HPRT_HAEIN
ID HPRT_HAEIN Reviewed; 179 AA.
AC P45078;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Hypoxanthine phosphoribosyltransferase;
DE Short=HPRT;
DE EC=2.4.2.8 {ECO:0000250|UniProtKB:P0A9M2};
GN Name=hpt; OrderedLocusNames=HI_1153;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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.
CC -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC family. {ECO:0000305}.
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DR EMBL; L42023; AAC22808.1; -; Genomic_DNA.
DR PIR; D64168; D64168.
DR RefSeq; NP_439311.1; NC_000907.1.
DR RefSeq; WP_005693468.1; NC_000907.1.
DR AlphaFoldDB; P45078; -.
DR SMR; P45078; -.
DR STRING; 71421.HI_1153; -.
DR EnsemblBacteria; AAC22808; AAC22808; HI_1153.
DR KEGG; hin:HI_1153; -.
DR PATRIC; fig|71421.8.peg.1203; -.
DR eggNOG; COG0634; Bacteria.
DR HOGENOM; CLU_073615_0_0_6; -.
DR OMA; TMDWMAV; -.
DR PhylomeDB; P45078; -.
DR BioCyc; HINF71421:G1GJ1-1186-MON; -.
DR UniPathway; UPA00591; UER00648.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0052657; F:guanine phosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004422; F:hypoxanthine phosphoribosyltransferase activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0032263; P:GMP salvage; IBA:GO_Central.
DR GO; GO:0006178; P:guanine salvage; IBA:GO_Central.
DR GO; GO:0046100; P:hypoxanthine metabolic process; IBA:GO_Central.
DR GO; GO:0032264; P:IMP salvage; IBA:GO_Central.
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; Reference proteome; Transferase.
FT CHAIN 1..179
FT /note="Hypoxanthine phosphoribosyltransferase"
FT /id="PRO_0000139634"
FT REGION 45..46
FT /note="Diphosphate"
FT /evidence="ECO:0000250|UniProtKB:P9WHQ9"
FT ACT_SITE 105
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0A9M2"
FT BINDING 101
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000250|UniProtKB:P0A9M2"
FT BINDING 101
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000250|UniProtKB:P0A9M2"
FT BINDING 101
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0A9M2"
FT BINDING 102
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0A9M2"
FT BINDING 105..110
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000250|UniProtKB:P0A9M2"
FT BINDING 105..110
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000250|UniProtKB:P0A9M2"
FT BINDING 133
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000250|UniProtKB:P0A9M2"
FT BINDING 133
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000250|UniProtKB:P0A9M2"
FT BINDING 161
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000250|UniProtKB:P0A9M2"
FT BINDING 167
FT /ligand="diphosphate"
FT /ligand_id="ChEBI:CHEBI:33019"
FT /evidence="ECO:0000250|UniProtKB:P9WHQ9"
SQ SEQUENCE 179 AA; 20370 MW; 65F8C1314942BFE7 CRC64;
MKKHHVDVLI SENDVHARIA ELGAQITKFY QEKQIDNLVV VGLLRGSFMF MADIVRQINL
PVEIEFMTTS SYGTGMTTNH DVRITKDLDG DIKGKHVLIV EDIIDTGYTL EKVRDILNLR
EPASLTICTL LDKPSRREVE VPVEWVGFEI PDEFVVGYGI DYAQRHRNLG YIGKVVLEE
