{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P45563","secondaryAccessions":["P77325"],"uniProtkbId":"XAPA_ECOLI","entryAudit":{"firstPublicDate":"1995-11-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1997-11-01","entryVersion":176,"sequenceVersion":2},"annotationScore":5.0,"organism":{"scientificName":"Escherichia coli (strain K12)","taxonId":83333,"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Purine nucleoside phosphorylase 2"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10400599"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15808857"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17151449"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3042752"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7007809"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7559336"}],"value":"2.4.2.1"}]},"alternativeNames":[{"fullName":{"value":"Inosine-guanosine phosphorylase"}},{"fullName":{"value":"Purine nucleoside phosphorylase II"},"shortNames":[{"value":"PNP II"}]},{"fullName":{"value":"Xanthosine phosphorylase"}}]},"genes":[{"geneName":{"value":"xapA"},"synonyms":[{"value":"pndA"}],"orderedLocusNames":[{"value":"b2407"},{"value":"JW2398"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15808857"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3042752"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7007808"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7007809"}],"value":"The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. This protein can degrade all purine nucleosides including xanthosine, inosine and guanosine, but cannot cleave adenosine, deoxyadenosine or hypoxanthine arabinoside. Has a preference for the neutral over the monoanionic form of xanthosine"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a purine D-ribonucleoside + phosphate = a purine nucleobase + alpha-D-ribose 1-phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:19805"},{"database":"ChEBI","id":"CHEBI:26386"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57720"},{"database":"ChEBI","id":"CHEBI:142355"}],"ecNumber":"2.4.2.1","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10400599"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15808857"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17151449"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3042752"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7007809"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7559336"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3042752"}],"value":"Rapidly inactivated by p-chloromercuriphenylsulfonic acid (p-CMB). Dithiothreitol incubation restores the activity"}],"commentType":"ACTIVITY REGULATION"},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"maximumVelocities":[{"velocity":8.7,"unit":"umol/min/mg","enzyme":"enzyme with xanthosine as substrate (at 25 degrees Celsius and pH 7.1)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15808857"}]},{"velocity":14.2,"unit":"umol/min/mg","enzyme":"enzyme with guanosine as substrate (at 25 degrees Celsius and pH 7.1)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15808857"}]},{"velocity":11.9,"unit":"umol/min/mg","enzyme":"enzyme with inosine as substrate (at 25 degrees Celsius and pH 7.1)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15808857"}]}],"michaelisConstants":[{"constant":51.0,"unit":"uM","substrate":"xanthosine (at pH 7.0)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3042752"}]},{"constant":72.0,"unit":"uM","substrate":"xanthosine (at 25 degrees Celsius and pH 7.1)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15808857"}]},{"constant":110.0,"unit":"uM","substrate":"guanosine (at pH 7.0)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3042752"}]},{"constant":155.0,"unit":"uM","substrate":"guanosine (at 25 degrees Celsius and pH 7.1)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15808857"}]},{"constant":963.0,"unit":"uM","substrate":"inosine (at 25 degrees Celsius and pH 7.1)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15808857"}]},{"constant":340.0,"unit":"uM","substrate":"inosine (at 25 degrees Celsius and pH 