ID A0A1R1ER84_9BACL Unreviewed; 190 AA.
AC A0A1R1ER84;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=BK138_14030 {ECO:0000313|EMBL:OMF54308.1};
OS Paenibacillus rhizosphaerae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=297318 {ECO:0000313|EMBL:OMF54308.1, ECO:0000313|Proteomes:UP000187172};
RN [1] {ECO:0000313|EMBL:OMF54308.1, ECO:0000313|Proteomes:UP000187172}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL R5-0378 {ECO:0000313|EMBL:OMF54308.1,
RC ECO:0000313|Proteomes:UP000187172};
RA Beno S.M.;
RT "Paenibacillus species isolates.";
RL Submitted (NOV-2016) 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:OMF54308.1}.
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DR EMBL; MRTP01000003; OMF54308.1; -; Genomic_DNA.
DR RefSeq; WP_076170214.1; NZ_MRTP01000003.1.
DR AlphaFoldDB; A0A1R1ER84; -.
DR STRING; 297318.BK138_14030; -.
DR UniPathway; UPA00602; UER00658.
DR Proteomes; UP000187172; 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:OMF54308.1};
KW Purine salvage {ECO:0000256|ARBA:ARBA00022726, ECO:0000256|HAMAP-
KW Rule:MF_01184}; Reference proteome {ECO:0000313|Proteomes:UP000187172};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01184}.
FT DOMAIN 51..156
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 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 190 AA; 20698 MW; F8EB43660598272E CRC64;
MDKLKERILQ EGVIVSDQVL NLDGLLNHQV DPQLTMEMGK EFASRFAEAG VTRVVTVESS
GIAVAFATAY ELGVPLVFAR RKKTLLADPD ALCERVPSFT KGIVTDIMLS RHYISEQDKV
LFIDDIIANG DAARGLIKII ERSGAELVGL GVVIEKCFQA GARTIREQGI SIEPLVRIQS
LEGGVITFAD
//
