HGPRT_STRA5
ID HGPRT_STRA5 Reviewed; 180 AA.
AC Q8E2H3;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Hypoxanthine-guanine phosphoribosyltransferase;
DE Short=HGPRT;
DE Short=HGPRTase;
DE EC=2.4.2.8 {ECO:0000250|UniProtKB:P9WHQ9};
GN Name=hpt; OrderedLocusNames=SAG0015;
OS Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=208435;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-611 / 2603 V/R;
RX PubMed=12200547; DOI=10.1073/pnas.182380799;
RA Tettelin H., Masignani V., Cieslewicz M.J., Eisen J.A., Peterson S.N.,
RA Wessels M.R., Paulsen I.T., Nelson K.E., Margarit I., Read T.D.,
RA Madoff L.C., Wolf A.M., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Lewis M.R., Radune D.,
RA Fedorova N.B., Scanlan D., Khouri H.M., Mulligan S., Carty H.A.,
RA Cline R.T., Van Aken S.E., Gill J., Scarselli M., Mora M., Iacobini E.T.,
RA Brettoni C., Galli G., Mariani M., Vegni F., Maione D., Rinaudo D.,
RA Rappuoli R., Telford J.L., Kasper D.L., Grandi G., Fraser C.M.;
RT "Complete genome sequence and comparative genomic analysis of an emerging
RT human pathogen, serotype V Streptococcus agalactiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:12391-12396(2002).
CC -!- FUNCTION: Purine salvage pathway enzyme that 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 the 6-oxopurines hypoxanthine
CC and guanine to form the corresponding ribonucleotides IMP (inosine 5'-
CC monophosphate) and GMP (guanosine 5'-monophosphate), with the release
CC of PPi. {ECO:0000250|UniProtKB:P9WHQ9}.
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:P9WHQ9};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17975;
CC Evidence={ECO:0000250|UniProtKB:P9WHQ9};
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:P9WHQ9};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:25426;
CC Evidence={ECO:0000250|UniProtKB:P9WHQ9};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P9WHQ9};
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway; IMP
CC from hypoxanthine: step 1/1. {ECO:0000250|UniProtKB:P9WHQ9}.
CC -!- PATHWAY: Purine metabolism; GMP biosynthesis via salvage pathway; GMP
CC from guanine: step 1/1. {ECO:0000250|UniProtKB:P9WHQ9}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC family. {ECO:0000305}.
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DR EMBL; AE009948; AAM98923.1; -; Genomic_DNA.
DR RefSeq; NP_687051.1; NC_004116.1.
DR RefSeq; WP_000892188.1; NC_004116.1.
DR AlphaFoldDB; Q8E2H3; -.
DR SMR; Q8E2H3; -.
DR STRING; 208435.SAG0015; -.
DR EnsemblBacteria; AAM98923; AAM98923; SAG0015.
DR GeneID; 66884927; -.
DR KEGG; sag:SAG0015; -.
DR PATRIC; fig|208435.3.peg.14; -.
DR HOGENOM; CLU_073615_0_0_9; -.
DR OMA; TMDWMAV; -.
DR UniPathway; UPA00591; UER00648.
DR UniPathway; UPA00909; UER00887.
DR Proteomes; UP000000821; 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:0032263; P:GMP salvage; IEA:UniProtKB-UniPathway.
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.
PE 3: Inferred from homology;
KW Cytoplasm; Glycosyltransferase; Magnesium; Metal-binding;
KW Nucleotide-binding; Purine salvage; Reference proteome; Transferase.
FT CHAIN 1..180
FT /note="Hypoxanthine-guanine phosphoribosyltransferase"
FT /id="PRO_0000139621"
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="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P9WHQ9"
FT BINDING 100
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P9WHQ9"
FT BINDING 131
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000250|UniProtKB:P9WHQ9"
FT BINDING 152..153
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000250|UniProtKB:P9WHQ9"
FT BINDING 159
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000250|UniProtKB:P9WHQ9"
FT BINDING 165
FT /ligand="diphosphate"
FT /ligand_id="ChEBI:CHEBI:33019"
FT /evidence="ECO:0000250|UniProtKB:P9WHQ9"
SQ SEQUENCE 180 AA; 20383 MW; FFB252189AA33AE3 CRC64;
MLENDIKKVL YSEEDIILKT KELGAKLTAD YAGKNPLLVG VLKGSVPFMA ELLKHIDTHV
EIDFMVVSSY HGGTTSSGEV KILKDVDTNI EGRDVIFIED IIDTGRTLKY LRDMFKYRQA
NSVKVATLFD KPEGRLVDID ADYVCYDIPN EFIVGFGLDY AENYRNLPYV GVLKEEIYSK
