(data stored in ACNUC7421 zone)

SWISSPROT: PPNP_ECODH

ID   PPNP_ECODH              Reviewed;          94 AA.
AC   B1XEY0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   05-JUL-2017, entry version 47.
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=ECDH10B_0348;
OS   Escherichia coli (strain K12 / DH10B).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=316385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / DH10B;
RX   PubMed=18245285; DOI=10.1128/JB.01695-07;
RA   Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA   Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA   Posfai G., Weinstock G.M., Blattner F.R.;
RT   "The complete genome sequence of Escherichia coli DH10B: insights into
RT   the biology of a laboratory workhorse.";
RL   J. Bacteriol. 190:2597-2606(2008).
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; CP000948; ACB01520.1; -; Genomic_DNA.
DR   RefSeq; WP_000941942.1; NC_010473.1.
DR   ProteinModelPortal; B1XEY0; -.
DR   SMR; B1XEY0; -.
DR   EnsemblBacteria; ACB01520; ACB01520; ECDH10B_0348.
DR   KEGG; ecd:ECDH10B_0348; -.
DR   eggNOG; ENOG4105NBK; Bacteria.
DR   eggNOG; COG3123; LUCA.
DR   HOGENOM; HOG000218057; -.
DR   KO; K09913; -.
DR   OMA; YHYICHF; -.
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; B1XEY0.
DR   SWISS-2DPAGE; B1XEY0.
KW   Glycosyltransferase; Transferase.
FT   CHAIN         1     94       Pyrimidine/purine nucleoside
FT                                phosphorylase.
FT                                /FTId=PRO_1000198657.
SQ   SEQUENCE   94 AA;  10234 MW;  D7EF5C0AFD86D661 CRC64;
     MLQSNEYFSG KVKSIGFSSS STGRASVGVM VEGEYTFSTA EPEEMTVISG ALNVLLPDAT
     DWQVYEAGSV FNVPGHSEFH LQVAEPTSYL CRYL
//

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