ID HPRT_CRIGR Reviewed; 218 AA. AC P00494; Q80XX0; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 117. DE RecName: Full=Hypoxanthine-guanine phosphoribosyltransferase; DE Short=HGPRT; DE Short=HGPRTase; DE EC=2.4.2.8 {ECO:0000250|UniProtKB:P00492}; GN Name=HPRT1; Synonyms=HPRT; OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; OC Cricetidae; Cricetinae; Cricetulus. OX NCBI_TaxID=10029; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=6294614; DOI=10.1093/nar/10.21.6763; RA Konecki D.S., Brennand J., Fuscoe J.C., Caskey C.T., Chinault A.C.; RT "Hypoxanthine-guanine phosphoribosyltransferase genes of mouse and Chinese RT hamster: construction and sequence analysis of cDNA recombinants."; RL Nucleic Acids Res. 10:6763-6775(1982). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2004774; DOI=10.1016/0888-7543(91)90249-e; RA Rossiter B.J.F., Fuscoe J.C., Muzny D.M., Fox M., Caskey C.T.; RT "The Chinese hamster HPRT gene: restriction map, sequence analysis, and RT multiplex PCR deletion screen."; RL Genomics 9:247-256(1991). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 32-42. RX PubMed=1383700; DOI=10.1016/0027-5107(92)90198-b; RA Fuscoe J.C., Zimmerman L.J., Fekete A., Setzer R.W., Rossiter B.J.; RT "Analysis of X-ray-induced HPRT mutations in CHO cells: insertion and RT deletions."; RL Mutat. Res. 269:171-183(1992). CC -!- FUNCTION: Converts guanine to guanosine monophosphate, and hypoxanthine CC to inosine monophosphate. Transfers the 5-phosphoribosyl group from 5- CC phosphoribosylpyrophosphate onto the purine. Plays a central role in CC the generation of purine nucleotides through the purine salvage pathway CC (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=diphosphate + IMP = 5-phospho-alpha-D-ribose 1-diphosphate + CC hypoxanthine; Xref=Rhea:RHEA:17973, ChEBI:CHEBI:17368, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58053; EC=2.4.2.8; CC Evidence={ECO:0000250|UniProtKB:P00492}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17975; CC Evidence={ECO:0000250|UniProtKB:P00492}; CC -!- CATALYTIC ACTIVITY: CC Reaction=diphosphate + GMP = 5-phospho-alpha-D-ribose 1-diphosphate + CC guanine; Xref=Rhea:RHEA:25424, ChEBI:CHEBI:16235, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:58017, ChEBI:CHEBI:58115; EC=2.4.2.8; CC Evidence={ECO:0000250|UniProtKB:P00492}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:25426; CC Evidence={ECO:0000250|UniProtKB:P00492}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Note=Binds 2 magnesium ions per subunit. The magnesium ions are CC essentially bound to the substrate and have few direct interactions CC with the protein. {ECO:0000250}; CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway; IMP CC from hypoxanthine: step 1/1. CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- MISCELLANEOUS: The cell lines from which this sequence was cloned are CC revertants from mutants with no detectable enzyme activity. The CC phenotypic reversions are the result of overproduction of variant CC enzymes because of gene amplification. This variant sequence is CC expected to be very similar to the wild-type. CC -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase CC family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; J00060; AAA36990.1; -; mRNA. DR EMBL; X53073; CAA37247.1; -; Genomic_DNA. DR EMBL; X53074; CAA37247.1; JOINED; Genomic_DNA. DR EMBL; X53075; CAA37247.1; JOINED; Genomic_DNA. DR EMBL; X53076; CAA37247.1; JOINED; Genomic_DNA. DR EMBL; X53077; CAA37247.1; JOINED; Genomic_DNA. DR EMBL; X53078; CAA37247.1; JOINED; Genomic_DNA. DR EMBL; X53079; CAA37247.1; JOINED; Genomic_DNA. DR EMBL; X53080; CAA37247.1; JOINED; Genomic_DNA. DR EMBL; S46270; AAP13884.1; -; Genomic_DNA. DR PIR; S14402; RTHYG. DR AlphaFoldDB; P00494; -. DR SMR; P00494; -. DR PaxDb; 10029-XP_007621351-1; -. DR eggNOG; KOG3367; Eukaryota. DR UniPathway; UPA00591; UER00648. DR Proteomes; UP000694386; Unplaced. DR Proteomes; UP001108280; Genome assembly. