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Database: UniProt
Entry: A0A2P6FBE4_9MOLU
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ID   A0A2P6FBE4_9MOLU        Unreviewed;       174 AA.
AC   A0A2P6FBE4;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Hypoxanthine phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00011895, ECO:0000256|RuleBase:RU364099};
DE            EC=2.4.2.8 {ECO:0000256|ARBA:ARBA00011895, ECO:0000256|RuleBase:RU364099};
GN   Name=hpt_1 {ECO:0000313|EMBL:PQM30793.1};
GN   ORFNames=SMSRO_SF005820 {ECO:0000313|EMBL:PQM30793.1};
OS   Spiroplasma poulsonii.
OC   Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC   Spiroplasma.
OX   NCBI_TaxID=2138 {ECO:0000313|EMBL:PQM30793.1, ECO:0000313|Proteomes:UP000031565};
RN   [1] {ECO:0000313|EMBL:PQM30793.1, ECO:0000313|Proteomes:UP000031565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSRO {ECO:0000313|EMBL:PQM30793.1,
RC   ECO:0000313|Proteomes:UP000031565};
RX   PubMed=25827421;
RA   Paredes J.C., Herren J.K., Schupfer F., Marin R., Claverol S., Kuo C.H.,
RA   Lemaitre B., Beven L.;
RT   "Genome sequence of the Drosophila melanogaster male-killing Spiroplasma
RT   strain MSRO endosymbiont.";
RL   MBio 6:e02437-e02414(2015).
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; 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PQM30793.1}.
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DR   EMBL; JTLV02000001; PQM30793.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P6FBE4; -.
DR   STRING; 2138.SMSRO_v1c05520; -.
DR   OrthoDB; 9802824at2; -.
DR   UniPathway; UPA00591; UER00648.
DR   Proteomes; UP000031565; Unassembled WGS sequence.
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|RuleBase:RU364099,
KW   ECO:0000313|EMBL:PQM30793.1}; Magnesium {ECO:0000256|RuleBase:RU364099};
KW   Metal-binding {ECO:0000256|RuleBase:RU364099};
KW   Nucleotide-binding {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          14..158
FT                   /note="Phosphoribosyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00156"
SQ   SEQUENCE   174 AA;  20027 MW;  C00FCBD42FBD9ED5 CRC64;
     MQMEKLELYL SEAKIQEGIK TYAEKINTLY AGKKLYCIGL MNGALFFMGD LLKQLKNYIV
     VDTMSVSSYE KTNSTNNITI HKDISKDITG QDVLLIEDLI DTGQTLSVVI EKLQAKKPNS
     LRVVCLADKI EMHPDFKYDY DALFNFPNEF VVGYGFDYDD QYRQLPDVYI FRGE
//
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