7.0)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3042752"}]},{"constant":62.0,"unit":"uM","substrate":"2'-deoxyinosine (at 25 degrees Celsius and pH 7.0)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3042752"}]},{"constant":600.0,"unit":"uM","substrate":"5'-deoxyinosine (at 25 degrees Celsius and pH 7.0)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3042752"}]},{"constant":2600.0,"unit":"uM","substrate":"2',3'-dideoxyinosine (at 25 degrees Celsius and pH 7.0)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3042752"}]},{"constant":44.0,"unit":"uM","substrate":"2'-deoxyguanosine (at 25 degrees Celsius and pH 7.0)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3042752"}]},{"constant":3.3,"unit":"uM","substrate":"hypoxanthine (at 25 degrees Celsius and pH 7.0)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3042752"}]},{"constant":4.1,"unit":"uM","substrate":"guanine (at 25 degrees Celsius and pH 7.0)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3042752"}]},{"constant":760.0,"unit":"uM","substrate":"phosphate (at 25 degrees Celsius and pH 7.0)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3042752"}]},{"constant":59.0,"unit":"uM","substrate":"alpha-D-ribose 1-phosphate (at 25 degrees Celsius and pH 7.0)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3042752"}]},{"constant":58.0,"unit":"uM","substrate":"alpha-D-2'-deoxyribose 1-phosphate (at 25 degrees Celsius and pH 7.0)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3042752"}]}]},"phDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15808857"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3042752"}],"value":"Optimum pH is 6.5-7.5 with guanosine as substrate. At pH higher than 7.5, there is a marked reduction in reaction rate and a steep drop at pH higher than 9. Below pH 6.5, there is a dramatic decrease in activity reaching virtually zero at pH 6.0. With xanthosine as substrate, the pH optimum is 5.8-7.2. In the reverse reaction with guanine or xanthine as substrates, the pH optimum is 6.5-8.0. The pH dependence of inosine cleavage does not vary between pH 6 and 8. Maximal activity with inosine as substrate is observed at pH 6.6."}]},"temperatureDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15808857"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3042752"}],"value":"The half-life at 45 degrees Celsius between pH 5 and 8 is 5 to 9 minutes."}]}},{"texts":[{"value":"Purine metabolism; xanthosine degradation"}],"commentType":"PATHWAY"},{"texts":[{"value":"Purine metabolism; purine nucleoside salvage"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15808857"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7007809"}],"value":"Hexamer. Dimer of trimers"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10400599"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7007809"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7559336"}],"value":"By xanthosine and to a lesser extent by deoxyinosine. Full expression requires XapR-xanthosine DNA-binding transcriptional activator"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17151449"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7559336"}],"value":"Does not grow on xanthosine. Slightly increases inosine productivity compared to wild-type (5.6 g/l of inosine versus 4.6 g/l, respectively, from 40 g/l of glucose)"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the PNP/MTAP phosphorylase family"}],"commentType":"SIMILARITY"},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Frameshift","sequence":"CAA52049.1","evidences":[{"evidenceCode":"ECO:0000305"}]}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":277,"modifier":"EXACT"}},"description":"Purine nucleoside phosphorylase 2","featureId":"PRO_0000184555"},{"type":"Binding site","location":{"start":{"value":65,"modifier":"EXACT"},"end":{"value":65,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:43474"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15808857"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1YQQ"}],"ligand":{"name":"phosphate","id":"ChEBI:CHEBI:43474"}},{"type":"Binding