ID HPRT_CHICK Reviewed; 218 AA. AC Q9W719; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 27-MAR-2024, entry version 127. 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 Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae; OC Phasianinae; Gallus. OX NCBI_TaxID=9031; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=10198428; DOI=10.1093/nar/27.9.1966; RA Fukagawa T., Hayward N., Yang J., Azzalin C., Griffin D., Stewart A.F., RA Brown W.; RT "The chicken HPRT gene: a counter selectable marker for the DT40 cell RT line."; RL Nucleic Acids Res. 27:1966-1969(1999). 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; AJ132697; CAB46657.1; -; mRNA. DR RefSeq; NP_990179.1; NM_204848.1. DR AlphaFoldDB; Q9W719; -. DR SMR; Q9W719; -. DR STRING; 9031.ENSGALP00000009829; -. DR PaxDb; 9031-ENSGALP00000009829; -. DR Ensembl; ENSGALT00010037920.1; ENSGALP00010021882.1; ENSGALG00010015742.1. DR Ensembl; ENSGALT00015032793; ENSGALP00015019090; ENSGALG00015013511. DR GeneID; 395653; -. DR KEGG; gga:395653; -. DR CTD; 3251; -. DR VEuPathDB; HostDB:geneid_395653; -. DR eggNOG; KOG3367; Eukaryota. DR GeneTree; ENSGT00940000155028; -. DR InParanoid; Q9W719; -. DR OMA; MQWRVAP; -. DR OrthoDB; 4216383at2759; -. DR PhylomeDB; Q9W719; -. DR UniPathway; UPA00591; UER00648. DR PRO; PR:Q9W719; -. DR Proteomes; UP000000539; Chromosome 4. DR GO; GO:0005694; C:chromosome; IDA:AgBase. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0002057; F:guanine binding; IDA:AgBase. DR GO; GO:0052657; F:guanine phosphoribosyltransferase activity; ISS:UniProtKB. DR GO; GO:0004422; F:hypoxanthine phosphoribosyltransferase activity; IDA:AgBase. 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:0002060; F:purine nucleobase binding; IDA:AgBase. 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 Cytoplasm; Glycosyltransferase; Magnesium; Metal-binding; KW Nucleotide-binding; Purine salvage; Reference proteome; Transferase. FT CHAIN 1..218 FT /note="Hypoxanthine-guanine phosphoribosyltransferase" FT /id="PRO_0000139592" 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" SQ SEQUENCE 218 AA; 24609 MW; 2228B84B0B6AF727 CRC64; MATHSPCIVI GDDEQGYDLD LFCIPKHYAD DLEKVYIPHG LIMDRTERLA REIMKGMGGH HIVALCVLKG GYKFFADLLD YIKALNRNSD KSIPMTVDFI RLKSYCNDQS TGDIKVIGGD DLSTLTGKNV LIVEDIIDTG KTMKTLLSLL KQYNPKMVKV ASLLVKRTPR SVGYRPDFVG FEVPDKFVVG YALDYNEYFR DLNHICVISE TGKQKYKA //