HPRT_BUCAP
ID HPRT_BUCAP Reviewed; 177 AA.
AC Q8K9U8;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Hypoxanthine phosphoribosyltransferase;
DE Short=HPRT;
DE EC=2.4.2.8 {ECO:0000250|UniProtKB:P0A9M2};
GN Name=hpt; OrderedLocusNames=BUsg_189;
OS Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=198804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sg;
RX PubMed=12089438; DOI=10.1126/science.1071278;
RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT "50 million years of genomic stasis in endosymbiotic bacteria.";
RL Science 296:2376-2379(2002).
CC -!- FUNCTION: Purine salvage pathway enzyme which catalyzes the transfer of
CC the ribosyl-5-phosphate group from 5-phospho-alpha-D-ribose 1-
CC diphosphate (PRPP) to the N9 position of hypoxanthine to yield IMP
CC (inosine 5'-monophosphate). To a lesser extent, can also act on guanine
CC leading to GMP, but shows a highly less efficient activity with
CC xanthine. {ECO:0000250|UniProtKB:P0A9M2}.
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:P0A9M2};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17975;
CC Evidence={ECO:0000250|UniProtKB:P0A9M2};
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:P0A9M2};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:25426;
CC Evidence={ECO:0000250|UniProtKB:P0A9M2};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P0A9M2};
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway; IMP
CC from hypoxanthine: step 1/1. {ECO:0000250|UniProtKB:P0A9M2}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P0A9M2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC family. {ECO:0000305}.
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DR EMBL; AE013218; AAM67754.1; -; Genomic_DNA.
DR RefSeq; WP_011053721.1; NC_004061.1.
DR AlphaFoldDB; Q8K9U8; -.
DR SMR; Q8K9U8; -.
DR STRING; 198804.BUsg_189; -.
DR EnsemblBacteria; AAM67754; AAM67754; BUsg_189.
DR KEGG; bas:BUsg_189; -.
DR eggNOG; COG0634; Bacteria.
DR HOGENOM; CLU_073615_0_0_6; -.
DR OMA; TMDWMAV; -.
DR OrthoDB; 1819460at2; -.
DR UniPathway; UPA00591; UER00648.
DR Proteomes; UP000000416; Chromosome.
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 3: Inferred from homology;
KW Cytoplasm; Glycosyltransferase; Magnesium; Metal-binding;
KW Nucleotide-binding; Purine salvage; Transferase.
FT CHAIN 1..177
FT /note="Hypoxanthine phosphoribosyltransferase"
FT /id="PRO_0000139631"
FT REGION 43..44
FT /note="Diphosphate"
FT /evidence="ECO:0000250|UniProtKB:P9WHQ9"
FT ACT_SITE 103
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0A9M2"
FT BINDING 99
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000250|UniProtKB:P0A9M2"
FT BINDING 99
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000250|UniProtKB:P0A9M2"
FT BINDING 99
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0A9M2"
FT BINDING 100
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0A9M2"
FT BINDING 103..108
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000250|UniProtKB:P0A9M2"
FT BINDING 103..108
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000250|UniProtKB:P0A9M2"
FT BINDING 131
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000250|UniProtKB:P0A9M2"
FT BINDING 131
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000250|UniProtKB:P0A9M2"
FT BINDING 159
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000250|UniProtKB:P0A9M2"
FT BINDING 165
FT /ligand="diphosphate"
FT /ligand_id="ChEBI:CHEBI:33019"
FT /evidence="ECO:0000250|UniProtKB:P9WHQ9"
SQ SEQUENCE 177 AA; 20342 MW; A5311913399CDB2B CRC64;
MKHTIKVIIS EKELDIRVRE LGEEITKKYK NSKNKIILIA LLRGSFVFIA DLCRRIKIEH
EIDFMTTSSY GRGMISTGDV KIIKDLDEDI YNKNVLIVED IIDSGKTLSK VLGILKLRNP
KSLSICTLLD KPECREVNIN IDFVGFSIPD EFMVGYGIDY AQSYRYLPYI GKVIFKK
