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Database: UniProt/SWISS-PROT
Entry: XPT_STRSV
LinkDB: XPT_STRSV
Original site: XPT_STRSV 
ID   XPT_STRSV               Reviewed;         193 AA.
AC   A3CMY9;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 2.
DT   29-MAY-2013, entry version 39.
DE   RecName: Full=Xanthine phosphoribosyltransferase;
DE            Short=XPRTase;
DE            EC=2.4.2.22;
GN   Name=xpt; OrderedLocusNames=SSA_1134;
OS   Streptococcus sanguinis (strain SK36).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=388919;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK36;
RX   PubMed=17277061; DOI=10.1128/JB.01808-06;
RA   Xu P., Alves J.M., Kitten T., Brown A., Chen Z., Ozaki L.S.,
RA   Manque P., Ge X., Serrano M.G., Puiu D., Hendricks S., Wang Y.,
RA   Chaplin M.D., Akan D., Paik S., Peterson D.L., Macrina F.L.,
RA   Buck G.A.;
RT   "Genome of the opportunistic pathogen Streptococcus sanguinis.";
RL   J. Bacteriol. 189:3166-3175(2007).
CC   -!- FUNCTION: Converts the preformed base xanthine, a product of
CC       nucleic acid breakdown, to xanthosine 5'-monophosphate (XMP), so
CC       it can be reused for RNA or DNA synthesis (By similarity).
CC   -!- CATALYTIC ACTIVITY: XMP + diphosphate = 5-phospho-alpha-D-ribose
CC       1-diphosphate + xanthine.
CC   -!- PATHWAY: Purine metabolism; XMP biosynthesis via salvage pathway;
CC       XMP from xanthine: step 1/1.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Potential).
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine
CC       phosphoribosyltransferase family. Xpt subfamily.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABN44544.1; Type=Erroneous initiation;
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DR   EMBL; CP000387; ABN44544.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_001035094.1; NC_009009.1.
DR   ProteinModelPortal; A3CMY9; -.
DR   SMR; A3CMY9; 1-190.
DR   STRING; 388919.SSA_1134; -.
DR   EnsemblBacteria; ABN44544; ABN44544; SSA_1134.
DR   GeneID; 4808079; -.
DR   KEGG; ssa:SSA_1134; -.
DR   PATRIC; 19769234; VBIStrSan33173_1078.
DR   eggNOG; COG0503; -.
DR   HOGENOM; HOG000036777; -.
DR   KO; K03816; -.
DR   ProtClustDB; PRK09219; -.
DR   BioCyc; SSAN388919:GHEN-1116-MONOMER; -.
DR   UniPathway; UPA00602; UER00658.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000310; F:xanthine phosphoribosyltransferase activity; IEA:HAMAP.
DR   GO; GO:0006166; P:purine ribonucleoside salvage; IEA:HAMAP.
DR   GO; GO:0046110; P:xanthine metabolic process; IEA:InterPro.
DR   GO; GO:0032265; P:XMP salvage; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_01184; XPRTase; 1; -.
DR   InterPro; IPR000836; PRibTrfase_dom.
DR   InterPro; IPR010079; Xanthine_PRibTrfase.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   TIGRFAMs; TIGR01744; XPRTase; 1.
DR   PROSITE; PS00103; PUR_PYR_PR_TRANSFER; FALSE_NEG.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage;
KW   Transferase.
FT   CHAIN         1    193       Xanthine phosphoribosyltransferase.
FT                                /FTId=PRO_0000339776.
FT   REGION      128    132       5-phospho-alpha-D-ribose 1-diphosphate
FT                                binding (By similarity).
FT   BINDING      20     20       Xanthine; via amide nitrogen and carbonyl
FT                                oxygen (By similarity).
FT   BINDING      27     27       Xanthine (By similarity).
FT   BINDING     156    156       Xanthine (By similarity).
SQ   SEQUENCE   193 AA;  20823 MW;  DBAF9B098FF8C97F CRC64;
     MKKLEERILR DGQVLGENIL KVDSFLTHQV DFSLMKEIGQ VFAEAVKDAG ITKVVTIEAS
     GIAPAVYVAE ALGLPMIFAK KAKNITMTEG ILTAEVYSFT KQVTSTVSIA GKFLNSDDKV
     LIIDDFLANG QAAKGLITII EQAGAQIEAV GIVIEKSFQD GRQLLETAGY RVLSLARIAG
     FEKGQIVFTE ADI
//
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