ID   HPRT_PIG                Reviewed;         218 AA.
AC   Q45FY6; A0SNU9;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 99.
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   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Carlson D.F., Clark K.J., Shiroma D.S., Fahrenkrug S.C.;
RT   "Gene targeting and chromosome engineering in porcine cells.";
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Nygaard A.-B., Joergensen C.B., Cirera S., Fredholm M.;
RT   "Selection of reference genes for gene expression studies in pig tissues
RT   using SYBR green qPCR.";
RL   Submitted (JUL-2006) 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}.
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DR   EMBL; DQ136030; AAZ43258.1; -; mRNA.
DR   EMBL; DQ845175; ABI29189.1; -; mRNA.
DR   RefSeq; NP_001027548.1; NM_001032376.2.
DR   AlphaFoldDB; Q45FY6; -.
DR   SMR; Q45FY6; -.
DR   IntAct; Q45FY6; 2.
DR   STRING; 9823.ENSSSCP00000041929; -.
DR   PaxDb; 9823-ENSSSCP00000025410; -.
DR   PeptideAtlas; Q45FY6; -.
DR   Ensembl; ENSSSCT00000051852.3; ENSSSCP00000044832.1; ENSSSCG00000034896.3.
DR   Ensembl; ENSSSCT00025061056.1; ENSSSCP00025025924.1; ENSSSCG00025044949.1.
DR   Ensembl; ENSSSCT00030047570.1; ENSSSCP00030021430.1; ENSSSCG00030034364.1.
DR   Ensembl; ENSSSCT00035006457.1; ENSSSCP00035002255.1; ENSSSCG00035005142.1.
DR   Ensembl; ENSSSCT00040034674.1; ENSSSCP00040014343.1; ENSSSCG00040025932.1.
DR   Ensembl; ENSSSCT00045052993.1; ENSSSCP00045036866.1; ENSSSCG00045031043.1.
DR   Ensembl; ENSSSCT00050037335.1; ENSSSCP00050015522.1; ENSSSCG00050027741.1.
DR   Ensembl; ENSSSCT00055013340.1; ENSSSCP00055010490.1; ENSSSCG00055006870.1.
DR   Ensembl; ENSSSCT00060077778.1; ENSSSCP00060033612.1; ENSSSCG00060057082.1.
DR   Ensembl; ENSSSCT00065066896.1; ENSSSCP00065029032.1; ENSSSCG00065048888.1.
DR   GeneID; 397351; -.
DR   KEGG; ssc:397351; -.
DR   CTD; 3251; -.
DR   VGNC; VGNC:109457; HPRT1.
DR   eggNOG; KOG3367; Eukaryota.
DR   GeneTree; ENSGT00940000155028; -.
DR   InParanoid; Q45FY6; -.
DR   OMA; MQWRVAP; -.
DR   OrthoDB; 4216383at2759; -.
DR   Reactome; R-SSC-74217; Purine salvage.
DR   Reactome; R-SSC-9748787; Azathioprine ADME.
DR   UniPathway; UPA00591; UER00648.
DR   Proteomes; UP000008227; Chromosome X.
DR   Proteomes; UP000314985; Unplaced.
DR   Proteomes; UP000694570; Unplaced.
DR   Proteomes; UP000694571; Unplaced.
DR   Proteomes; UP000694720; Unplaced.
DR   Proteomes; UP000694722; Unplaced.
DR   Proteomes; UP000694723; Unplaced.
DR   Proteomes; UP000694724; Unplaced.
DR   Proteomes; UP000694725; Unplaced.
DR   Proteomes; UP000694726; Unplaced.
DR   Proteomes; UP000694727; Unplaced.
DR   Proteomes; UP000694728; Unplaced.
DR   Bgee; ENSSSCG00000034896; Expressed in Ammon's horn and 44 other cell types or tissues.
DR   ExpressionAtlas; Q45FY6; 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_0000139590"
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;  24555 MW;  920FCBB948B2CFA4 CRC64;
     MATRSPSVVI SDDEPGYDLD LFCIPNHYAE DLEKVFIPHG LIMDRTERLA RDVMKEMGGH
     HIVALCVLKG GYKFFADLLD YIKALNRNSD RSIPMTVDFI RLKSYCNDQS TGDIKVIGGD
     DLSTLTGKNV LIVEDIIDTG KTMQTLLSLV KQHNPKMVKV ASLLVKRTPR SVGYRPDFVG
     FEIPDKFVVG YALDYNEYFR DLNHVCVISE TGKAKYKA
//