HGPRT_RHOCB
ID HGPRT_RHOCB Reviewed; 182 AA.
AC P37171; D5AU96;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=RCAP_rcc01790;
OS Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=272942;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=1756169; DOI=10.1016/0167-4781(91)90223-9;
RA Beckman D.L., Kranz R.G.;
RT "A bacterial homolog to HPRT.";
RL Biochim. Biophys. Acta 1129:112-114(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=20418398; DOI=10.1128/jb.00366-10;
RA Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA Haselkorn R.;
RT "Complete genome sequence of the photosynthetic purple nonsulfur bacterium
RT Rhodobacter capsulatus SB 1003.";
RL J. Bacteriol. 192:3545-3546(2010).
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.
CC -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC family. {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; X60977; CAA43293.1; -; Genomic_DNA.
DR EMBL; CP001312; ADE85535.1; -; Genomic_DNA.
DR PIR; S19720; S19720.
DR RefSeq; WP_013067514.1; NC_014034.1.
DR AlphaFoldDB; P37171; -.
DR SMR; P37171; -.
DR STRING; 272942.RCAP_rcc01790; -.
DR EnsemblBacteria; ADE85535; ADE85535; RCAP_rcc01790.
DR GeneID; 31490665; -.
DR KEGG; rcp:RCAP_rcc01790; -.
DR eggNOG; COG0634; Bacteria.
DR HOGENOM; CLU_073615_0_0_5; -.
DR OMA; TMDWMAV; -.
DR OrthoDB; 1819460at2; -.
DR UniPathway; UPA00591; UER00648.
DR UniPathway; UPA00909; UER00887.
DR Proteomes; UP000002361; 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.
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..182
FT /note="Hypoxanthine-guanine phosphoribosyltransferase"
FT /id="PRO_0000139611"
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="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P9WHQ9"
FT BINDING 102
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P9WHQ9"
FT BINDING 133
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000250|UniProtKB:P9WHQ9"
FT BINDING 154..155
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000250|UniProtKB:P9WHQ9"
FT BINDING 161
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000250|UniProtKB:P9WHQ9"
FT BINDING 167
FT /ligand="diphosphate"
FT /ligand_id="ChEBI:CHEBI:33019"
FT /evidence="ECO:0000250|UniProtKB:P9WHQ9"
SQ SEQUENCE 182 AA; 20323 MW; 890A60FCE67C0E05 CRC64;
MSQSGYVIDQ MISAKAIAAR VEALGAEITE AFKDTDRLVV VGLLRGSFVF IADLIREIGV
PCEVDFLEAS SYGNETTSTR EVRVLKDLRG IIGGRDVLVV EDIIDTGHTI SKVMEMLRAR
APRRIECCAM LDKPSRREVD VKARWTGFEI PDEFVVGYGL DYAQNHRNLP FIGTVRFTDP
QK
