(data stored in ACNUC7421 zone)

SWISSPROT: PPNP_ECO27

ID   PPNP_ECO27              Reviewed;          94 AA.
AC   B7UJL5;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 46.
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=E2348C_0327;
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC;
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
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:
CC       Reaction=a purine D-ribonucleoside + phosphate = a purine
CC         nucleobase + alpha-D-ribose 1-phosphate; Xref=Rhea:RHEA:19805,
CC         ChEBI:CHEBI:26386, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720,
CC         ChEBI:CHEBI:142355; Evidence={ECO:0000255|HAMAP-Rule:MF_01537};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine + phosphate = adenine + alpha-D-ribose 1-
CC         phosphate; Xref=Rhea:RHEA:27642, ChEBI:CHEBI:16335,
CC         ChEBI:CHEBI:16708, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01537};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cytidine + phosphate = alpha-D-ribose 1-phosphate +
CC         cytosine; Xref=Rhea:RHEA:52540, ChEBI:CHEBI:16040,
CC         ChEBI:CHEBI:17562, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01537};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanosine + phosphate = alpha-D-ribose 1-phosphate +
CC         guanine; Xref=Rhea:RHEA:13233, ChEBI:CHEBI:16235,
CC         ChEBI:CHEBI:16750, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720;
CC         EC=2.4.2.15; Evidence={ECO:0000255|HAMAP-Rule:MF_01537};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=inosine + phosphate = alpha-D-ribose 1-phosphate +
CC         hypoxanthine; Xref=Rhea:RHEA:27646, ChEBI:CHEBI:17368,
CC         ChEBI:CHEBI:17596, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01537};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=phosphate + thymidine = 2-deoxy-alpha-D-ribose 1-
CC         phosphate + thymine; Xref=Rhea:RHEA:16037, ChEBI:CHEBI:17748,
CC         ChEBI:CHEBI:17821, ChEBI:CHEBI:43474, ChEBI:CHEBI:57259;
CC         EC=2.4.2.2; Evidence={ECO:0000255|HAMAP-Rule:MF_01537};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=phosphate + thymidine = 2-deoxy-alpha-D-ribose 1-
CC         phosphate + thymine; Xref=Rhea:RHEA:16037, ChEBI:CHEBI:17748,
CC         ChEBI:CHEBI:17821, ChEBI:CHEBI:43474, ChEBI:CHEBI:57259;
CC         EC=2.4.2.4; Evidence={ECO:0000255|HAMAP-Rule:MF_01537};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=phosphate + uridine = alpha-D-ribose 1-phosphate +
CC         uracil; Xref=Rhea:RHEA:24388, ChEBI:CHEBI:16704,
CC         ChEBI:CHEBI:17568, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720;
CC         EC=2.4.2.2; Evidence={ECO:0000255|HAMAP-Rule:MF_01537};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=phosphate + uridine = alpha-D-ribose 1-phosphate +
CC         uracil; Xref=Rhea:RHEA:24388, ChEBI:CHEBI:16704,
CC         ChEBI:CHEBI:17568, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720;
CC         EC=2.4.2.3; Evidence={ECO:0000255|HAMAP-Rule:MF_01537};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=phosphate + xanthosine = alpha-D-ribose 1-phosphate +
CC         xanthine; Xref=Rhea:RHEA:27638, ChEBI:CHEBI:17712,
CC         ChEBI:CHEBI:18107, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01537};
CC   -!- SIMILARITY: Belongs to the nucleoside phosphorylase PpnP family.
CC       {ECO:0000255|HAMAP-Rule:MF_01537}.
DR   EMBL; FM180568; CAS07875.1; -; Genomic_DNA.
DR   RefSeq; WP_000941942.1; NC_011601.1.
DR   SMR; B7UJL5; -.
DR   EnsemblBacteria; CAS07875; CAS07875; E2348C_0327.
DR   KEGG; ecg:E2348C_0327; -.
DR   KO; K09913; -.
DR   OMA; YHYICHF; -.
DR   BioCyc; ECOL574521:E2348C_RS01725-MONOMER; -.
DR   Proteomes; UP000008205; Chromosome.
DR   GO; GO:0047975; F:guanosine phosphorylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004731; F:purine-nucleoside phosphorylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016154; F:pyrimidine-nucleoside phosphorylase activity; IEA:UniProtKB-UniRule.
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_sf.
DR   PANTHER; PTHR36540; PTHR36540; 1.
DR   Pfam; PF06865; Ppnp; 1.
DR   SUPFAM; SSF51182; SSF51182; 1.
PE   3: Inferred from homology;
DR   PRODOM; B7UJL5.
DR   SWISS-2DPAGE; B7UJL5.
KW   Complete proteome; Glycosyltransferase; Transferase.
FT   CHAIN         1     94       Pyrimidine/purine nucleoside
FT                                phosphorylase.
FT                                /FTId=PRO_1000185193.
SQ   SEQUENCE   94 AA;  10234 MW;  D7EF5C0AFD86D661 CRC64;
     MLQSNEYFSG KVKSIGFSSS STGRASVGVM VEGEYTFSTA EPEEMTVISG ALNVLLPDAT
     DWQVYEAGSV FNVPGHSEFH LQVAEPTSYL CRYL
//

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