ID HPRT_BUCAI Reviewed; 178 AA. AC P57291; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 09-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 129. DE RecName: Full=Hypoxanthine phosphoribosyltransferase; DE Short=HPRT; DE EC=2.4.2.8 {ECO:0000250|UniProtKB:P0A9M2}; GN Name=hpt; OrderedLocusNames=BU195; OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon OS pisum symbiotic bacterium). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Erwiniaceae; Buchnera. OX NCBI_TaxID=107806; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=APS; RX PubMed=10993077; DOI=10.1038/35024074; RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.; RT "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera RT sp. APS."; RL Nature 407:81-86(2000). 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}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB12912.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BA000003; BAB12912.1; ALT_SEQ; Genomic_DNA. DR RefSeq; NP_240026.1; NC_002528.1. DR RefSeq; WP_010895994.1; NC_002528.1. DR AlphaFoldDB; P57291; -. DR SMR; P57291; -. DR STRING; 563178.BUAP5A_192; -. DR EnsemblBacteria; BAB12912; BAB12912; BAB12912. DR KEGG; buc:BU195; -. DR PATRIC; fig|107806.10.peg.206; -. DR eggNOG; COG0634; Bacteria. DR HOGENOM; CLU_073615_0_0_6; -. DR UniPathway; UPA00591; UER00648. DR Proteomes; UP000001806; 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 NCBIfam; TIGR01203; HGPRTase; 1. DR PANTHER; PTHR43340:SF1; HYPOXANTHINE PHOSPHORIBOSYLTRANSFERASE; 1. DR PANTHER; PTHR43340; HYPOXANTHINE-GUANINE PHOSPHORIBOSYLTRANSFERASE; 1. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; PRTase-like; 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; Reference proteome; Transferase. FT CHAIN 1..178 FT /note="Hypoxanthine phosphoribosyltransferase" FT /id="PRO_0000139630" FT ACT_SITE 103 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:P0A9M2" FT BINDING 43 FT /ligand="diphosphate" FT /ligand_id="ChEBI:CHEBI:33019" FT /evidence="ECO:0000250|UniProtKB:P9WHQ9" FT BINDING 44 FT /ligand="diphosphate" FT /ligand_id="ChEBI:CHEBI:33019" FT /evidence="ECO:0000250|UniProtKB:P9WHQ9" 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 160 FT /ligand="GMP" FT /ligand_id="ChEBI:CHEBI:58115" FT /evidence="ECO:0000250|UniProtKB:P0A9M2" FT BINDING 166 FT /ligand="diphosphate" FT /ligand_id="ChEBI:CHEBI:33019" FT /evidence="ECO:0000250|UniProtKB:P9WHQ9" SQ SEQUENCE 178 AA; 20593 MW; D79B7A06E5E2C350 CRC64; MKHTLQVIIT EKELDIRVRE LGQEITKKYR NSRNKMILIA LLRGSFIFIS DLCRRIHIEH EIDFMTTSSY GRGMLSSGDV KIIKDLDEDI YNKNVLIVED IIDSGKTLSK VLDILKLRNP KSLSICTLLD KPECREVNIN VDFIGFSILE NFFIVGYGID YAQSYRYLPN IGKVVFKK //