ID   XGPT_BUCAI              Reviewed;         158 AA.
AC   P57339;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   18-APR-2012, entry version 74.
DE   RecName: Full=Xanthine phosphoribosyltransferase;
DE            EC=2.4.2.22;
DE   AltName: Full=Xanthine-guanine phosphoribosyltransferase;
DE            Short=XGPRT;
GN   Name=gpt; OrderedLocusNames=BU251;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS)
OS   (Acyrthosiphon pisum symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   MEDLINE=20445173; PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids
RT   Buchnera sp. APS.";
RL   Nature 407:81-86(2000).
CC   -!- FUNCTION: Acts on guanine, xanthine and to a lesser extent
CC       hypoxanthine (By similarity).
CC   -!- CATALYTIC ACTIVITY: XMP + diphosphate = 5-phospho-alpha-D-ribose
CC       1-diphosphate + xanthine.
CC   -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
CC   -!- PATHWAY: Purine metabolism; XMP biosynthesis via salvage pathway;
CC       XMP from xanthine: step 1/1.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine
CC       phosphoribosyltransferase family. XGPT subfamily.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB12961.1; Type=Erroneous initiation;
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DR   EMBL; BA000003; BAB12961.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_240075.2; NC_002528.1.
DR   ProteinModelPortal; P57339; -.
DR   SMR; P57339; 3-151.
DR   EnsemblBacteria; EBBUCT00000002828; EBBUCP00000002604; EBBUCG00000002828.
DR   GeneID; 1109690; -.
DR   GenomeReviews; BA000003_GR; BU251.
DR   KEGG; buc:BU251; -.
DR   PATRIC; 21244026; VBIBucAph127364_0261.
DR   eggNOG; COG0503; -.
DR   HOGENOM; HBG503428; -.
DR   KO; K00769; -.
DR   OMA; LVDTFIT; -.
DR   ProtClustDB; PRK09177; -.
DR   BioCyc; BSP107806:BU251-MONOMER; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000310; F:xanthine phosphoribosyltransferase activity; IEA:EC.
DR   GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-KW.
DR   HAMAP; MF_01903; XGPRT; 1; -.
DR   InterPro; IPR000836; PRibTrfase.
DR   InterPro; IPR023747; Xanthine_Guanine_PRibTrfase.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Complete proteome; Glycosyltransferase; Magnesium;
KW   Membrane; Metal-binding; Purine salvage; Reference proteome;
KW   Transferase.
FT   CHAIN         1    158       Xanthine phosphoribosyltransferase.
FT                                /FTId=PRO_0000139660.
FT   REGION       38     39       5-phosphoribose 1-diphosphate binding (By
FT                                similarity).
FT   REGION       94     98       5-phosphoribose 1-diphosphate binding (By
FT                                similarity).
FT   METAL        91     91       Magnesium (By similarity).
FT   BINDING      94     94       Xanthine (By similarity).
FT   BINDING     137    137       Xanthine; via amide nitrogen and carbonyl
FT                                oxygen (By similarity).
SQ   SEQUENCE   158 AA;  18064 MW;  2B40B2A98EAABF28 CRC64;
     MSEKYIVTWD MLQIHTRKLA NRLVKKIHSW NGIIAVSRGG LVPSALLARE LGLRCVDTVC
     IESYNYDCLK ENRKIIKKAE GNGEKIIVID DLVDTGGTAK IIRKLYPKAC FVTIFAKPMG
     RSLVDNYIID IPQNVWIEQP WDMSISYIPP LIQNYKIK
//