ID H3GHL0_PHYRM Unreviewed; 222 AA.
AC H3GHL0;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
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};
OS Phytophthora ramorum (Sudden oak death agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=164328 {ECO:0000313|EnsemblProtists:Phyra75431, ECO:0000313|Proteomes:UP000005238};
RN [1] {ECO:0000313|Proteomes:UP000005238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pr102 {ECO:0000313|Proteomes:UP000005238};
RX PubMed=16946064; DOI=10.1126/science.1128796;
RA Tyler B.M., Tripathy S., Zhang X., Dehal P., Jiang R.H., Aerts A.,
RA Arredondo F.D., Baxter L., Bensasson D., Beynon J.L., Chapman J.,
RA Damasceno C.M., Dorrance A.E., Dou D., Dickerman A.W., Dubchak I.L.,
RA Garbelotto M., Gijzen M., Gordon S.G., Govers F., Grunwald N.J., Huang W.,
RA Ivors K.L., Jones R.W., Kamoun S., Krampis K., Lamour K.H., Lee M.K.,
RA McDonald W.H., Medina M., Meijer H.J., Nordberg E.K., Maclean D.J.,
RA Ospina-Giraldo M.D., Morris P.F., Phuntumart V., Putnam N.H., Rash S.,
RA Rose J.K., Sakihama Y., Salamov A.A., Savidor A., Scheuring C.F.,
RA Smith B.M., Sobral B.W., Terry A., Torto-Alalibo T.A., Win J., Xu Z.,
RA Zhang H., Grigoriev I.V., Rokhsar D.S., Boore J.L.;
RT "Phytophthora genome sequences uncover evolutionary origins and mechanisms
RT of pathogenesis.";
RL Science 313:1261-1266(2006).
RN [2] {ECO:0000313|EnsemblProtists:Phyra75431}
RP IDENTIFICATION.
RC STRAIN=Pr102 {ECO:0000313|EnsemblProtists:Phyra75431};
RG EnsemblProtists;
RL Submitted (JUN-2015) to UniProtKB.
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|RuleBase:RU364099};
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}.
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DR EMBL; DS566009; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H3GHL0; -.
DR STRING; 164328.H3GHL0; -.
DR EnsemblProtists; Phyra75431; Phyra75431; Phyra75431.
DR VEuPathDB; FungiDB:PSURA_75431; -.
DR eggNOG; KOG3367; Eukaryota.
DR HOGENOM; CLU_073615_3_0_1; -.
DR InParanoid; H3GHL0; -.
DR OMA; MQWRVAP; -.
DR UniPathway; UPA00591; UER00648.
DR Proteomes; UP000005238; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0052657; F:guanine phosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004422; F:hypoxanthine phosphoribosyltransferase activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0032263; P:GMP salvage; IBA:GO_Central.
DR GO; GO:0006178; P:guanine salvage; IBA:GO_Central.
DR GO; GO:0046100; P:hypoxanthine metabolic process; IBA:GO_Central.
DR GO; GO:0032264; P:IMP salvage; IBA:GO_Central.
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 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:UP000005238};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU364099}.
FT DOMAIN 43..197
FT /note="Phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00156"
SQ SEQUENCE 222 AA; 24937 MW; ECBC6C6462754A4E CRC64;
MAAAHDPKRV IYLEDDATYD KAQFLVPHHY LESIESVLIS KGLIEDRVEK LAQDIRYAYE
GKTVHLLCVL KGGSAFFHAL VDKLRLFHKY NKCDYVPFTF DFIKVKSYAG TKSTGNVEVS
GADLAKFKGK SLLLVEDIID TGKTMSKLVP MLSEYEPESV RVASLLEKRN PESCGFQADF
VGFNIPDKFV IGFCLDYNEV FRDLDHICVI NEAGIAKYAS SS
//
