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Database: UniProt
Entry: W6RZY7_9CLOT
LinkDB: W6RZY7_9CLOT
Original site: W6RZY7_9CLOT 
ID   W6RZY7_9CLOT            Unreviewed;       189 AA.
AC   W6RZY7;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 44.
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:CDM67582.1};
GN   ORFNames=CM240_0415 {ECO:0000313|EMBL:CDM67582.1};
OS   Clostridium bornimense.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1216932 {ECO:0000313|EMBL:CDM67582.1, ECO:0000313|Proteomes:UP000019426};
RN   [1] {ECO:0000313|EMBL:CDM67582.1, ECO:0000313|Proteomes:UP000019426}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M2/40 {ECO:0000313|Proteomes:UP000019426};
RA   Wibberg D., Puehler A., Schlueter A.;
RT   "Complete genome sequence of Clostridum sp. M2/40.";
RL   Submitted (NOV-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}.
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DR   EMBL; HG917868; CDM67582.1; -; Genomic_DNA.
DR   RefSeq; WP_044036034.1; NZ_HG917868.1.
DR   AlphaFoldDB; W6RZY7; -.
DR   STRING; 1216932.CM240_0415; -.
DR   KEGG; clt:CM240_0415; -.
DR   PATRIC; fig|1216932.3.peg.399; -.
DR   eggNOG; COG0503; Bacteria.
DR   HOGENOM; CLU_099015_0_0_9; -.
DR   OrthoDB; 9790678at2; -.
DR   UniPathway; UPA00602; UER00658.
DR   Proteomes; UP000019426; Chromosome 1.
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; XANTHINE 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|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW   Rule:MF_01184}; Purine salvage {ECO:0000256|HAMAP-Rule:MF_01184};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019426};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01184, ECO:0000313|EMBL:CDM67582.1}.
FT   DOMAIN          44..162
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   189 AA;  21183 MW;  1B4CE784B167ED27 CRC64;
     MELLKKRILD EGKALSENVL KVDSFLNHGV DAKLMYEIGT EFKNYFEKHN VTKIFTIESS
     GIAPTVMTAM QMELPMVTLK KQSSKILNGE VYQTTVHSFT KSLDYQLTLS KKYISEDDNI
     LIIDDFLANG EAALGAIRLV EEAGAKVAGI GIVIEKSFQP GRKLLEDKGY DIYSLARIKK
     LGKDLIEFI
//
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