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Database: UniProt
Entry: A0A1F2PGE7_9FIRM
LinkDB: A0A1F2PGE7_9FIRM
Original site: A0A1F2PGE7_9FIRM 
ID   A0A1F2PGE7_9FIRM        Unreviewed;       197 AA.
AC   A0A1F2PGE7;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
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   ECO:0000313|EMBL:OFV69942.1};
GN   ORFNames=ACWI_25840 {ECO:0000313|EMBL:OFV69942.1}, FXB42_08375
GN   {ECO:0000313|EMBL:TYC85873.1};
OS   Acetobacterium wieringae.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC   Acetobacterium.
OX   NCBI_TaxID=52694 {ECO:0000313|EMBL:OFV69942.1, ECO:0000313|Proteomes:UP000176244};
RN   [1] {ECO:0000313|EMBL:OFV69942.1, ECO:0000313|Proteomes:UP000176244}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1911 {ECO:0000313|EMBL:OFV69942.1,
RC   ECO:0000313|Proteomes:UP000176244};
RA   Poehlein A., Bengelsdorf F.R., Schiel-Bengelsdorf B., Duerre P., Daniel R.;
RT   "Genome sequence of Acetobacterium wieringae DSM 1911.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:TYC85873.1, ECO:0000313|Proteomes:UP000322619}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JM {ECO:0000313|EMBL:TYC85873.1,
RC   ECO:0000313|Proteomes:UP000322619};
RA   Antares A.L., Moreira J., Diender M., Parshina S.N., Stams A.J.M.,
RA   Alves M., Alves J.I., Sousa D.Z.;
RT   "Isolation and enrichment of carboxydotrophic bacteria from anaerobic
RT   sludge for the production of bio-based chemicals from syngas.";
RL   Submitted (AUG-2019) 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: 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:OFV69942.1}.
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DR   EMBL; LKEU01000035; OFV69942.1; -; Genomic_DNA.
DR   EMBL; VSLA01000013; TYC85873.1; -; Genomic_DNA.
DR   RefSeq; WP_070371854.1; NZ_VSLA01000013.1.
DR   AlphaFoldDB; A0A1F2PGE7; -.
DR   STRING; 52694.ACWI_25840; -.
DR   OrthoDB; 9790678at2; -.
DR   UniPathway; UPA00602; UER00658.
DR   Proteomes; UP000176244; Unassembled WGS sequence.
DR   Proteomes; UP000322619; 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:OFV69942.1};
KW   Purine salvage {ECO:0000256|ARBA:ARBA00022726, ECO:0000256|HAMAP-
KW   Rule:MF_01184};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01184}.
FT   DOMAIN          48..158
FT                   /note="Phosphoribosyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00156"
FT   BINDING         20
FT                   /ligand="xanthine"
FT                   /ligand_id="ChEBI:CHEBI:17712"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01184"
FT   BINDING         27
FT                   /ligand="xanthine"
FT                   /ligand_id="ChEBI:CHEBI:17712"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01184"
FT   BINDING         129..133
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         157
FT                   /ligand="xanthine"
FT                   /ligand_id="ChEBI:CHEBI:17712"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01184"
SQ   SEQUENCE   197 AA;  21826 MW;  BE386D621BD70440 CRC64;
     MELLEEKIRQ EGLVKGQGIL KVDSFLNHQL DVKLFEEMGK VFAKRFAGEG VNKILTIETS
     GIAIATSTSR YFDYCPVVFG KKYVSLNLDE EIYSSDVYSY TKQQAYKIMV SKKYLNPTDR
     ILIIDDFLAN GKAVEALIDL INQAGATLVG VGIAIEKGFQ DGGALIREQG VALESLAIID
     DMSKEKGIIF RDQSGKK
//
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