(data stored in ACNUC7421 zone)

SWISSPROT: XPT_PSEU2

ID   XPT_PSEU2               Reviewed;         189 AA.
AC   Q500M2;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   08-MAY-2019, entry version 87.
DE   RecName: Full=Xanthine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01184};
DE            Short=XPRTase {ECO:0000255|HAMAP-Rule:MF_01184};
DE            EC=2.4.2.22 {ECO:0000255|HAMAP-Rule:MF_01184};
GN   Name=xpt {ECO:0000255|HAMAP-Rule:MF_01184};
GN   OrderedLocusNames=Psyr_0076;
OS   Pseudomonas syringae pv. syringae (strain B728a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=205918;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B728a;
RX   PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA   Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA   Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA   Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA   Kyrpides N.C., Ivanova N., Lindow S.E.;
RT   "Comparison of the complete genome sequences of Pseudomonas syringae
RT   pv. syringae B728a and pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
CC   -!- FUNCTION: Converts the preformed base xanthine, a product of
CC       nucleic acid breakdown, to xanthosine 5'-monophosphate (XMP), so
CC       it can be reused for RNA or DNA synthesis. {ECO:0000255|HAMAP-
CC       Rule:MF_01184}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=diphosphate + XMP = 5-phospho-alpha-D-ribose 1-
CC         diphosphate + xanthine; Xref=Rhea:RHEA:10800, ChEBI:CHEBI:17712,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57464, ChEBI:CHEBI:58017;
CC         EC=2.4.2.22; Evidence={ECO:0000255|HAMAP-Rule:MF_01184};
CC   -!- PATHWAY: Purine metabolism; XMP biosynthesis via salvage pathway;
CC       XMP from xanthine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01184}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01184}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01184}.
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine
CC       phosphoribosyltransferase family. Xpt subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01184}.
DR   EMBL; CP000075; AAY35150.1; -; Genomic_DNA.
DR   RefSeq; WP_003401587.1; NC_007005.1.
DR   RefSeq; YP_233188.1; NC_007005.1.
DR   SMR; Q500M2; -.
DR   STRING; 205918.Psyr_0076; -.
DR   EnsemblBacteria; AAY35150; AAY35150; Psyr_0076.
DR   GeneID; 3365551; -.
DR   KEGG; psb:Psyr_0076; -.
DR   PATRIC; fig|205918.7.peg.74; -.
DR   eggNOG; ENOG4108UPS; Bacteria.
DR   eggNOG; COG0503; LUCA.
DR   HOGENOM; HOG000036777; -.
DR   KO; K03816; -.
DR   OMA; HQVDPVL; -.
DR   BioCyc; PSYR205918:G1G4J-76-MONOMER; -.
DR   UniPathway; UPA00602; UER00658.
DR   Proteomes; UP000000426; Chromosome.
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   HAMAP; MF_01184; XPRTase; 1.
DR   InterPro; IPR000836; PRibTrfase_dom.
DR   InterPro; IPR029057; PRTase-like.
DR   InterPro; IPR010079; Xanthine_PRibTrfase.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   SUPFAM; SSF53271; SSF53271; 1.
DR   TIGRFAMs; TIGR01744; XPRTase; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q500M2.
DR   SWISS-2DPAGE; Q500M2.
KW   Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage;
KW   Transferase.
FT   CHAIN         1    189       Xanthine phosphoribosyltransferase.
FT                                /FTId=PRO_0000339739.
FT   REGION      128    132       5-phospho-alpha-D-ribose 1-diphosphate
FT                                binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01184}.
FT   BINDING      20     20       Xanthine; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_01184}.
FT   BINDING      27     27       Xanthine. {ECO:0000255|HAMAP-
FT                                Rule:MF_01184}.
FT   BINDING     156    156       Xanthine. {ECO:0000255|HAMAP-
FT                                Rule:MF_01184}.
SQ   SEQUENCE   189 AA;  20147 MW;  4DC178E982BFCD66 CRC64;
     MEALHKKIRE EGIVLSDQVL KVDAFLNHQI DPALMKEIGD EFARLFADAG VTKIVTIEAS
     GIAPAVMAGL NMGVPVIFAR KHQSLTLTEN LLTASVYSFT KQVESTVAIS PRHLSSDDNV
     LIIDDFLANG KASQALISII KQAGATVAGL GIVIEKSFQG GRAELDAQGY RVESLARVES
     LAGGVVTFK
//

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