ID HPRT_MUSSP Reviewed; 214 AA. AC Q64531; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 13-SEP-2023, entry version 104. DE RecName: Full=Hypoxanthine-guanine phosphoribosyltransferase; DE Short=HGPRT; DE Short=HGPRTase; DE Short=HPRT A; DE EC=2.4.2.8 {ECO:0000250|UniProtKB:P00492}; DE Flags: Fragment; GN Name=Hprt1; Synonyms=Hprt; OS Mus spretus (Western Mediterranean mouse) (Algerian mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10096; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. RC TISSUE=Brain; RX PubMed=3379061; DOI=10.1016/s0021-9258(19)76510-7; RA Johnson G.G., Kronert W.A., Bernstein S.I., Chapman V.M., Smith K.D.; RT "Altered turnover of allelic variants of hypoxanthine RT phosphoribosyltransferase is associated with N-terminal amino acid sequence RT variation."; RL J. Biol. Chem. 263:9079-9082(1988). 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 -!- 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; M20011; AAA96234.1; -; mRNA. DR PIR; I49758; I49758. DR AlphaFoldDB; Q64531; -. DR SMR; Q64531; -. DR MGI; MGI:96217; Hprt1. DR UniPathway; UPA00591; UER00648. 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 1: Evidence at protein level; KW Acetylation; Cytoplasm; Direct protein sequencing; Glycosyltransferase; KW Isopeptide bond; Magnesium; Metal-binding; Nucleotide-binding; KW Phosphoprotein; Purine salvage; Transferase; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT CHAIN 2..>214 FT /note="Hypoxanthine-guanine phosphoribosyltransferase" FT /id="PRO_0000139589" 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, ECO:0000305" 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 NON_TER 214 SQ SEQUENCE 214 AA; 24082 MW; 986078ACAF2688C3 CRC64; MATRSPSVVI SDDEPGYDLD LFCIPNHYVE DLEKVFIPHG LIMDRTERLA RDVMKEMGGH HIVALCVLKG GYKFFADLLD YIKALNRNSD RSIPMTVDFI RLKSYCNDQS TGDIKVIGGD DLSTLTGKNV LIVEDIIDTG KTMQTLLSLV KQYSPKMVKV ASLLVKRTSR SVGYRPDFVG FEIPDKFVVG YALDYNEYFR DLNHVCVISE TGKA //