(data stored in ACNUC7421 zone)

SWISSPROT: PPNP_ECO57

ID   PPNP_ECO57              Reviewed;          94 AA.
AC   P0C039; P36768; P77343;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   05-JUL-2017, entry version 67.
DE   RecName: Full=Pyrimidine/purine nucleoside phosphorylase {ECO:0000255|HAMAP-Rule:MF_01537};
DE            EC=2.4.2.2 {ECO:0000255|HAMAP-Rule:MF_01537};
DE   AltName: Full=Adenosine phosphorylase {ECO:0000255|HAMAP-Rule:MF_01537};
DE   AltName: Full=Cytidine phosphorylase {ECO:0000255|HAMAP-Rule:MF_01537};
DE   AltName: Full=Guanosine phosphorylase {ECO:0000255|HAMAP-Rule:MF_01537};
DE            EC=2.4.2.15 {ECO:0000255|HAMAP-Rule:MF_01537};
DE   AltName: Full=Inosine phosphorylase {ECO:0000255|HAMAP-Rule:MF_01537};
DE   AltName: Full=Thymidine phosphorylase {ECO:0000255|HAMAP-Rule:MF_01537};
DE            EC=2.4.2.4 {ECO:0000255|HAMAP-Rule:MF_01537};
DE   AltName: Full=Uridine phosphorylase {ECO:0000255|HAMAP-Rule:MF_01537};
DE            EC=2.4.2.3 {ECO:0000255|HAMAP-Rule:MF_01537};
DE   AltName: Full=Xanthosine phosphorylase {ECO:0000255|HAMAP-Rule:MF_01537};
GN   Name=ppnP {ECO:0000255|HAMAP-Rule:MF_01537};
GN   OrderedLocusNames=Z0487, ECs0441;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Catalyzes the phosphorolysis of diverse nucleosides,
CC       yielding D-ribose 1-phosphate and the respective free bases. Can
CC       use uridine, adenosine, guanosine, cytidine, thymidine, inosine
CC       and xanthosine as substrates. Also catalyzes the reverse
CC       reactions. {ECO:0000255|HAMAP-Rule:MF_01537}.
CC   -!- CATALYTIC ACTIVITY: Purine nucleoside + phosphate = purine +
CC       alpha-D-ribose 1-phosphate. {ECO:0000255|HAMAP-Rule:MF_01537}.
CC   -!- CATALYTIC ACTIVITY: Adenosine + phosphate = adenine + alpha-D-
CC       ribose 1-phosphate. {ECO:0000255|HAMAP-Rule:MF_01537}.
CC   -!- CATALYTIC ACTIVITY: Cytidine + phosphate = cytosine + alpha-D-
CC       ribose 1-phosphate. {ECO:0000255|HAMAP-Rule:MF_01537}.
CC   -!- CATALYTIC ACTIVITY: Guanosine + phosphate = guanine + alpha-D-
CC       ribose 1-phosphate. {ECO:0000255|HAMAP-Rule:MF_01537}.
CC   -!- CATALYTIC ACTIVITY: Inosine + phosphate = hypoxanthine + alpha-D-
CC       ribose 1-phosphate. {ECO:0000255|HAMAP-Rule:MF_01537}.
CC   -!- CATALYTIC ACTIVITY: Thymidine + phosphate = thymine + 2-deoxy-
CC       alpha-D-ribose 1-phosphate. {ECO:0000255|HAMAP-Rule:MF_01537}.
CC   -!- CATALYTIC ACTIVITY: Uridine + phosphate = uracil + alpha-D-ribose
CC       1-phosphate. {ECO:0000255|HAMAP-Rule:MF_01537}.
CC   -!- CATALYTIC ACTIVITY: Xanthosine + phosphate = xanthine + alpha-D-
CC       ribose 1-phosphate. {ECO:0000255|HAMAP-Rule:MF_01537}.
CC   -!- SIMILARITY: Belongs to the nucleoside phosphorylase PpnP family.
CC       {ECO:0000255|HAMAP-Rule:MF_01537}.
DR   EMBL; AE005174; AAG54737.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33864.1; -; Genomic_DNA.
DR   PIR; A90684; A90684.
DR   PIR; E85534; E85534.
DR   RefSeq; NP_308468.1; NC_002695.1.
DR   RefSeq; WP_000941942.1; NZ_MWVM01000009.1.
DR   ProteinModelPortal; P0C039; -.
DR   SMR; P0C039; -.
DR   STRING; 155864.Z0487; -.
DR   EnsemblBacteria; AAG54737; AAG54737; Z0487.
DR   EnsemblBacteria; BAB33864; BAB33864; BAB33864.
DR   GeneID; 914543; -.
DR   KEGG; ece:Z0487; -.
DR   KEGG; ecs:ECs0441; -.
DR   PATRIC; fig|386585.9.peg.537; -.
DR   eggNOG; ENOG4105NBK; Bacteria.
DR   eggNOG; COG3123; LUCA.
DR   HOGENOM; HOG000218057; -.
DR   KO; K09913; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0047975; F:guanosine phosphorylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016154; F:pyrimidine-nucleoside phosphorylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009032; F:thymidine phosphorylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004850; F:uridine phosphorylase activity; IEA:UniProtKB-EC.
DR   Gene3D; 2.60.120.10; -; 1.
DR   HAMAP; MF_01537; Nucleos_phosphorylase_PpnP; 1.
DR   InterPro; IPR009664; Ppnp.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin.
DR   Pfam; PF06865; DUF1255; 1.
DR   SUPFAM; SSF51182; SSF51182; 1.
PE   3: Inferred from homology;
DR   PRODOM; P0C039.
DR   SWISS-2DPAGE; P0C039.
KW   Complete proteome; Glycosyltransferase; Transferase.
FT   CHAIN         1     94       Pyrimidine/purine nucleoside
FT                                phosphorylase.
FT                                /FTId=PRO_0000211765.
SQ   SEQUENCE   94 AA;  10234 MW;  D7EF5C0AFD86D661 CRC64;
     MLQSNEYFSG KVKSIGFSSS STGRASVGVM VEGEYTFSTA EPEEMTVISG ALNVLLPDAT
     DWQVYEAGSV FNVPGHSEFH LQVAEPTSYL CRYL
//

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