ID   XPT_ENTFA               Reviewed;         193 AA.
AC   Q831Y0;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Xanthine phosphoribosyltransferase;
DE            Short=XPRTase;
DE            EC=2.4.2.22;
GN   Name=xpt; OrderedLocusNames=EF_2365;
OS   Enterococcus faecalis (strain ATCC 700802 / V583).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=226185;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700802 / V583;
RX   PubMed=12663927; DOI=10.1126/science.1080613;
RA   Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA   Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA   Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA   DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA   Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA   Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT   "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT   faecalis.";
RL   Science 299:2071-2074(2003).
RN   [2]
RP   FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=4216296; DOI=10.1016/0003-9861(74)90173-8;
RA   Miller R.L., Adamczyk D.L., Fyfe J.A., Elion G.B.;
RT   "Xanthine phosphoribosyltransferase from Streptococcus faecalis. Properties
RT   and specificity.";
RL   Arch. Biochem. Biophys. 165:349-358(1974).
CC   -!- FUNCTION: Converts the preformed base xanthine, a product of nucleic
CC       acid breakdown, to xanthosine 5'-monophosphate (XMP), so it can be
CC       reused for RNA or DNA synthesis. {ECO:0000269|PubMed:4216296}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=diphosphate + XMP = 5-phospho-alpha-D-ribose 1-diphosphate +
CC         xanthine; Xref=Rhea:RHEA:10800, ChEBI:CHEBI:17712, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57464, ChEBI:CHEBI:58017; EC=2.4.2.22;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.02 mM for xanthine {ECO:0000269|PubMed:4216296};
CC       pH dependence:
CC         Optimum pH is 7.4-8.8. {ECO:0000269|PubMed:4216296};
CC       Temperature dependence:
CC         Thermostable for 60 minutes up to 55 degrees Celsius.
CC         {ECO:0000269|PubMed:4216296};
CC   -!- PATHWAY: Purine metabolism; XMP biosynthesis via salvage pathway; XMP
CC       from xanthine: step 1/1.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC       family. Xpt subfamily. {ECO:0000305}.
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DR   EMBL; AE016830; AAO82087.1; -; Genomic_DNA.
DR   RefSeq; NP_816017.1; NC_004668.1.
DR   RefSeq; WP_002356804.1; NZ_KE136528.1.
DR   AlphaFoldDB; Q831Y0; -.
DR   SMR; Q831Y0; -.
DR   STRING; 226185.EF_2365; -.
DR   EnsemblBacteria; AAO82087; AAO82087; EF_2365.
DR   GeneID; 60894423; -.
DR   KEGG; efa:EF2365; -.
DR   PATRIC; fig|226185.45.peg.1173; -.
DR   eggNOG; COG0503; Bacteria.
DR   HOGENOM; CLU_099015_0_0_9; -.
DR   OMA; HQVDPVL; -.
DR   SABIO-RK; Q831Y0; -.
DR   UniPathway; UPA00602; UER00658.
DR   Proteomes; UP000001415; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000310; F:xanthine phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-UniRule.
DR   GO; GO:0046110; P:xanthine metabolic process; IEA:InterPro.
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_01184; XPRTase; 1.
DR   InterPro; IPR000836; PRibTrfase_dom.
DR   InterPro; IPR029057; PRTase-like.
DR   InterPro; IPR010079; Xanthine_PRibTrfase.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   SUPFAM; SSF53271; SSF53271; 1.
DR   TIGRFAMs; TIGR01744; XPRTase; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Glycosyltransferase; Purine salvage; Reference proteome;
KW   Transferase.
FT   CHAIN           1..193
FT                   /note="Xanthine phosphoribosyltransferase"
FT                   /id="PRO_0000339698"
FT   BINDING         20
FT                   /ligand="xanthine"
FT                   /ligand_id="ChEBI:CHEBI:17712"
FT                   /evidence="ECO:0000250"
FT   BINDING         27
FT                   /ligand="xanthine"
FT                   /ligand_id="ChEBI:CHEBI:17712"
FT                   /evidence="ECO:0000250"
FT   BINDING         128..132
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT                   /evidence="ECO:0000250"
FT   BINDING         156
FT                   /ligand="xanthine"
FT                   /ligand_id="ChEBI:CHEBI:17712"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   193 AA;  20854 MW;  58C30CE219319B5C CRC64;
     MKELVERIKN DGRVLGEGVL KVDSFITHQV DPELMEAMGN RFAEVFAEAG ITKVITIEAS
     GIAPALYAAQ KLGVPMIFAR KAKSLTMDEE LLTASVYSFT KQVTSQISIS RKFLSDADKV
     LIIDDFLANG QAAKGLVELC QQAGAKVEGI GIVIEKSFQD GRQLLEDMGL NVVSLARIAS
     LSEGTVTFLE EDA