site","location":{"start":{"value":85,"modifier":"EXACT"},"end":{"value":87,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:43474"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15808857"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1YQQ"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1YQU"}],"ligand":{"name":"phosphate","id":"ChEBI:CHEBI:43474"}},{"type":"Binding site","location":{"start":{"value":117,"modifier":"EXACT"},"end":{"value":117,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:43474"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15808857"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1YQQ"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1YQU"}],"ligand":{"name":"phosphate","id":"ChEBI:CHEBI:43474"}},{"type":"Binding site","location":{"start":{"value":197,"modifier":"EXACT"},"end":{"value":197,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:142355"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15808857"}],"ligand":{"name":"a purine D-ribonucleoside","id":"ChEBI:CHEBI:142355"}},{"type":"Binding site","location":{"start":{"value":216,"modifier":"EXACT"},"end":{"value":216,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:43474"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15808857"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1YQQ"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1YQU"}],"ligand":{"name":"phosphate","id":"ChEBI:CHEBI:43474"}},{"type":"Binding site","location":{"start":{"value":239,"modifier":"EXACT"},"end":{"value":239,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:142355"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15808857"}],"ligand":{"name":"a purine D-ribonucleoside","id":"ChEBI:CHEBI:142355"}},{"type":"Mutagenesis","location":{"start":{"value":191,"modifier":"EXACT"},"end":{"value":191,"modifier":"EXACT"}},"description":"No detectable activity with xanthosine as substrate, but largely retains its activity against other substrates, namely inosine and guanosine, although with altered affinities, higher and lower respectively, and clearly reduced maximal velocities for both.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15808857"}],"alternativeSequence":{"originalSequence":"Y","alternativeSequences":["L"]}},{"type":"Mutagenesis","location":{"start":{"value":239,"modifier":"EXACT"},"end":{"value":239,"modifier":"EXACT"}},"description":"Catalyzes the phosphorolysis of adenosine with moderate efficiency, and essentially has lost all activity against the 6-oxo-purine substrates xanthosine, inosine and guanosine.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15808857"}],"alternativeSequence":{"originalSequence":"N","alternativeSequences":["D"]}},{"type":"Sequence conflict","location":{"start":{"value":144,"modifier":"EXACT"},"end":{"value":144,"modifier":"EXACT"}},"description":"in Ref. 1; CAA52049","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"P","alternativeSequences":["A"]}},{"type":"Sequence conflict","location":{"start":{"value":261,"modifier":"EXACT"},"end":{"value":261,"modifier":"EXACT"}},"description":"in Ref. 1; CAA52049","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"S","alternativeSequences":["H"]}},{"type":"Sequence conflict","location":{"start":{"value":265,"modifier":"EXACT"},"end":{"value":265,"modifier":"EXACT"}},"description":"in Ref. 1; CAA52049","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"F","alternativeSequences":["L"]}},{"type":"Helix","location":{"start":{"value":9,"modifier":"EXACT"},"end":{"value":20,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1YQQ"}]},{"type":"Beta strand","location":{"start":{"value":27,"modifier":"EXACT"},"end":{"value":32,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1YQQ"}]},{"type":"Helix","location":{"start":{"value":36,"modifier":"EXACT"},"end":{"value":42,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1YQQ"}]},{"type":"Beta strand","location":{"start":{"value":44,"modifier":"EXACT"},"end":{"value":50,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1YQQ"}]},{"type":"Helix","location":{"start":{"value":51,"modifier":"EXACT"},"end":{"value":53,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1YQQ"}]},{"type":"Beta