ID Q1JP91_BOVIN Unreviewed; 218 AA.
AC Q1JP91;
DT 13-JUN-2006, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2006, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Hypoxanthine phosphoribosyltransferase {ECO:0000256|RuleBase:RU364099};
DE EC=2.4.2.8 {ECO:0000256|RuleBase:RU364099};
GN Name=HPRT1 {ECO:0000313|EMBL:ABF57418.1};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|EMBL:ABF57418.1};
RN [1] {ECO:0000313|EMBL:ABF57418.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Pooled {ECO:0000313|EMBL:ABF57418.1};
RX PubMed=11282978; DOI=10.1101/gr.170101;
RA Smith T.P., Grosse W.M., Freking B.A., Roberts A.J., Stone R.T., Casas E.,
RA Wray J.E., White J., Cho J., Fahrenkrug S.C., Bennett G.L., Heaton M.P.,
RA Laegreid W.W., Rohrer G.A., Chitko-McKown C.G., Pertea G., Holt I.,
RA Karamycheva S., Liang F., Quackenbush J., Keele J.W.;
RT "Sequence evaluation of four pooled-tissue normalized bovine cDNA libraries
RT and construction of a gene index for cattle.";
RL Genome Res. 11:626-630(2001).
RN [2] {ECO:0000313|EMBL:ABF57418.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Pooled {ECO:0000313|EMBL:ABF57418.1};
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [3] {ECO:0000313|EMBL:ABF57418.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Pooled {ECO:0000313|EMBL:ABF57418.1};
RA Harhay G.P., Sonstegard T.S., Van Tassell C.P., Clawson M.L., Heaton M.P.,
RA Keele J.W., Snelling W.M., Weidmann R.T., Smith T.P.L.;
RT "Sequencing and analysis of Bos taurus full-length insert cDNA clones.";
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Converts guanine to guanosine monophosphate, and hypoxanthine
CC to inosine monophosphate. Transfers the 5-phosphoribosyl group from 5-
CC phosphoribosylpyrophosphate onto the purine. Plays a central role in
CC the generation of purine nucleotides through the purine salvage
CC pathway. {ECO:0000256|ARBA:ARBA00025301}.
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 -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {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; BT025462; ABF57418.1; -; mRNA.
DR AlphaFoldDB; Q1JP91; -.
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; HYPOXANTHINE-GUANINE PHOSPHORIBOSYLTRANSFERASE; 1.
DR PANTHER; PTHR43340:SF6; HYPOXANTHINE-GUANINE PHOSPHORIBOSYLTRANSFERASE; 1.
DR Pfam; PF00156; Pribosyltran; 1.
DR SUPFAM; SSF53271; PRTase-like; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm {ECO:0000256|RuleBase:RU364099};
KW Glycosyltransferase {ECO:0000256|RuleBase:RU364099,
KW ECO:0000313|EMBL:ABF57418.1};
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|RuleBase:RU364099};
KW Transferase {ECO:0000256|RuleBase:RU364099, ECO:0000313|EMBL:ABF57418.1}.
FT DOMAIN 41..195
FT /note="Phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00156"
SQ SEQUENCE 218 AA; 24464 MW; 22F871E38A516D9B CRC64;
MAARSPSVVI SDDEPGYDLN LFCIPNHYAE DLEKVLIPHG LIMDRTERLA RDVMKEMGGH
HIVALCVLKG GYKFFADLLD YIKALNRNSD KSIPMTVDFI RLKSYCNDQS TGDIKVIGGD
DLSTLTGKNV LIVEDIIDTG KTMQTLLALV KKHKPKMVKV ASLLMKRTPR SVGYKPDFVG
FEIPDKFVVG YALDYNEYFR DLNHVCVISE TGKAKYKA
//
