XPT_BACFN
ID XPT_BACFN Reviewed; 189 AA.
AC Q5LEQ1;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=BF1699;
OS Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019
OS / NCTC 9343 / Onslow).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=272559;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / NCTC 9343 / Onslow;
RX PubMed=15746427; DOI=10.1126/science.1107008;
RA Cerdeno-Tarraga A.-M., Patrick S., Crossman L.C., Blakely G., Abratt V.,
RA Lennard N., Poxton I., Duerden B., Harris B., Quail M.A., Barron A.,
RA Clark L., Corton C., Doggett J., Holden M.T.G., Larke N., Line A., Lord A.,
RA Norbertczak H., Ormond D., Price C., Rabbinowitsch E., Woodward J.,
RA Barrell B.G., Parkhill J.;
RT "Extensive DNA inversions in the B. fragilis genome control variable gene
RT expression.";
RL Science 307:1463-1465(2005).
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; CR626927; CAH07399.1; -; Genomic_DNA.
DR RefSeq; WP_005786581.1; NC_003228.3.
DR AlphaFoldDB; Q5LEQ1; -.
DR SMR; Q5LEQ1; -.
DR STRING; 272559.BF9343_1618; -.
DR EnsemblBacteria; CAH07399; CAH07399; BF9343_1618.
DR GeneID; 66329479; -.
DR KEGG; bfs:BF9343_1618; -.
DR eggNOG; COG0503; Bacteria.
DR HOGENOM; CLU_099015_0_0_10; -.
DR OMA; HQVDPVL; -.
DR OrthoDB; 1532478at2; -.
DR UniPathway; UPA00602; UER00658.
DR Proteomes; UP000006731; 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 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..189
FT /note="Xanthine phosphoribosyltransferase"
FT /id="PRO_0000339671"
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 127..131
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 155
FT /ligand="xanthine"
FT /ligand_id="ChEBI:CHEBI:17712"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01184"
SQ SEQUENCE 189 AA; 20933 MW; A1EE58DC45FF7CEA CRC64;
MQLLKKRILQ DGKCYEGGIL KVDSFINHQM DPVLMKSIGV EFVRLFAGTN VNKIMTIEAS
GIAPAIMTGY LMDLPVVFAK KKSPRTIQNA LSTTVHSFTK DRDYEVVISS DFLTPKDNVL
FVDDFLAYGN AALGVIDLIK QSGANLVGMG FIIEKAFQNG RKTLEERGVR VESLAIIEDL
SNCRITIKD