strand","location":{"start":{"value":68,"modifier":"EXACT"},"end":{"value":74,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1YQQ"}]},{"type":"Beta strand","location":{"start":{"value":77,"modifier":"EXACT"},"end":{"value":84,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1YQQ"}]},{"type":"Helix","location":{"start":{"value":88,"modifier":"EXACT"},"end":{"value":90,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1YQQ"}]},{"type":"Turn","location":{"start":{"value":94,"modifier":"EXACT"},"end":{"value":97,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1YQQ"}]},{"type":"Helix","location":{"start":{"value":98,"modifier":"EXACT"},"end":{"value":107,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1YQQ"}]},{"type":"Beta strand","location":{"start":{"value":110,"modifier":"EXACT"},"end":{"value":121,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1YQQ"}]},{"type":"Beta strand","location":{"start":{"value":130,"modifier":"EXACT"},"end":{"value":137,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1YQQ"}]},{"type":"Beta strand","location":{"start":{"value":140,"modifier":"EXACT"},"end":{"value":142,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1YQQ"}]},{"type":"Turn","location":{"start":{"value":151,"modifier":"EXACT"},"end":{"value":153,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1YQQ"}]},{"type":"Beta strand","location":{"start":{"value":156,"modifier":"EXACT"},"end":{"value":158,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1YQQ"}]},{"type":"Helix","location":{"start":{"value":166,"modifier":"EXACT"},"end":{"value":177,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1YQQ"}]},{"type":"Turn","location":{"start":{"value":178,"modifier":"EXACT"},"end":{"value":180,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1YQQ"}]},{"type":"Beta strand","location":{"start":{"value":183,"modifier":"EXACT"},"end":{"value":190,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1YQQ"}]},{"type":"Helix","location":{"start":{"value":196,"modifier":"EXACT"},"end":{"value":198,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1YQQ"}]},{"type":"Helix","location":{"start":{"value":199,"modifier":"EXACT"},"end":{"value":207,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1YQQ"}]},{"type":"Beta strand","location":{"start":{"value":211,"modifier":"EXACT"},"end":{"value":217,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1YQQ"}]},{"type":"Helix","location":{"start":{"value":218,"modifier":"EXACT"},"end":{"value":226,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1YQQ"}]},{"type":"Beta strand","location":{"start":{"value":230,"modifier":"EXACT"},"end":{"value":240,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1YQQ"}]},{"type":"Beta strand","location":{"start":{"value":244,"modifier":"EXACT"},"end":{"value":246,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1YQQ"}]},{"type":"Helix","location":{"start":{"value":247,"modifier":"EXACT"},"end":{"value":249,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1YQQ"}]},{"type":"Helix","location":{"start":{"value":251,"modifier":"EXACT"},"end":{"value":256,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1YQQ"}]},{"type":"Helix","location":{"start":{"value":257,"modifier":"EXACT"},"end":{"value":259,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1YQQ"}]},{"type":"Helix","location":{"start":{"value":262,"modifier":"EXACT"},"end":{"value":276,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1YQQ"}]}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0328","category":"Molecular function","name":"Glycosyltransferase"},{"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"7559336","citationType":"journal article","authors":["Seeger C.","Poulsen C.","Dandanell G."],"citationCrossReferences":[{"database":"PubMed","id":"7559336"},{"database":"DOI","id":"10.1128/jb.177.19.5506-5516.1995"}],"title":"Identification and characterization of genes (xapA, xapB, and xapR) involved in xanthosine catabolism in Escherichia coli.","publicationDate":"1995","journal":"J. Bacteriol.","firstPage":"5506","lastPage":"5516","volume":"177"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","CATALYTIC ACTIVITY","INDUCTION","DISRUPTION