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0052657; F:guanine phosphoribosyltransferase activity; ISS:UniProtKB. DR GO; GO:0004422; F:hypoxanthine phosphoribosyltransferase activity; ISS:UniProtKB. DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB. DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0046038; P:GMP catabolic process; ISS:UniProtKB. DR GO; GO:0006178; P:guanine salvage; ISS:UniProtKB. DR GO; GO:0046100; P:hypoxanthine metabolic process; ISS:UniProtKB. DR GO; GO:0043103; P:hypoxanthine salvage; ISS:UniProtKB. DR GO; GO:0046040; P:IMP metabolic process; ISS:UniProtKB. DR GO; GO:0032264; P:IMP salvage; IEA:UniProtKB-UniPathway. DR GO; GO:0045964; P:positive regulation of dopamine metabolic process; ISS:UniProtKB. DR GO; GO:0006164; P:purine nucleotide biosynthetic process; ISS:UniProtKB. DR GO; GO:0006166; P:purine ribonucleoside salvage; ISS:UniProtKB. DR CDD; cd06223; PRTases_typeI; 1. DR Gene3D; 3.40.50.2020; -; 1. DR InterPro; IPR005904; Hxn_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR NCBIfam; TIGR01203; HGPRTase; 1. DR PANTHER; PTHR43340; HYPOXANTHINE-GUANINE PHOSPHORIBOSYLTRANSFERASE; 1. DR PANTHER; PTHR43340:SF6; HYPOXANTHINE-GUANINE PHOSPHORIBOSYLTRANSFERASE; 1. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; PRTase-like; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 2: Evidence at transcript level; KW Acetylation; Cytoplasm; Glycosyltransferase; Isopeptide bond; Magnesium; KW Metal-binding; Nucleotide-binding; Phosphoprotein; Purine salvage; KW Transferase; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P00492" FT CHAIN 2..218 FT /note="Hypoxanthine-guanine phosphoribosyltransferase" FT /id="PRO_0000139584" FT ACT_SITE 138 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT BINDING 69 FT /ligand="GMP" FT /ligand_id="ChEBI:CHEBI:58115" FT /evidence="ECO:0000250" FT BINDING 134..142 FT /ligand="GMP" FT /ligand_id="ChEBI:CHEBI:58115" FT /evidence="ECO:0000250" FT BINDING 166 FT /ligand="GMP" FT /ligand_id="ChEBI:CHEBI:58115" FT /evidence="ECO:0000250" FT BINDING 186..188 FT /ligand="GMP" FT /ligand_id="ChEBI:CHEBI:58115" FT /evidence="ECO:0000250" FT BINDING 194 FT /ligand="GMP" FT /ligand_id="ChEBI:CHEBI:58115" FT /evidence="ECO:0000250" FT BINDING 194 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000250|UniProtKB:P00492" FT MOD_RES 103 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P00493" FT MOD_RES 142 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P27605" FT CROSSLNK 115 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0000250|UniProtKB:P00492" FT CROSSLNK 115 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P00492" FT CONFLICT 32 FT /note="L -> M (in Ref. 3; AAP13884)" FT /evidence="ECO:0000305" SQ SEQUENCE 218 AA; 24644 MW; 21DA6A26D92B7511 CRC64; MATRSPSVVI SDDEPGYDLD LFCIPNHYVE DLEKVFIPHG VIMDRTERLA RDVMKEMGGH HIVALCVLKG GYKFFADLLD YIKALNRNSD RSIPMTVDFI RLKSYCNDQS TGDIKVIGGD DLSTLTGKNV LIVEDIIDTG KTMQTLLSLV KRYNLKMVKV ASLLVKRTSR SVGYRPDFVG FEIPDKFVVG YALDYNEYFR DLNHICVISE TGKAKYKA //