step 1/1. {ECO:0000269|PubMed:37248548, ECO:0000269|PubMed:40295500, ECO:0000269|PubMed:8387514}.
uniprot
proteins
protein_family
Ribose-phosphate pyrophosphokinase family
uniprot
proteins
pubmed
1314091
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
2538352
uniprot
proteins
pubmed
2560337
uniprot
proteins
pubmed
37248548
uniprot
proteins
pubmed
40295500
uniprot
proteins
pubmed
8387514
uniprot
proteins
sequence_length
318
uniprot
proteins