ID   HPRT_LEIDO              Reviewed;         211 AA.
AC   P43152;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   27-MAR-2024, entry version 97.
DE   RecName: Full=Hypoxanthine-guanine phosphoribosyltransferase;
DE            Short=HGPRT;
DE            Short=HGPRTase;
DE            EC=2.4.2.8;
OS   Leishmania donovani.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=5661;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MHOM/SD/62/1S;
RX   PubMed=8577321; DOI=10.1016/0166-6851(94)00105-v;
RA   Allen T.E., Hwang H.Y., Jardim A., Olafson R., Ullman B.;
RT   "Cloning and expression of the hypoxanthine-guanine
RT   phosphoribosyltransferase from Leishmania donovani.";
RL   Mol. Biochem. Parasitol. 73:133-143(1995).
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   -!- PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway; IMP
CC       from hypoxanthine: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC       family. {ECO:0000305}.
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DR   EMBL; L25412; AAB00074.1; -; Genomic_DNA.
DR   RefSeq; XP_003860615.1; XM_003860567.1.
DR   AlphaFoldDB; P43152; -.
DR   SMR; P43152; -.
DR   GeneID; 13386422; -.
DR   KEGG; ldo:LDBPK_210980; -.
DR   VEuPathDB; TriTrypDB:LdBPK_210980.1; -.
DR   VEuPathDB; TriTrypDB:LdCL_210014800; -.
DR   VEuPathDB; TriTrypDB:LDHU3_21.1150; -.
DR   OMA; VIFMEDI; -.
DR   OrthoDB; 4216383at2759; -.
DR   UniPathway; UPA00591; UER00648.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0052657; F:guanine phosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004422; F:hypoxanthine phosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0032264; P:IMP salvage; IEA:UniProtKB-UniPathway.
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   NCBIfam; TIGR01203; HGPRTase; 1.
DR   PANTHER; PTHR43340:SF1; HYPOXANTHINE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR43340; HYPOXANTHINE-GUANINE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   SUPFAM; SSF53271; PRTase-like; 1.
DR   PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Glycosyltransferase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Purine salvage; Transferase.
FT   CHAIN           1..211
FT                   /note="Hypoxanthine-guanine phosphoribosyltransferase"
FT                   /id="PRO_0000139593"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        129
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         66
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000250"
FT   BINDING         125..133
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000250"
FT   BINDING         157
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000250"
FT   BINDING         185
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000250"
FT   BINDING         185
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   211 AA;  23612 MW;  7802A85B00CA2190 CRC64;
     MSNSAKSPSG PVGDEGRRNY PMSAHTLVTQ EQVWAATAKC AKKIAEDYRS FKLTTDNPLY
     LLCVLKGSFI FTADLARFLA DEGVPVKVEF ICASSYGTGV ETSGQVRMLL DVRDSVENRH
     ILIVEDIVDS AITLQYLMRF MLAKKPASLK TVVLLDKPSG RKVEVLVDYP VITIPHAFVI
     GYGMDYAESY RELRDICVLK KEYYEKPESK V
//