PHENOTYPE"],"referenceComments":[{"value":"K12","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"9205837","citationType":"journal article","authors":["Yamamoto Y.","Aiba H.","Baba T.","Hayashi K.","Inada T.","Isono K.","Itoh T.","Kimura S.","Kitagawa M.","Makino K.","Miki T.","Mitsuhashi N.","Mizobuchi K.","Mori H.","Nakade S.","Nakamura Y.","Nashimoto H.","Oshima T.","Oyama S.","Saito N.","Sampei G.","Satoh Y.","Sivasundaram S.","Tagami H.","Takahashi H.","Takeda J.","Takemoto K.","Uehara K.","Wada C.","Yamagata S.","Horiuchi T."],"citationCrossReferences":[{"database":"PubMed","id":"9205837"},{"database":"DOI","id":"10.1093/dnares/4.2.91"}],"title":"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features.","publicationDate":"1997","journal":"DNA Res.","firstPage":"91","lastPage":"113","volume":"4"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"value":"K12 / W3110 / ATCC 27325 / DSM 5911","type":"STRAIN"}]},{"referenceNumber":3,"citation":{"id":"9278503","citationType":"journal article","authors":["Blattner F.R.","Plunkett G. III","Bloch C.A.","Perna N.T.","Burland V.","Riley M.","Collado-Vides J.","Glasner J.D.","Rode C.K.","Mayhew G.F.","Gregor J.","Davis N.W.","Kirkpatrick H.A.","Goeden M.A.","Rose D.J.","Mau B.","Shao Y."],"citationCrossReferences":[{"database":"PubMed","id":"9278503"},{"database":"DOI","id":"10.1126/science.277.5331.1453"}],"title":"The complete genome sequence of Escherichia coli K-12.","publicationDate":"1997","journal":"Science","firstPage":"1453","lastPage":"1462","volume":"277"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"value":"K12 / MG1655 / ATCC 47076","type":"STRAIN"}]},{"referenceNumber":4,"citation":{"id":"16738553","citationType":"journal article","authors":["Hayashi K.","Morooka N.","Yamamoto Y.","Fujita K.","Isono K.","Choi S.","Ohtsubo E.","Baba T.","Wanner B.L.","Mori H.","Horiuchi T."],"citationCrossReferences":[{"database":"PubMed","id":"16738553"},{"database":"DOI","id":"10.1038/msb4100049"}],"title":"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.","publicationDate":"2006","journal":"Mol. Syst. Biol.","firstPage":"E1","lastPage":"E5","volume":"2"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"value":"K12 / W3110 / ATCC 27325 / DSM 5911","type":"STRAIN"}]},{"referenceNumber":5,"citation":{"id":"7007808","citationType":"journal article","authors":["Buxton R.S.","Hammer-Jespersen K.","Valentin-Hansen P."],"citationCrossReferences":[{"database":"PubMed","id":"7007808"},{"database":"DOI","id":"10.1007/bf00425461"}],"title":"A second purine nucleoside phosphorylase in Escherichia coli K-12. I. Xanthosine phosphorylase regulatory mutants isolated as secondary-site revertants of a deoD mutant.","publicationDate":"1980","journal":"Mol. Gen. Genet.","firstPage":"331","lastPage":"340","volume":"179"},"referencePositions":["FUNCTION"],"referenceComments":[{"value":"K12","type":"STRAIN"}]},{"referenceNumber":6,"citation":{"id":"7007809","citationType":"journal article","authors":["Hammer-Jespersen K.","Buxton R.S.","Hansen T.D."],"citationCrossReferences":[{"database":"PubMed","id":"7007809"},{"database":"DOI","id":"10.1007/bf00425462"}],"title":"A second purine nucleoside phosphorylase in Escherichia coli K-12. II. Properties of xanthosine phosphorylase and its induction by xanthosine.","publicationDate":"1980","journal":"Mol. Gen. Genet.","firstPage":"341","lastPage":"348","volume":"179"},"referencePositions":["FUNCTION","CATALYTIC ACTIVITY","SUBSTRATE SPECIFICITY","SUBUNIT","INDUCTION"],"referenceComments":[{"value":"K12","type":"STRAIN"}]},{"referenceNumber":7,"citation":{"id":"3042752","citationType":"journal article","authors":["Koszalka G.W.","Vanhooke J.","Short S.A.","Hall W.W."],"citationCrossReferences":[{"database":"PubMed","id":"3042752"},{"database":"DOI","id":"10.1128/jb.170.8.3493-3498.1988"}],"title":"Purification and properties of inosine-guanosine phosphorylase from Escherichia coli K-12.","publicationDate":"1988","journal":"J. Bacteriol.","firstPage":"3493","lastPage":"3498","volume":"170"},"referencePositions":["FUNCTION","CATALYTIC ACTIVITY","SUBSTRATE SPECIFICITY","ACTIVITY REGULATION","BIOPHYSICOCHEMICAL