ID   HPRT_DICDI              Reviewed;         180 AA.
AC   Q54NJ8;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Hypoxanthine-guanine phosphoribosyltransferase;
DE            Short=HGPRT;
DE            Short=HGPRTase;
DE            EC=2.4.2.8;
GN   Name=hprT; ORFNames=DDB_G0285193;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [2]
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=6428268; DOI=10.1016/0003-2697(84)90118-0;
RA   Jahngen E.G., Rossomando E.F.;
RT   "Intermediary purine-metabolizing enzymes from the cytosol of Dictyostelium
RT   discoideum monitored by high-performance liquid chromatography.";
RL   Anal. Biochem. 137:493-504(1984).
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   -!- 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   -!- 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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=55.5 uM for hypoxanthine {ECO:0000269|PubMed:6428268};
CC         Vmax=34.3 nmol/min/mg enzyme {ECO:0000269|PubMed:6428268};
CC         Note=When guanine is used as the substrate, the rate of nucleotide
CC         formation is 50% that with hypoxanthine as the substrate.;
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway; IMP
CC       from hypoxanthine: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC       family. {ECO:0000305}.
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DR   EMBL; AAFI02000075; EAL64853.1; -; Genomic_DNA.
DR   RefSeq; XP_638364.1; XM_633272.1.
DR   AlphaFoldDB; Q54NJ8; -.
DR   SMR; Q54NJ8; -.
DR   STRING; 44689.DDB0216388; -.
DR   PaxDb; Q54NJ8; -.
DR   EnsemblProtists; EAL64853; EAL64853; DDB_G0285193.
DR   GeneID; 8624988; -.
DR   KEGG; ddi:DDB_G0285193; -.
DR   dictyBase; DDB_G0285193; hprT.
DR   eggNOG; KOG3367; Eukaryota.
DR   HOGENOM; CLU_073615_0_0_1; -.
DR   InParanoid; Q54NJ8; -.
DR   OMA; IEFMAVS; -.
DR   PhylomeDB; Q54NJ8; -.
DR   UniPathway; UPA00591; UER00648.
DR   PRO; PR:Q54NJ8; -.
DR   Proteomes; UP000002195; Chromosome 4.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0052657; F:guanine phosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004422; F:hypoxanthine phosphoribosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0032263; P:GMP salvage; IBA:GO_Central.
DR   GO; GO:0006178; P:guanine salvage; IBA:GO_Central.
DR   GO; GO:0046100; P:hypoxanthine metabolic process; IBA:GO_Central.
DR   GO; GO:0032264; P:IMP salvage; IBA:GO_Central.
DR   GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-KW.
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   1: Evidence at protein level;
KW   Cytoplasm; Glycosyltransferase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Purine salvage; Reference proteome; Transferase.
FT   CHAIN           1..180
FT                   /note="Hypoxanthine-guanine phosphoribosyltransferase"
FT                   /id="PRO_0000328334"
FT   ACT_SITE        103
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         40
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000250"
FT   BINDING         99..107
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000250"
FT   BINDING         131
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000250"
FT   BINDING         159
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000250"
FT   BINDING         159
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   180 AA;  20536 MW;  68D542EEEE7B6D2F CRC64;
     MSREVIFTEK EIKERVSELG RQITQDYKDS KNLVLVGILK GSFVFMSDLV RSIHLPNTNV
     SLEFMSISSY GAETSSSGVI RIMMDLRTSI EGKDVLIIED IVDSGLTLKH LMELLNHRNP
     NSLHTAVLLR KKEGLKVEVP VKYMGFDIPM VFIIGYGLDF AENYRELPYL GELKEECYKK