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   02-NOV-2016, entry version 100.
DE   RecName: Full=Xanthine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01903};
DE            EC=2.4.2.22 {ECO:0000255|HAMAP-Rule:MF_01903};
DE   AltName: Full=Xanthine-guanine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01903};
DE            Short=XGPRT {ECO:0000255|HAMAP-Rule:MF_01903};
GN   Name=gpt {ECO:0000255|HAMAP-Rule:MF_01903}; OrderedLocusNames=BU251;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS)
OS   (Acyrthosiphon pisum symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   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. {ECO:0000255|HAMAP-Rule:MF_01903}.
CC   -!- CATALYTIC ACTIVITY: XMP + diphosphate = 5-phospho-alpha-D-ribose
CC       1-diphosphate + xanthine. {ECO:0000255|HAMAP-Rule:MF_01903}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01903};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01903};
CC   -!- PATHWAY: Purine metabolism; XMP biosynthesis via salvage pathway;
CC       XMP from xanthine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01903}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01903}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01903}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01903}.
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine
CC       phosphoribosyltransferase family. XGPT subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01903}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB12961.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BA000003; BAB12961.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_240075.2; NC_002528.1.
DR   RefSeq; WP_009874205.1; NC_002528.1.
DR   ProteinModelPortal; P57339; -.
DR   STRING; 107806.BU251; -.
DR   EnsemblBacteria; BAB12961; BAB12961; BAB12961.
DR   GeneID; 1109690; -.
DR   KEGG; buc:BU251; -.
DR   PATRIC; 21244026; VBIBucAph127364_0261.
DR   eggNOG; ENOG4105DYA; Bacteria.
DR   eggNOG; COG0503; LUCA.
DR   HOGENOM; HOG000226805; -.
DR   KO; K00769; -.
DR   OMA; FHRDCRA; -.
DR   UniPathway; UPA00602; UER00658.
DR   Proteomes; UP000001806; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000310; F:xanthine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-HAMAP.
DR   GO; GO:0032265; P:XMP salvage; IEA:UniProtKB-UniPathway.
DR   CDD; cd06223; PRTases_typeI; 1.
DR   Gene3D; 3.40.50.2020; -; 1.
DR   HAMAP; MF_01903; XGPRT; 1.
DR   InterPro; IPR000836; PRibTrfase_dom.
DR   InterPro; IPR029057; PRTase-like.
DR   InterPro; IPR023747; Xanthine_Guanine_PRibTrfase.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   SUPFAM; SSF53271; SSF53271; 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.
FT                                {ECO:0000255|HAMAP-Rule:MF_01903}.
FT   REGION       94     98       5-phosphoribose 1-diphosphate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01903}.
FT   METAL        91     91       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01903}.
FT   BINDING      94     94       Xanthine. {ECO:0000255|HAMAP-
FT                                Rule:MF_01903}.
FT   BINDING     137    137       Xanthine; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_01903}.
SQ   SEQUENCE   158 AA;  18064 MW;  2B40B2A98EAABF28 CRC64;
     MSEKYIVTWD MLQIHTRKLA NRLVKKIHSW NGIIAVSRGG LVPSALLARE LGLRCVDTVC
     IESYNYDCLK ENRKIIKKAE GNGEKIIVID DLVDTGGTAK IIRKLYPKAC FVTIFAKPMG
     RSLVDNYIID IPQNVWIEQP WDMSISYIPP LIQNYKIK
//