HGXR_PLAFK
ID HGXR_PLAFK Reviewed; 231 AA.
AC P07833;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Hypoxanthine-guanine-xanthine phosphoribosyltransferase;
DE Short=HGPRT;
DE Short=HGXPRT;
DE Short=HGXPRTase;
DE EC=2.4.2.22 {ECO:0000250|UniProtKB:Q26997};
DE EC=2.4.2.8 {ECO:0000250|UniProtKB:Q26997};
GN Name=LACZ;
OS Plasmodium falciparum (isolate K1 / Thailand).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=5839;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3320967; DOI=10.1093/nar/15.24.10469;
RA King A., Melton D.W.;
RT "Characterisation of cDNA clones for hypoxanthine-guanine
RT phosphoribosyltransferase from the human malarial parasite, Plasmodium
RT falciparum: comparisons to the mammalian gene and protein.";
RL Nucleic Acids Res. 15:10469-10481(1987).
CC -!- FUNCTION: Catalyzes the transfer of a ribosyl phosphate group from 5-
CC phosphoribose 1-diphosphate to the N(9) of hypoxanthine, guanine or
CC xanthine, leading to IMP, GMP and XMP, respectively. Plays a central
CC role in the generation of purine nucleotides through the purine salvage
CC pathway. {ECO:0000250|UniProtKB:Q26997}.
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:Q26997};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17975;
CC Evidence={ECO:0000250|UniProtKB:Q26997};
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:Q26997};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:25426;
CC Evidence={ECO:0000250|UniProtKB:Q26997};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diphosphate + XMP = 5-phospho-alpha-D-ribose 1-diphosphate +
CC xanthine; Xref=Rhea:RHEA:10800, ChEBI:CHEBI:17712, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57464, ChEBI:CHEBI:58017; EC=2.4.2.22;
CC Evidence={ECO:0000250|UniProtKB:Q26997};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10802;
CC Evidence={ECO:0000250|UniProtKB:Q26997};
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; GMP biosynthesis via salvage pathway; GMP
CC from guanine: step 1/1.
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway; IMP
CC from hypoxanthine: step 1/1.
CC -!- PATHWAY: Purine metabolism; XMP biosynthesis via salvage pathway; XMP
CC from xanthine: step 1/1.
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC family. {ECO:0000305}.
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DR EMBL; Y00519; CAA68573.1; -; mRNA.
DR PIR; S06315; S06315.
DR AlphaFoldDB; P07833; -.
DR SMR; P07833; -.
DR PRIDE; P07833; -.
DR UniPathway; UPA00591; UER00648.
DR UniPathway; UPA00602; UER00658.
DR UniPathway; UPA00909; UER00887.
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:0000310; F:xanthine phosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0032263; P:GMP salvage; IEA:UniProtKB-UniPathway.
DR GO; GO:0032264; P:IMP salvage; IEA:UniProtKB-UniPathway.
DR GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-KW.
DR GO; GO:0032265; P:XMP salvage; IEA:UniProtKB-UniPathway.
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 Cytoplasm; Glycosyltransferase; Magnesium; Metal-binding;
KW Nucleotide-binding; Purine salvage; Transferase.
FT CHAIN 1..231
FT /note="Hypoxanthine-guanine-xanthine
FT phosphoribosyltransferase"
FT /id="PRO_0000139598"
FT ACT_SITE 148
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 77
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000250"
FT BINDING 144..152
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000250"
FT BINDING 204
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000250"
FT BINDING 204
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 231 AA; 26393 MW; A350333D5F5DD287 CRC64;
MPIPNNPGAG ENAFDPVFVK DDDGYDLDSF MIPAHYKKYL TKVLVPNGVI KNRIEKLAYD
IKKVYNNEEF HILCLLKGSR GFFTALLKHL SRIHNYSAVE MSKPLFGEHY VRVKSYCNDQ
STGTLEIVSE DLSCLKGKHV LIVEDIIDTG KTLVKFCEYL KKFEIKTVAI ACLFIKRTPL
WNGFKADFVG FSIPDHFVVG YSLDYNEIFR DLDHCCLVND EGKKKYKATS L
