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Database: UniProt
Entry: R6CWR1_9FIRM
LinkDB: R6CWR1_9FIRM
Original site: R6CWR1_9FIRM 
ID   R6CWR1_9FIRM            Unreviewed;       192 AA.
AC   R6CWR1;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=Xanthine phosphoribosyltransferase {ECO:0000256|HAMAP-Rule:MF_01184};
DE            Short=XPRTase {ECO:0000256|HAMAP-Rule:MF_01184};
DE            EC=2.4.2.22 {ECO:0000256|HAMAP-Rule:MF_01184};
GN   Name=xpt {ECO:0000256|HAMAP-Rule:MF_01184};
GN   ORFNames=BN516_01048 {ECO:0000313|EMBL:CDA81018.1};
OS   Firmicutes bacterium CAG:176.
OC   Bacteria; Bacillota.
OX   NCBI_TaxID=1263007 {ECO:0000313|EMBL:CDA81018.1, ECO:0000313|Proteomes:UP000017932};
RN   [1] {ECO:0000313|EMBL:CDA81018.1, ECO:0000313|Proteomes:UP000017932}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:176 {ECO:0000313|Proteomes:UP000017932};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-Rule:MF_01184};
CC   -!- PATHWAY: Purine metabolism; XMP biosynthesis via salvage pathway; XMP
CC       from xanthine: step 1/1. {ECO:0000256|HAMAP-Rule:MF_01184}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01184}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01184}.
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC       family. Xpt subfamily. {ECO:0000256|HAMAP-Rule:MF_01184}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01184}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CDA81018.1}.
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DR   EMBL; CBCO010000009; CDA81018.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6CWR1; -.
DR   UniPathway; UPA00602; UER00658.
DR   Proteomes; UP000017932; Unassembled WGS sequence.
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   NCBIfam; TIGR01744; XPRTase; 1.
DR   PANTHER; PTHR43864; HYPOXANTHINE/GUANINE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR43864:SF1; HYPOXANTHINE_GUANINE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   SUPFAM; SSF53271; PRTase-like; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01184};
KW   Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_01184,
KW   ECO:0000313|EMBL:CDA81018.1};
KW   Purine salvage {ECO:0000256|ARBA:ARBA00022726, ECO:0000256|HAMAP-
KW   Rule:MF_01184}; Reference proteome {ECO:0000313|Proteomes:UP000017932};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01184}.
FT   DOMAIN          39..157
FT                   /note="Phosphoribosyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00156"
FT   BINDING         27
FT                   /ligand="xanthine"
FT                   /ligand_id="ChEBI:CHEBI:17712"
FT                   /evidence="ECO:0000256|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:0000256|HAMAP-Rule:MF_01184"
FT   BINDING         156
FT                   /ligand="xanthine"
FT                   /ligand_id="ChEBI:CHEBI:17712"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01184"
SQ   SEQUENCE   192 AA;  21303 MW;  03D1762238C29985 CRC64;
     MQQLKERILR EGRVLPGNII KVDGFLNHRV DTALMRDLAD EFAKYFDVKN ITMVLTAEAS
     GIALATICAE RYGVPMVFAK KAKSDNIEGG LYQSDIFSYT YKKKVTLLVS QDWITKDDKV
     LIIDDFMAKG YAMRGLIDIV NKAGAQLAGI GVAVEKGFQD GGDSLRREGY PIKSLAVIDS
     AENGVIRFRE DD
//
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