PROPERTIES"],"referenceComments":[{"value":"K12","type":"STRAIN"}]},{"referenceNumber":8,"citation":{"id":"10400599","citationType":"journal article","authors":["Jorgensen C.","Dandanell G."],"citationCrossReferences":[{"database":"PubMed","id":"10400599"},{"database":"DOI","id":"10.1128/jb.181.14.4397-4403.1999"}],"title":"Isolation and characterization of mutations in the Escherichia coli regulatory protein XapR.","publicationDate":"1999","journal":"J. Bacteriol.","firstPage":"4397","lastPage":"4403","volume":"181"},"referencePositions":["CATALYTIC ACTIVITY","INDUCTION"]},{"referenceNumber":9,"citation":{"id":"17151449","citationType":"journal article","authors":["Shimaoka M.","Takenaka Y.","Mihara Y.","Kurahashi O.","Kawasaki H.","Matsui H."],"citationCrossReferences":[{"database":"PubMed","id":"17151449"},{"database":"DOI","id":"10.1271/bbb.60398"}],"title":"Effects of xapA and guaA disruption on inosine accumulation in Escherichia coli.","publicationDate":"2006","journal":"Biosci. Biotechnol. Biochem.","firstPage":"3069","lastPage":"3072","volume":"70"},"referencePositions":["CATALYTIC ACTIVITY","DISRUPTION PHENOTYPE"],"referenceComments":[{"value":"K12 / W3110 / ATCC 27325 / DSM 5911","type":"STRAIN"}]},{"referenceNumber":10,"citation":{"id":"15808857","citationType":"journal article","authors":["Dandanell G.","Szczepanowski R.H.","Kierdaszuk B.","Shugar D.","Bochtler M."],"citationCrossReferences":[{"database":"PubMed","id":"15808857"},{"database":"DOI","id":"10.1016/j.jmb.2005.02.019"}],"title":"Escherichia coli purine nucleoside phosphorylase II, the product of the xapA gene.","publicationDate":"2005","journal":"J. Mol. Biol.","firstPage":"113","lastPage":"125","volume":"348"},"referencePositions":["X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH GUANINE","XANTHINE AND PHOSPHATE","FUNCTION","CATALYTIC ACTIVITY","SUBSTRATE SPECIFICITY","BIOPHYSICOCHEMICAL PROPERTIES","SUBUNIT","MUTAGENESIS OF TYR-191 AND ASN-239"],"referenceComments":[{"value":"K12","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"X73828","properties":[{"key":"ProteinId","value":"CAA52049.1"},{"key":"Status","value":"ALT_FRAME"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"U00096","properties":[{"key":"ProteinId","value":"AAC75460.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"AP009048","properties":[{"key":"ProteinId","value":"BAA16275.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"F65014","properties":[{"key":"EntryName","value":"F65014"}]},{"database":"RefSeq","id":"NP_416902.1","properties":[{"key":"NucleotideSequenceId","value":"NC_000913.3"}]},{"database":"RefSeq","id":"WP_000084573.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP009789.1"}]},{"database":"PDB","id":"1YQQ","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.60 A"},{"key":"Chains","value":"A/B/C=1-277"}]},{"database":"PDB","id":"1YQU","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"3.10 A"},{"key":"Chains","value":"A/B/C=1-277"}]},{"database":"PDB","id":"1YR3","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"3.20 A"},{"key":"Chains","value":"A/B/C/D/E/F=1-277"}]},{"database":"PDBsum","id":"1YQQ","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"1YQU","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"1YR3","properties":[{"key":"Description","value":"-"}]},{"database":"AlphaFoldDB","id":"P45563","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P45563","properties":[{"key":"Description","value":"-"}]},{"database":"BioGRID","id":"4260565","properties":[{"key":"Interactions","value":"23"}]},{"database":"FunCoup","id":"P45563","properties":[{"key":"Number of