ID HPRT_BOVIN Reviewed; 218 AA. AC Q3SZ18; DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 119. 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; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Hereford; TISSUE=Fetal liver; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. 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 {ECO:0000250}. 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; BC103248; AAI03249.1; -; mRNA. DR RefSeq; NP_001029207.1; NM_001034035.2. DR AlphaFoldDB; Q3SZ18; -. DR SMR; Q3SZ18; -. DR STRING; 9913.ENSBTAP00000019547; -. DR PaxDb; 9913-ENSBTAP00000019547; -. DR PeptideAtlas; Q3SZ18; -. DR Ensembl; ENSBTAT00000019547.5; ENSBTAP00000019547.4; ENSBTAG00000014685.6. DR GeneID; 281229; -. DR KEGG; bta:281229; -. DR CTD; 3251; -. DR VEuPathDB; HostDB:ENSBTAG00000014685; -. DR eggNOG; KOG3367; Eukaryota. DR GeneTree; ENSGT00940000155028; -. DR HOGENOM; CLU_073615_3_0_1; -. DR InParanoid; Q3SZ18; -. DR OMA; MQWRVAP; -. DR OrthoDB; 4216383at2759; -. DR TreeFam; TF313367; -. DR Reactome; R-BTA-74217; Purine salvage. DR Reactome; R-BTA-9748787; Azathioprine ADME. DR UniPathway; UPA00591; UER00648. DR Proteomes; UP000009136; Chromosome X. DR Bgee; ENSBTAG00000014685; Expressed in caput epididymis and 103 other cell types or tissues. DR ExpressionAtlas; Q3SZ18; baseline and differential. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. 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:0032263; P:GMP salvage; IBA:GO_Central. 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; IBA:GO_Central. 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 Reference proteome; 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_0000257812" 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" SQ SEQUENCE 218 AA; 24498 MW; 761695098A5B6A20 CRC64; MAARSPSVVI SDDEPGYDLN LFCIPNHYAE DLEKVFIPHG LIMDRTERLA RDVMKEMGGH HIVALCVLKG GYKFFADLLD YIKALNRNSD KSIPMTVDFI RLKSYCNDQS TGDIKVIGGD DLSTLTGKNV LIVEDIIDTG KTMQTLLALV KKHKPKMVKV ASLLMKRTPR SVGYKPDFVG FEIPDKFVVG YALDYNEYFR DLNHVCVISE TGKAKYKA //