ID   Q2RGP1_MOOTA            Unreviewed;       181 AA.
AC   Q2RGP1;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 91.
DE   RecName: Full=Hypoxanthine phosphoribosyltransferase {ECO:0000256|RuleBase:RU364099};
DE            EC=2.4.2.8 {ECO:0000256|RuleBase:RU364099};
GN   OrderedLocusNames=Moth_2106 {ECO:0000313|EMBL:ABC20398.1};
OS   Moorella thermoacetica (strain ATCC 39073 / JCM 9320).
OC   Bacteria; Bacillota; Clostridia; Moorellales; Moorellaceae; Moorella.
OX   NCBI_TaxID=264732 {ECO:0000313|EMBL:ABC20398.1};
RN   [1] {ECO:0000313|EMBL:ABC20398.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 39073 {ECO:0000313|EMBL:ABC20398.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chertkov O., Saunders E.H., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Richardson P., Ragsdale S.;
RT   "Complete sequence of Moorella thermoacetica ATCC 39073.";
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00002049}.
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:0000256|ARBA:ARBA00000210};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:25426;
CC         Evidence={ECO:0000256|ARBA:ARBA00000210};
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:0000256|ARBA:ARBA00001442};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17975;
CC         Evidence={ECO:0000256|ARBA:ARBA00001442};
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; CP000232; ABC20398.1; -; Genomic_DNA.
DR   RefSeq; YP_430941.1; NC_007644.1.
DR   AlphaFoldDB; Q2RGP1; -.
DR   STRING; 264732.Moth_2106; -.
DR   EnsemblBacteria; ABC20398; ABC20398; Moth_2106.
DR   KEGG; mta:Moth_2106; -.
DR   PATRIC; fig|264732.11.peg.2290; -.
DR   eggNOG; COG0634; Bacteria.
DR   HOGENOM; CLU_073615_0_0_9; -.
DR   OrthoDB; 9802824at2; -.
DR   UniPathway; UPA00591; UER00648.
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.
PE   3: Inferred from homology;
KW   Cytoplasm {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   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU364099}.
FT   DOMAIN          15..159
FT                   /note="Phosphoribosyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00156"
SQ   SEQUENCE   181 AA;  20248 MW;  EC62ABB499DC2862 CRC64;
     MHEDIAEVLV SAADIQKRVK EMGAAISRDY AGKDLLVVGI LKGAIIFLAD LVREITIPLQ
     LDFMAVSSYG SGTSTSGAVR ILKDLEVPVE DKHLLIVEDI IDTGLTLKYL LENLKARQPL
     SVKACTILDK PERRLVDVHV DYSGFCIPDY FVVGYGLDYA QKYRHLPDIC VLKPEVYRRK
     K
//