interactors","value":"942"}]},{"database":"IntAct","id":"P45563","properties":[{"key":"Interactions","value":"4"}]},{"database":"STRING","id":"511145.b2407","properties":[{"key":"Description","value":"-"}]},{"database":"DrugBank","id":"DB02377","properties":[{"key":"GenericName","value":"Guanine"}]},{"database":"DrugBank","id":"DB02134","properties":[{"key":"GenericName","value":"Xanthine"}]},{"database":"PaxDb","id":"511145-b2407","properties":[{"key":"Description","value":"-"}]},{"database":"EnsemblBacteria","id":"AAC75460","properties":[{"key":"ProteinId","value":"AAC75460"},{"key":"GeneId","value":"b2407"}]},{"database":"GeneID","id":"946878","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ecj:JW2398","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"eco:b2407","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ecoc:C3026_13380","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|1411691.4.peg.4325","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"EchoBASE","id":"EB4152","properties":[{"key":"Description","value":"-"}]},{"database":"eggNOG","id":"COG0005","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"HOGENOM","id":"CLU_054456_1_0_6","properties":[{"key":"Description","value":"-"}]},{"database":"InParanoid","id":"P45563","properties":[{"key":"Description","value":"-"}]},{"database":"OMA","id":"EGVYAQF","properties":[{"key":"Fingerprint","value":"-"}]},{"database":"OrthoDB","id":"1523230at2","properties":[{"key":"Description","value":"-"}]},{"database":"PhylomeDB","id":"P45563","properties":[{"key":"Description","value":"-"}]},{"database":"BioCyc","id":"EcoCyc:XANTHOSINEPHOSPHORY-MONOMER","properties":[{"key":"Description","value":"-"}]},{"database":"BioCyc","id":"MetaCyc:XANTHOSINEPHOSPHORY-MONOMER","properties":[{"key":"Description","value":"-"}]},{"database":"BRENDA","id":"2.4.2.1","properties":[{"key":"OrganismId","value":"2026"}]},{"database":"UniPathway","id":"UPA00119","properties":[{"key":"RectionId","value":"-"}]},{"database":"UniPathway","id":"UPA00606","properties":[{"key":"RectionId","value":"-"}]},{"database":"EvolutionaryTrace","id":"P45563","properties":[{"key":"Description","value":"-"}]},{"database":"PRO","id":"PR:P45563","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000000625","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"AbasyAtlas","id":"P45563","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IDA:EcoliWiki"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"15808857"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IBA:GO_Central"}]},{"database":"GO","id":"GO:0047975","properties":[{"key":"GoTerm","value":"F:guanosine phosphorylase activity"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"15808857"},{"evidenceCode":"ECO:0000314","source":"PubMed","id":"3042752"}]},{"database":"GO","id":"GO:0042802","properties":[{"key":"GoTerm","value":"F:identical protein binding"},{"key":"GoEvidenceType","value":"IDA:EcoCyc"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"7007809"}]},{"database":"GO","id":"GO:0047724","properties":[{"key":"GoTerm","value":"F:inosine nucleosidase activity"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"15808857"},{"evidenceCode":"ECO:0000314","source":"PubMed","id":"17151449"},{"evidenceCode":"ECO:0000314","source":"PubMed","id":"3042752"}]},{"database":"GO","id":"GO:0004731","properties":[{"key":"GoTerm","value":"F:purine-nucleoside phosphorylase activity"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"10400599"},{"evidenceCode":"ECO:0000314","source":"PubMed","id":"17151449"},{"evidenceCode":"ECO:0000314","source":"PubMed","id":"3042752"},{"evidenceCode":"ECO:0000314","source":"PubMed","id":"7559336"}]},{"database":"GO","id":"GO:0006161","properties":[{"key":"GoTerm","value":"P:deoxyguanosine catabolic process"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"3042752"}]},{"database":"GO","id":"GO:0006149","properties":[{"key":"GoTerm","value":"P:deoxyinosine catabolic process"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"3042752"}]},{"database":"GO","id":"GO:0046115","properties":[{"key":"GoTerm","value":"P:guanosine catabolic process"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"15808857"},{"evidenceCode":"ECO:0000314","source":"PubMed","id":"3042752"}]},{"database":"GO","id":"GO:0006148","properties":[{"key":"GoTerm","value":"P:inosine catabolic process"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"15808857"},{"evidenceCode":"ECO:0000314","source":"PubMed","id":"17151449"},{"evidenceCode":"ECO:0000314","source":"PubMed","id":"3042752"}]},{"database":"GO","id":"GO:0034355","properties":[{"key":"GoTerm","value":"P:NAD+ biosynthetic process via the salvage