HPRT_PIG
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 03-AUG-2022, entry version 91.
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.ENSSSCP00000025410; -.
DR PaxDb; Q45FY6; -.
DR PeptideAtlas; Q45FY6; -.
DR PRIDE; Q45FY6; -.
DR Ensembl; ENSSSCT00000051852; ENSSSCP00000044832; ENSSSCG00000034896.
DR Ensembl; ENSSSCT00025061056; ENSSSCP00025025924; ENSSSCG00025044949.
DR Ensembl; ENSSSCT00030047570; ENSSSCP00030021430; ENSSSCG00030034364.
DR Ensembl; ENSSSCT00035006457; ENSSSCP00035002255; ENSSSCG00035005142.
DR Ensembl; ENSSSCT00040034674; ENSSSCP00040014343; ENSSSCG00040025932.
DR Ensembl; ENSSSCT00045052993; ENSSSCP00045036866; ENSSSCG00045031043.
DR Ensembl; ENSSSCT00050037335; ENSSSCP00050015522; ENSSSCG00050027741.
DR Ensembl; ENSSSCT00055013340; ENSSSCP00055010490; ENSSSCG00055006870.
DR Ensembl; ENSSSCT00060077778; ENSSSCP00060033612; ENSSSCG00060057082.
DR Ensembl; ENSSSCT00065066896; ENSSSCP00065029032; ENSSSCG00065048888.
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; TMDWMAV; -.
DR OrthoDB; 1537610at2759; -.
DR UniPathway; UPA00591; UER00648.
DR Proteomes; UP000008227; Chromosome X.
DR Proteomes; UP000314985; Unplaced.
DR Bgee; ENSSSCG00000034896; Expressed in Ammon's horn and 44 other 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 Pfam; PF00156; Pribosyltran; 1.
DR SUPFAM; SSF53271; SSF53271; 1.
DR TIGRFAMs; TIGR01203; HGPRTase; 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
