GenomeNet

Database: UniProt
Entry: R2S5E8_9ENTE
LinkDB: R2S5E8_9ENTE
Original site: R2S5E8_9ENTE 
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
//
DBGET integrated database retrieval system