pathway"},{"key":"GoEvidenceType","value":"EXP:EcoCyc"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24506841"}]},{"database":"GO","id":"GO:0015949","properties":[{"key":"GoTerm","value":"P:nucleobase-containing small molecule interconversion"},{"key":"GoEvidenceType","value":"IMP:EcoliWiki"}],"evidences":[{"evidenceCode":"ECO:0000315","source":"PubMed","id":"7559336"}]},{"database":"GO","id":"GO:0055086","properties":[{"key":"GoTerm","value":"P:nucleobase-containing small molecule metabolic process"},{"key":"GoEvidenceType","value":"IMP:EcoliWiki"}],"evidences":[{"evidenceCode":"ECO:0000315","source":"PubMed","id":"7559336"}]},{"database":"GO","id":"GO:0034214","properties":[{"key":"GoTerm","value":"P:protein hexamerization"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"15808857"}]},{"database":"GO","id":"GO:0006152","properties":[{"key":"GoTerm","value":"P:purine nucleoside catabolic process"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"10400599"},{"evidenceCode":"ECO:0000314","source":"PubMed","id":"15808857"},{"evidenceCode":"ECO:0000314","source":"PubMed","id":"17151449"},{"evidenceCode":"ECO:0000314","source":"PubMed","id":"3042752"}]},{"database":"GO","id":"GO:1903228","properties":[{"key":"GoTerm","value":"P:xanthosine catabolic process"},{"key":"GoEvidenceType","value":"IMP:EcoCyc"}],"evidences":[{"evidenceCode":"ECO:0000315","source":"PubMed","id":"7559336"}]},{"database":"CDD","id":"cd09009","properties":[{"key":"EntryName","value":"PNP-EcPNPII_like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.1580:FF:000011","properties":[{"key":"EntryName","value":"Purine nucleoside phosphorylase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1580","properties":[{"key":"EntryName","value":"Nucleoside phosphorylase domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000845","properties":[{"key":"EntryName","value":"Nucleoside_phosphorylase_d"}]},{"database":"InterPro","id":"IPR035994","properties":[{"key":"EntryName","value":"Nucleoside_phosphorylase_sf"}]},{"database":"InterPro","id":"IPR011268","properties":[{"key":"EntryName","value":"Purine_phosphorylase"}]},{"database":"InterPro","id":"IPR018099","properties":[{"key":"EntryName","value":"Purine_phosphorylase-2_CS"}]},{"database":"InterPro","id":"IPR010943","properties":[{"key":"EntryName","value":"Xanthosine_phosphorylase"}]},{"database":"NCBIfam","id":"TIGR01697","properties":[{"key":"EntryName","value":"PNPH-PUNA-XAPA"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF006054","properties":[{"key":"EntryName","value":"PRK08202.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01699","properties":[{"key":"EntryName","value":"XAPA"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11904","properties":[{"key":"EntryName","value":"METHYLTHIOADENOSINE/PURINE NUCLEOSIDE PHOSPHORYLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11904:SF9","properties":[{"key":"EntryName","value":"PURINE NUCLEOSIDE PHOSPHORYLASE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01048","properties":[{"key":"EntryName","value":"PNP_UDP_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000477","properties":[{"key":"EntryName","value":"PurNPase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53167","properties":[{"key":"EntryName","value":"Purine and uridine phosphorylases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01240","properties":[{"key":"EntryName","value":"PNP_MTAP_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSQVQFSHNPLFCIDIIKTYKPDFTPRVAFILGSGLGALADQIENAVAISYEKLPGFPVSTVHGHAGELVLGHLQGVPVVCMKGRGHFYEGRGMTIMTDAIRTFKLLGCELLFCTNAAGSLRPEVGAGSLVALKDHINTMPGTPMVGLNDDRFGERFFSLANAYDAEYRALLQKVAKEEGFPLTEGVFVSYPGPNFETAAEIRMMQIIGGDVVGMSVVPEVISARHCDLKVVAVSAITNMAEGLSDVKLSHAQTLAAAELSKQNFINLICGFLRKIA","length":277,"molWeight":29835,"crc64":"DD26545755C08F8B","md5":"810ED5968DDC5E27D1081642822C0E04"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"ACTIVITY REGULATION":1,"BIOPHYSICOCHEMICAL PROPERTIES":1,"PATHWAY":2,"SUBUNIT":1,"INDUCTION":1,"DISRUPTION PHENOTYPE":1,"SIMILARITY":1,"SEQUENCE CAUTION":1},"countByFeatureType":{"Chain":1,"Binding site":6,"Mutagenesis":2,"Sequence conflict":3,"Helix":13,"Beta strand":12,"Turn":3},"uniParcId":"UPI0000138FCE"}}