ID   XPT_OENOB               Reviewed;         206 AA.
AC   Q04GD7;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Xanthine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01184};
DE            Short=XPRTase {ECO:0000255|HAMAP-Rule:MF_01184};
DE            EC=2.4.2.22 {ECO:0000255|HAMAP-Rule:MF_01184};
GN   Name=xpt {ECO:0000255|HAMAP-Rule:MF_01184}; OrderedLocusNames=OEOE_0537;
OS   Oenococcus oeni (strain ATCC BAA-331 / PSU-1).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Oenococcus.
OX   NCBI_TaxID=203123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-331 / PSU-1;
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA   Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA   Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA   Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA   Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA   Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA   Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA   O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA   Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
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:0000255|HAMAP-Rule:MF_01184}.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_01184};
CC   -!- PATHWAY: Purine metabolism; XMP biosynthesis via salvage pathway; XMP
CC       from xanthine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01184}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01184}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01184}.
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC       family. Xpt subfamily. {ECO:0000255|HAMAP-Rule:MF_01184}.
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DR   EMBL; CP000411; ABJ56485.1; -; Genomic_DNA.
DR   RefSeq; WP_011677511.1; NC_008528.1.
DR   AlphaFoldDB; Q04GD7; -.
DR   SMR; Q04GD7; -.
DR   STRING; 203123.OEOE_0537; -.
DR   EnsemblBacteria; ABJ56485; ABJ56485; OEOE_0537.
DR   KEGG; ooe:OEOE_0537; -.
DR   PATRIC; fig|203123.7.peg.543; -.
DR   eggNOG; COG0503; Bacteria.
DR   HOGENOM; CLU_099015_0_0_9; -.
DR   OMA; HQVDPVL; -.
DR   OrthoDB; 1532478at2; -.
DR   UniPathway; UPA00602; UER00658.
DR   Proteomes; UP000000774; 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   3: Inferred from homology;
KW   Cytoplasm; Glycosyltransferase; Purine salvage; Reference proteome;
KW   Transferase.
FT   CHAIN           1..206
FT                   /note="Xanthine phosphoribosyltransferase"
FT                   /id="PRO_0000339723"
FT   BINDING         28
FT                   /ligand="xanthine"
FT                   /ligand_id="ChEBI:CHEBI:17712"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01184"
FT   BINDING         35
FT                   /ligand="xanthine"
FT                   /ligand_id="ChEBI:CHEBI:17712"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01184"
FT   BINDING         136..140
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01184"
FT   BINDING         164
FT                   /ligand="xanthine"
FT                   /ligand_id="ChEBI:CHEBI:17712"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01184"
SQ   SEQUENCE   206 AA;  22794 MW;  E1A284AF745F6337 CRC64;
     MKLDRRLVIK ILEEKIKSEG IVLGSDILKV NSFLNHQIDP FLMSQIGQAF AEKFSHENIS
     KVLTIESSGI APALMTSLQL QVPMIFARKH QSRTLNEEFF SASVYSYTKQ TENQIAVSKR
     FINPGDRVLI IDDFLANGQA VQGLLDIINQ AGASAVGVGI VIEKRFQAGH QLILSKNLPL
     VSLASIDRFE DGQVVFSKQG ETSHVN