HPRT_CRIGR
ID HPRT_CRIGR Reviewed; 218 AA.
AC P00494; Q80XX0;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 110.
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 Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6294614; DOI=10.1093/nar/10.21.6763;
RA Konecki D.S., Brennand J., Fuscoe J.C., Caskey C.T., Chinault A.C.;
RT "Hypoxanthine-guanine phosphoribosyltransferase genes of mouse and Chinese
RT hamster: construction and sequence analysis of cDNA recombinants.";
RL Nucleic Acids Res. 10:6763-6775(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2004774; DOI=10.1016/0888-7543(91)90249-e;
RA Rossiter B.J.F., Fuscoe J.C., Muzny D.M., Fox M., Caskey C.T.;
RT "The Chinese hamster HPRT gene: restriction map, sequence analysis, and
RT multiplex PCR deletion screen.";
RL Genomics 9:247-256(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 32-42.
RX PubMed=1383700; DOI=10.1016/0027-5107(92)90198-b;
RA Fuscoe J.C., Zimmerman L.J., Fekete A., Setzer R.W., Rossiter B.J.;
RT "Analysis of X-ray-induced HPRT mutations in CHO cells: insertion and
RT deletions.";
RL Mutat. Res. 269:171-183(1992).
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 -!- MISCELLANEOUS: The cell lines from which this sequence was cloned are
CC revertants from mutants with no detectable enzyme activity. The
CC phenotypic reversions are the result of overproduction of variant
CC enzymes because of gene amplification. This variant sequence is
CC expected to be very similar to the wild-type.
CC -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC family. {ECO:0000305}.
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DR EMBL; J00060; AAA36990.1; -; mRNA.
DR EMBL; X53073; CAA37247.1; -; Genomic_DNA.
DR EMBL; X53074; CAA37247.1; JOINED; Genomic_DNA.
DR EMBL; X53075; CAA37247.1; JOINED; Genomic_DNA.
DR EMBL; X53076; CAA37247.1; JOINED; Genomic_DNA.
DR EMBL; X53077; CAA37247.1; JOINED; Genomic_DNA.
DR EMBL; X53078; CAA37247.1; JOINED; Genomic_DNA.
DR EMBL; X53079; CAA37247.1; JOINED; Genomic_DNA.
DR EMBL; X53080; CAA37247.1; JOINED; Genomic_DNA.
DR EMBL; S46270; AAP13884.1; -; Genomic_DNA.
DR PIR; S14402; RTHYG.
DR AlphaFoldDB; P00494; -.
DR SMR; P00494; -.
DR STRING; 10029.XP_007621351.1; -.
DR eggNOG; KOG3367; Eukaryota.
DR UniPathway; UPA00591; UER00648.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
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: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; IEA:UniProtKB-UniPathway.
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 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_0000139584"
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"
FT CONFLICT 32
FT /note="L -> M (in Ref. 3; AAP13884)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 218 AA; 24644 MW; 21DA6A26D92B7511 CRC64;
MATRSPSVVI SDDEPGYDLD LFCIPNHYVE DLEKVFIPHG VIMDRTERLA RDVMKEMGGH
HIVALCVLKG GYKFFADLLD YIKALNRNSD RSIPMTVDFI RLKSYCNDQS TGDIKVIGGD
DLSTLTGKNV LIVEDIIDTG KTMQTLLSLV KRYNLKMVKV ASLLVKRTSR SVGYRPDFVG
FEIPDKFVVG YALDYNEYFR DLNHICVISE TGKAKYKA
