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XPT1_YEAST
ID   XPT1_YEAST              Reviewed;         209 AA.
AC   P47165; D6VWV1;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 153.
DE   RecName: Full=Xanthine phosphoribosyltransferase 1;
DE            Short=XPRT;
DE            EC=2.4.2.-;
GN   Name=XPT1; OrderedLocusNames=YJR133W; ORFNames=J2118;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA   Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA   Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA   Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA   Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA   Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA   Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA   Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA   Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA   To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA   von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL   EMBO J. 15:2031-2049(1996).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   FUNCTION.
RX   PubMed=10217799; DOI=10.1128/jb.181.9.2984-2986.1999;
RA   Guetsova M.L., Crother T.R., Taylor M.W., Daignan-Fornier B.;
RT   "Isolation and characterization of the Saccharomyces cerevisiae XPT1 gene
RT   encoding xanthine phosphoribosyl transferase.";
RL   J. Bacteriol. 181:2984-2986(1999).
RN   [4]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [5]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
CC   -!- FUNCTION: May act as a xanthine phosphoribosyltransferase involved in
CC       the synthesis of purine nucleotides. Such activity is however unclear
CC       in vivo. {ECO:0000269|PubMed:10217799}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 721 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; Z49633; CAA89664.1; -; Genomic_DNA.
DR   EMBL; BK006943; DAA08917.1; -; Genomic_DNA.
DR   PIR; S57156; S57156.
DR   RefSeq; NP_012667.1; NM_001181791.1.
DR   AlphaFoldDB; P47165; -.
DR   SMR; P47165; -.
DR   BioGRID; 33888; 76.
DR   DIP; DIP-1576N; -.
DR   IntAct; P47165; 4.
DR   MINT; P47165; -.
DR   STRING; 4932.YJR133W; -.
DR   iPTMnet; P47165; -.
DR   MaxQB; P47165; -.
DR   PaxDb; P47165; -.
DR   PRIDE; P47165; -.
DR   EnsemblFungi; YJR133W_mRNA; YJR133W; YJR133W.
DR   GeneID; 853597; -.
DR   KEGG; sce:YJR133W; -.
DR   SGD; S000003894; XPT1.
DR   VEuPathDB; FungiDB:YJR133W; -.
DR   eggNOG; ENOG502QRN9; Eukaryota.
DR   GeneTree; ENSGT00940000176607; -.
DR   HOGENOM; CLU_092544_0_0_1; -.
DR   InParanoid; P47165; -.
DR   OMA; TYNDVHN; -.
DR   BioCyc; YEAST:YJR133W-MON; -.
DR   PRO; PR:P47165; -.
DR   Proteomes; UP000002311; Chromosome X.
DR   RNAct; P47165; protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0004422; F:hypoxanthine phosphoribosyltransferase activity; IGI:SGD.
DR   GO; GO:0004615; F:phosphomannomutase activity; IBA:GO_Central.
DR   GO; GO:0000310; F:xanthine phosphoribosyltransferase activity; IMP:SGD.
DR   GO; GO:0032263; P:GMP salvage; IBA:GO_Central.
DR   GO; GO:0046100; P:hypoxanthine metabolic process; IGI:SGD.
DR   GO; GO:0032264; P:IMP salvage; IBA:GO_Central.
DR   GO; GO:0032265; P:XMP salvage; IMP:SGD.
DR   CDD; cd06223; PRTases_typeI; 1.
DR   Gene3D; 3.40.50.2020; -; 1.
DR   InterPro; IPR000836; PRibTrfase_dom.
DR   InterPro; IPR029057; PRTase-like.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   SUPFAM; SSF53271; SSF53271; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Glycosyltransferase; Phosphoprotein; Purine biosynthesis;
KW   Reference proteome; Transferase.
FT   CHAIN           1..209
FT                   /note="Xanthine phosphoribosyltransferase 1"
FT                   /id="PRO_0000066042"
FT   MOD_RES         79
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
SQ   SEQUENCE   209 AA;  23671 MW;  0F47BE92DF82F0B7 CRC64;
     MAENERMYIS YNNIHKLCQG VAKHILARNE RPDIIIAITG GGMIPARIIR SFLKTKGQKN
     IPIQAIGLSL YEDLGLDNSV ETIGKEVIRT QWLDFGALNQ HFDSLIGKKV LIVDEVDDTR
     TTLHYAVSEL EKEIAEQQKV LNRMSEETVI SIFVLHNKDK PKRAGLPDSM MNSGRYIAAQ
     TVPDKWLCYP WDAEDIEEHT MLAKAQGHD
 
 
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