ID R2S5E8_9ENTE Unreviewed; 193 AA.
AC R2S5E8;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
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=UAS_00907 {ECO:0000313|EMBL:EOH88146.1};
OS Enterococcus asini ATCC 700915.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1158606 {ECO:0000313|EMBL:EOH88146.1, ECO:0000313|Proteomes:UP000013777};
RN [1] {ECO:0000313|EMBL:EOH88146.1, ECO:0000313|Proteomes:UP000013777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700915 {ECO:0000313|EMBL:EOH88146.1,
RC ECO:0000313|Proteomes:UP000013777};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A.M., Gilmore M.S., Lebreton F., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Enterococcus asini ATCC_700915.";
RL Submitted (FEB-2013) 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:EOH88146.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJAP01000010; EOH88146.1; -; Genomic_DNA.
DR RefSeq; WP_010753555.1; NZ_KB946293.1.
DR AlphaFoldDB; R2S5E8; -.
DR STRING; 57732.RU94_GL001119; -.
DR GeneID; 78365950; -.
DR PATRIC; fig|1158606.3.peg.865; -.
DR eggNOG; COG0503; Bacteria.
DR HOGENOM; CLU_099015_0_0_9; -.
DR OrthoDB; 9790678at2; -.
DR UniPathway; UPA00602; UER00658.
DR Proteomes; UP000013777; 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:EOH88146.1};
KW Purine salvage {ECO:0000256|ARBA:ARBA00022726, ECO:0000256|HAMAP-
KW Rule:MF_01184}; Reference proteome {ECO:0000313|Proteomes:UP000013777};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01184}.
FT DOMAIN 36..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 193 AA; 21128 MW; 7943DFBE8B2795BE CRC64;
MKELRERIEA DGHVLGEGVL KVDSFVTHQV DPVLMEQIGR VFAKVFAEAK ITKVVTIEAS
GIAPALYAAQ YLQVPMVFAR KSKSLTMNEE LLTAEVYSFT KQVTSTISIS RKFLSAEDNV
LIVDDFLANG QAAKGLIELC RQAGAHVEGI GIVIEKSFQD GRELLEAMGL KVVSLARIKS
LSEGKVEFLE EDA
//