ID   XPT_ALKHC               Reviewed;         198 AA.
AC   Q9KCQ5;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 119.
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=BH1514;
OS   Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS   / JCM 9153 / C-125) (Bacillus halodurans).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=272558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA   Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA   Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT   "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT   and genomic sequence comparison with Bacillus subtilis.";
RL   Nucleic Acids Res. 28:4317-4331(2000).
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; BA000004; BAB05233.1; -; Genomic_DNA.
DR   PIR; B83839; B83839.
DR   RefSeq; WP_010897679.1; NC_002570.2.
DR   AlphaFoldDB; Q9KCQ5; -.
DR   SMR; Q9KCQ5; -.
DR   STRING; 272558.10174131; -.
DR   EnsemblBacteria; BAB05233; BAB05233; BAB05233.
DR   KEGG; bha:BH1514; -.
DR   eggNOG; COG0503; Bacteria.
DR   HOGENOM; CLU_099015_0_0_9; -.
DR   OMA; HQVDPVL; -.
DR   OrthoDB; 1532478at2; -.
DR   UniPathway; UPA00602; UER00658.
DR   Proteomes; UP000001258; 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..198
FT                   /note="Xanthine phosphoribosyltransferase"
FT                   /id="PRO_0000339665"
FT   BINDING         20
FT                   /ligand="xanthine"
FT                   /ligand_id="ChEBI:CHEBI:17712"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01184"
FT   BINDING         27
FT                   /ligand="xanthine"
FT                   /ligand_id="ChEBI:CHEBI:17712"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01184"
FT   BINDING         128..132
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         156
FT                   /ligand="xanthine"
FT                   /ligand_id="ChEBI:CHEBI:17712"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01184"
SQ   SEQUENCE   198 AA;  22054 MW;  08CD7A1E89E4509F CRC64;
     MESLKQAIRE RGNVLSDTVL KVDSFLNHQV DPKLINEIGQ AFAERFKNEG ITKVLTIESS
     GIAPSLVVAT HLGVPFIFAR KKKPLTMTDN VYRSQVYSFT KQETNEITVS KDLLHADDRV
     LIIDDFLANG QAAFGLCEIV EQAGAQVVGF GIVIEKSFQD GRKKLTDKGY RVESLARIQS
     FKNGTVQFVD EFVTQLSK