HPRT_SCHMA
ID HPRT_SCHMA Reviewed; 284 AA.
AC P09383;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Hypoxanthine-guanine phosphoribosyltransferase;
DE Short=HGPRT;
DE Short=HGPRTase;
DE EC=2.4.2.8;
GN Name=HGPRT;
OS Schistosoma mansoni (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6183;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Puerto Rican;
RX PubMed=3136439; DOI=10.1093/nar/16.14.7087;
RA Craig S.P., McKerrow J.H., Newport G.N., Wang C.C.;
RT "Analysis of cDNA encoding the hypoxanthine-guanine
RT phosphoribosyltransferase (HGPRTase) of Schistosoma mansoni; a putative
RT target for chemotherapy.";
RL Nucleic Acids Res. 16:7087-7101(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Puerto Rican;
RX PubMed=2701934; DOI=10.1093/nar/17.4.1635;
RA Craig S.P., Muralidhar M.G., McKerrow J.H., Wang C.C.;
RT "Evidence for a class of very small introns in the gene for hypoxanthine-
RT guanine phosphoribosyltransferase in Schistosoma mansoni.";
RL Nucleic Acids Res. 17:1635-1647(1989).
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 -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC family. {ECO:0000305}.
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DR EMBL; X07883; CAA30730.1; ALT_SEQ; mRNA.
DR EMBL; X13531; CAA31885.1; -; Genomic_DNA.
DR EMBL; X13532; CAA31885.1; JOINED; Genomic_DNA.
DR EMBL; X13533; CAA31885.1; JOINED; Genomic_DNA.
DR EMBL; X13534; CAA31885.1; JOINED; Genomic_DNA.
DR PIR; S04278; S04278.
DR PIR; S09614; S09614.
DR PDB; 5IPF; X-ray; 2.80 A; A/B/C/D=55-284.
DR PDBsum; 5IPF; -.
DR AlphaFoldDB; P09383; -.
DR SMR; P09383; -.
DR STRING; 6183.Smp_103560.1; -.
DR eggNOG; KOG3367; Eukaryota.
DR HOGENOM; CLU_073615_3_0_1; -.
DR BRENDA; 2.4.2.8; 5608.
DR UniPathway; UPA00591; UER00648.
DR Proteomes; UP000008854; Unassembled WGS sequence.
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 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; Reference proteome; Transferase.
FT CHAIN 1..284
FT /note="Hypoxanthine-guanine phosphoribosyltransferase"
FT /id="PRO_0000139594"
FT ACT_SITE 198
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000250"
FT BINDING 194..202
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000250"
FT BINDING 226
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000250"
FT BINDING 253
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000250"
FT BINDING 253
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:5IPF"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:5IPF"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:5IPF"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:5IPF"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:5IPF"
FT HELIX 96..116
FT /evidence="ECO:0007829|PDB:5IPF"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:5IPF"
FT TURN 128..131
FT /evidence="ECO:0007829|PDB:5IPF"
FT HELIX 132..147
FT /evidence="ECO:0007829|PDB:5IPF"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:5IPF"
FT STRAND 155..160
FT /evidence="ECO:0007829|PDB:5IPF"
FT STRAND 188..200
FT /evidence="ECO:0007829|PDB:5IPF"
FT HELIX 201..210
FT /evidence="ECO:0007829|PDB:5IPF"
FT STRAND 216..226
FT /evidence="ECO:0007829|PDB:5IPF"
FT STRAND 237..242
FT /evidence="ECO:0007829|PDB:5IPF"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:5IPF"
FT STRAND 262..267
FT /evidence="ECO:0007829|PDB:5IPF"
FT HELIX 269..274
FT /evidence="ECO:0007829|PDB:5IPF"
SQ SEQUENCE 284 AA; 31854 MW; 5C2492D6ADFC6654 CRC64;
MLTSLITSST TVTLTLSQIY YILDIACGFL ISVLVWMNSS VLDNGNHSNP QIRDMSSNMI
KADCVVIEDS FRGFPTEYFC TSPRYDECLD YVLIPNGMIK DRLEKMSMDI VDYYEACNAT
SITLMCVLKG GFKFLADLVD GLERTVRARG IVLPMSVEFV RVKSYVNDVS IHEPILTGLG
DPSEYKDKNV LVVEDIIDTG KTITKLISHL DSLSTKSVKV ASLLVKRTSP RNDYRPDVGF
EVPNRFVVGY ALDYNDNFRD LHHICVINEV GQKKFSVPCT SKPV
