HPRT_TRYBB
ID HPRT_TRYBB Reviewed; 210 AA.
AC Q07010;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Hypoxanthine-guanine phosphoribosyltransferase;
DE Short=HGPRT;
DE Short=HGPRTase;
DE EC=2.4.2.8;
GN Name=HGPRT;
OS Trypanosoma brucei brucei.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=5702;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=8265360; DOI=10.1093/nar/21.23.5431;
RA Allen T.E., Ullman B.;
RT "Cloning and expression of the hypoxanthine-guanine
RT phosphoribosyltransferase gene from Trypanosoma brucei.";
RL Nucleic Acids Res. 21:5431-5438(1993).
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; L10721; AAA16328.1; -; Unassigned_DNA.
DR PIR; S41631; S41631.
DR PDB; 5JSQ; X-ray; 1.50 A; A/B=1-210.
DR PDB; 5JV5; X-ray; 2.73 A; A/B=1-210.
DR PDB; 5K51; X-ray; 2.96 A; A/B/C/D=1-210.
DR PDB; 5KAM; X-ray; 2.48 A; A/C=1-210.
DR PDB; 5KAP; X-ray; 2.95 A; A/B=1-210.
DR PDB; 6APS; X-ray; 1.76 A; A/B=1-210.
DR PDB; 6APT; X-ray; 1.79 A; A/B=1-210.
DR PDB; 6APU; X-ray; 1.84 A; A/B=1-210.
DR PDB; 6APV; X-ray; 1.99 A; A/B/C/D=1-210.
DR PDB; 6MXG; X-ray; 2.39 A; A/B=1-210.
DR PDB; 7SB7; X-ray; 2.65 A; A/B=1-210.
DR PDBsum; 5JSQ; -.
DR PDBsum; 5JV5; -.
DR PDBsum; 5K51; -.
DR PDBsum; 5KAM; -.
DR PDBsum; 5KAP; -.
DR PDBsum; 6APS; -.
DR PDBsum; 6APT; -.
DR PDBsum; 6APU; -.
DR PDBsum; 6APV; -.
DR PDBsum; 6MXG; -.
DR PDBsum; 7SB7; -.
DR AlphaFoldDB; Q07010; -.
DR SMR; Q07010; -.
DR BindingDB; Q07010; -.
DR ChEMBL; CHEMBL5069; -.
DR DrugCentral; Q07010; -.
DR OMA; IEFMAVS; -.
DR BioCyc; MetaCyc:MON-15863; -.
DR BRENDA; 2.4.2.8; 6520.
DR UniPathway; UPA00591; UER00648.
DR GO; GO:0097014; C:ciliary plasm; IDA:GeneDB.
DR GO; GO:0005737; C:cytoplasm; IDA:GeneDB.
DR GO; GO:0005829; C:cytosol; IDA:GeneDB.
DR GO; GO:0020015; C:glycosome; IDA:GeneDB.
DR GO; GO:0031981; C:nuclear lumen; IDA:GeneDB.
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; Transferase.
FT CHAIN 1..210
FT /note="Hypoxanthine-guanine phosphoribosyltransferase"
FT /id="PRO_0000139596"
FT ACT_SITE 117
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 54
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000250"
FT BINDING 113..121
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT STRAND 10..15
FT /evidence="ECO:0007829|PDB:5JSQ"
FT HELIX 17..34
FT /evidence="ECO:0007829|PDB:5JSQ"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:5JSQ"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:5JSQ"
FT STRAND 47..53
FT /evidence="ECO:0007829|PDB:5JSQ"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:5JSQ"
FT HELIX 57..69
FT /evidence="ECO:0007829|PDB:5JSQ"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:5JSQ"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:6APU"
FT STRAND 108..118
FT /evidence="ECO:0007829|PDB:5JSQ"
FT HELIX 120..130
FT /evidence="ECO:0007829|PDB:5JSQ"
FT STRAND 135..144
FT /evidence="ECO:0007829|PDB:5JSQ"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:5JSQ"
FT STRAND 156..161
FT /evidence="ECO:0007829|PDB:5JSQ"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:5JSQ"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:6MXG"
FT STRAND 182..187
FT /evidence="ECO:0007829|PDB:5JSQ"
FT HELIX 189..198
FT /evidence="ECO:0007829|PDB:5JSQ"
FT HELIX 201..204
FT /evidence="ECO:0007829|PDB:6APV"
SQ SEQUENCE 210 AA; 23360 MW; 6134FA880F40EC3D CRC64;
MEPACKYDFA TSVLFTEAEL HTRMRGVAQR IADDYSNCNL KPLENPLVIV SVLKGSFVFT
ADMVRILGDF GVPTRVEFLR ASSYGHDTKS CGRVDVKADG LCDIRGKHVL VLEDILDTAL
TLREVVDSLK KSEPASIKTL VAIDKPGGRK IPFTAEYVVA DVPNVFVVGY GLDYDQSYRE
VRDVVILKPS VYETWGKELE RRKAAGEAKR
