HGXR_PLAFG
ID HGXR_PLAFG Reviewed; 231 AA.
AC P20035;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 110.
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 FCR-3 / Gambia).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=5838;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2682528; DOI=10.1093/nar/17.20.8382;
RA Vasanthakumar G., Davis R.L. Jr., Sullivan M.A., Donahue J.P.;
RT "Nucleotide sequence of cDNA clone for hypoxanthine-guanine
RT phosphoribosyltransferase from Plasmodium falciparum.";
RL Nucleic Acids Res. 17:8382-8382(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2205541; DOI=10.1016/0378-1119(90)90163-l;
RA Vasanthakumar G., Davis R.L. Jr., Sullivan M.A., Donahue J.P.;
RT "Cloning and expression in Escherichia coli of a hypoxanthine-guanine
RT phosphoribosyltransferase-encoding cDNA from Plasmodium falciparum.";
RL Gene 91:63-69(1990).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND
RP TRANSITION-STATE ANALOG.
RX PubMed=10433693; DOI=10.1021/bi990664p;
RA Shi W., Li C.M., Tyler P.C., Furneaux R.H., Cahill S.M., Girvin M.E.,
RA Grubmeyer C., Schramm V.L., Almo S.C.;
RT "The 2.0 A structure of malarial purine phosphoribosyltransferase in
RT complex with a transition-state analogue inhibitor.";
RL Biochemistry 38:9872-9880(1999).
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;
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.;
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. {ECO:0000269|PubMed:10433693}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC family. {ECO:0000305}.
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DR EMBL; X16279; CAA34355.1; -; mRNA.
DR PIR; S06601; S06601.
DR PDB; 1CJB; X-ray; 2.00 A; A/B/C/D=1-231.
DR PDB; 2VFA; X-ray; 2.80 A; A/B=1-56, A/B=171-231.
DR PDB; 3OZF; X-ray; 1.94 A; A/B/C/D=1-231.
DR PDB; 3OZG; X-ray; 1.99 A; A/B/C/D=1-231.
DR PDBsum; 1CJB; -.
DR PDBsum; 2VFA; -.
DR PDBsum; 3OZF; -.
DR PDBsum; 3OZG; -.
DR AlphaFoldDB; P20035; -.
DR SMR; P20035; -.
DR BindingDB; P20035; -.
DR ChEMBL; CHEMBL3988608; -.
DR DrugBank; DB02075; [(2R,3R,4S,5S)-3,4-Dihydroxy-5-(4-oxo-4,5-dihydro-1H-pyrrolo[3,2-d]pyrimidin-7-yl)-2-pyrrolidinyl]methyl dihydrogen phosphate.
DR DrugBank; DB11638; Artenimol.
DR BRENDA; 2.4.2.8; 4889.
DR UniPathway; UPA00591; UER00648.
DR UniPathway; UPA00602; UER00658.
DR UniPathway; UPA00909; UER00887.
DR EvolutionaryTrace; P20035; -.
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 1: Evidence at protein level;
KW 3D-structure; 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_0000139597"
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 BINDING 144..152
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT BINDING 176
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT BINDING 204
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT BINDING 204
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:10433693"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:3OZF"
FT HELIX 34..39
FT /evidence="ECO:0007829|PDB:3OZF"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:3OZF"
FT HELIX 47..65
FT /evidence="ECO:0007829|PDB:3OZF"
FT STRAND 70..76
FT /evidence="ECO:0007829|PDB:3OZF"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:3OZF"
FT HELIX 80..97
FT /evidence="ECO:0007829|PDB:3OZF"
FT STRAND 106..117
FT /evidence="ECO:0007829|PDB:3OZF"
FT STRAND 120..128
FT /evidence="ECO:0007829|PDB:3OZF"
FT HELIX 132..135
FT /evidence="ECO:0007829|PDB:3OZF"
FT STRAND 139..150
FT /evidence="ECO:0007829|PDB:3OZF"
FT HELIX 151..160
FT /evidence="ECO:0007829|PDB:3OZF"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:3OZF"
FT STRAND 166..176
FT /evidence="ECO:0007829|PDB:3OZF"
FT STRAND 187..193
FT /evidence="ECO:0007829|PDB:3OZF"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:3OZF"
FT STRAND 204..209
FT /evidence="ECO:0007829|PDB:2VFA"
FT STRAND 213..218
FT /evidence="ECO:0007829|PDB:3OZF"
FT HELIX 220..225
FT /evidence="ECO:0007829|PDB:3OZF"
SQ SEQUENCE 231 AA; 26348 MW; 4E681B63FD3D8131 CRC64;
MPIPNNPGAG ENAFDPVFVN DDDGYDLDSF MIPAHYKKYL TKVLVPNGVI KNRIEKLAYD
IKKVYNNEEF HILCLLKGSR GFFTALLKHL SRIHNYSAVE TSKPLFGEHY VRVKSYCNDQ
STGTLEIVSE DLSCLKGKHV LIVEDIIDTG KTLVKFCEYL KKFEIKTVAI ACLFIKRTPL
WNGFKADFVG FSIPDHFVVG YSLDYNEIFR DLDHCCLVND EGKKKYKATS L
