ID   Q1AS81_RUBXD            Unreviewed;       175 AA.
AC   Q1AS81;
DT   11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2006, sequence version 1.
DT   02-SEP-2026, entry version 103.
DE   RecName: Full=Hypoxanthine phosphoribosyltransferase {ECO:0000256|RuleBase:RU364099};
DE            EC=2.4.2.8 {ECO:0000256|RuleBase:RU364099};
GN   OrderedLocusNames=Rxyl_2835 {ECO:0000313|EMBL:ABG05747.1};
OS   Rubrobacter xylanophilus (strain DSM 9941 / JCM 11954 / NBRC 16129 /
OS   PRD-1).
OC   Bacteria; Bacillati; Actinomycetota; Rubrobacteria; Rubrobacterales;
OC   Rubrobacteraceae; Rubrobacter.
OX   NCBI_TaxID=266117 {ECO:0000313|EMBL:ABG05747.1, ECO:0000313|Proteomes:UP000006637};
RN   [1] {ECO:0000313|EMBL:ABG05747.1, ECO:0000313|Proteomes:UP000006637}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 9941 / NBRC 16129 / PRD-1
RC   {ECO:0000313|Proteomes:UP000006637};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., da Costa M.S.,
RA   Rainey F.A., Empadinhas N., Jolivet E., Battista J.R., Richardson P.;
RT   "Complete sequence of Rubrobacter xylanophilus DSM 9941.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GMP + diphosphate = guanine + 5-phospho-alpha-D-ribose 1-
CC         diphosphate; Xref=Rhea:RHEA:25424, ChEBI:CHEBI:16235,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58115; EC=2.4.2.8;
CC         Evidence={ECO:0000256|ARBA:ARBA00048811};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:25426;
CC         Evidence={ECO:0000256|ARBA:ARBA00048811};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-
CC         diphosphate; 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:0000256|ARBA:ARBA00049402};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17975;
CC         Evidence={ECO:0000256|ARBA:ARBA00049402};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|RuleBase:RU364099};
CC   -!- PATHWAY: Purine metabolism; GMP biosynthesis via salvage pathway; GMP
CC       from guanine: step 1/1. {ECO:0000256|ARBA:ARBA00004676}.
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway; IMP
CC       from hypoxanthine: step 1/1. {ECO:0000256|ARBA:ARBA00004669,
CC       ECO:0000256|RuleBase:RU364099}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|RuleBase:RU364099}.
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC       family. {ECO:0000256|ARBA:ARBA00008391, ECO:0000256|RuleBase:RU364099}.
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DR   EMBL; CP000386; ABG05747.1; -; Genomic_DNA.
DR   RefSeq; WP_011565756.1; NC_008148.1.
DR   AlphaFoldDB; Q1AS81; -.
DR   STRING; 266117.Rxyl_2835; -.
DR   KEGG; rxy:Rxyl_2835; -.
DR   eggNOG; COG0634; Bacteria.
DR   HOGENOM; CLU_073615_0_0_11; -.
DR   PhylomeDB; Q1AS81; -.
DR   UniPathway; UPA00591; UER00648.
DR   Proteomes; UP000006637; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0052657; F:guanine phosphoribosyltransferase activity; IEA:UniProtKB-ARBA.
DR   GO; GO:0004422; F:hypoxanthine phosphoribosyltransferase activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:TreeGrafter.
DR   GO; GO:0032263; P:GMP salvage; IEA:TreeGrafter.
DR   GO; GO:0006178; P:guanine salvage; IEA:TreeGrafter.
DR   GO; GO:0046100; P:hypoxanthine metabolic process; IEA:TreeGrafter.
DR   GO; GO:0032264; P:IMP salvage; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006166; P:purine ribonucleoside salvage; IEA:InterPro.
DR   CDD; cd06223; PRTases_typeI; 1.
DR   FunFam; 3.40.50.2020:FF:000006; Hypoxanthine phosphoribosyltransferase; 1.
DR   Gene3D; 3.40.50.2020; -; 1.
DR   InterPro; IPR050408; HGPRT.
DR   InterPro; IPR005904; Hxn_phspho_trans.
DR   InterPro; IPR029057; PRTase-like.
DR   InterPro; IPR000836; PRTase_dom.
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.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU364099};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000256|RuleBase:RU364099};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU364099};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU364099};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU364099};
KW   Purine salvage {ECO:0000256|ARBA:ARBA00022726,
KW   ECO:0000256|RuleBase:RU364099};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006637};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU364099}.
FT   DOMAIN          14..159
FT                   /note="Phosphoribosyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00156"
SQ   SEQUENCE   175 AA;  19568 MW;  8598F109E9B2E66B CRC64;
     MMPEIGPVLV PAGEIQRKVR ELGERITRDY AGQNLLLVGI LRGAFVVLSD LIRQIEIPCE
     VDFMEVSSYG AGTTSSGVVR ILKDLEEDIS GRHVLIVEDI IDTGLTLSYL RRSLLARKPA
     SLEICALLSK PARRQVDIQV RYQGFEVPDV FVVGYGIDYA GFYRNLRDIY ALKQP
//