ID   D8A4F5_ECOMS            Unreviewed;        94 AA.
AC   D8A4F5;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   13-FEB-2019, entry version 35.
DE   RecName: Full=Pyrimidine/purine nucleoside phosphorylase {ECO:0000256|HAMAP-Rule:MF_01537};
DE            EC=2.4.2.1 {ECO:0000256|HAMAP-Rule:MF_01537};
DE            EC=2.4.2.2 {ECO:0000256|HAMAP-Rule:MF_01537};
DE   AltName: Full=Adenosine phosphorylase {ECO:0000256|HAMAP-Rule:MF_01537};
DE   AltName: Full=Cytidine phosphorylase {ECO:0000256|HAMAP-Rule:MF_01537};
DE   AltName: Full=Guanosine phosphorylase {ECO:0000256|HAMAP-Rule:MF_01537};
DE            EC=2.4.2.15 {ECO:0000256|HAMAP-Rule:MF_01537};
DE   AltName: Full=Inosine phosphorylase {ECO:0000256|HAMAP-Rule:MF_01537};
DE   AltName: Full=Thymidine phosphorylase {ECO:0000256|HAMAP-Rule:MF_01537};
DE            EC=2.4.2.4 {ECO:0000256|HAMAP-Rule:MF_01537};
DE   AltName: Full=Uridine phosphorylase {ECO:0000256|HAMAP-Rule:MF_01537};
DE            EC=2.4.2.3 {ECO:0000256|HAMAP-Rule:MF_01537};
DE   AltName: Full=Xanthosine phosphorylase {ECO:0000256|HAMAP-Rule:MF_01537};
GN   Name=ppnP {ECO:0000256|HAMAP-Rule:MF_01537};
GN   ORFNames=HMPREF9530_01393 {ECO:0000313|EMBL:EFK21973.1};
OS   Escherichia coli (strain MS 21-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=749527 {ECO:0000313|EMBL:EFK21973.1, ECO:0000313|Proteomes:UP000005688};
RN   [1] {ECO:0000313|EMBL:EFK21973.1, ECO:0000313|Proteomes:UP000005688}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MS 21-1 {ECO:0000313|EMBL:EFK21973.1,
RC   ECO:0000313|Proteomes:UP000005688};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B.,
RA   Courtney L., Fronick C., Harrison M., Strong C., Farmer C.,
RA   Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C.,
RA   Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M.,
RA   Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_01537,
CC       ECO:0000256|SAAS:SAAS01088094}.
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; EC=2.4.2.1; Evidence={ECO:0000256|HAMAP-
CC         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:0000256|HAMAP-Rule:MF_01537,
CC         ECO:0000256|SAAS:SAAS01122736};
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:0000256|HAMAP-Rule:MF_01537,
CC         ECO:0000256|SAAS:SAAS01122750};
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:0000256|HAMAP-Rule:MF_01537,
CC         ECO:0000256|SAAS:SAAS01122744};
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:0000256|HAMAP-Rule:MF_01537,
CC         ECO:0000256|SAAS:SAAS01122753};
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:0000256|HAMAP-Rule:MF_01537,
CC         ECO:0000256|SAAS:SAAS01122742};
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:0000256|HAMAP-Rule:MF_01537,
CC         ECO:0000256|SAAS:SAAS01122737};
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:0000256|HAMAP-Rule:MF_01537,
CC         ECO:0000256|SAAS:SAAS01122739};
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:0000256|HAMAP-Rule:MF_01537,
CC         ECO:0000256|SAAS:SAAS01122747};
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:0000256|HAMAP-Rule:MF_01537,
CC         ECO:0000256|SAAS:SAAS01122751};
CC   -!- SIMILARITY: Belongs to the nucleoside phosphorylase PpnP family.
CC       {ECO:0000256|HAMAP-Rule:MF_01537, ECO:0000256|SAAS:SAAS01088098}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EFK21973.1}.
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DR   EMBL; ADTR01000128; EFK21973.1; -; Genomic_DNA.
DR   RefSeq; WP_000941942.1; NZ_GG772658.1.
DR   ProteinModelPortal; D8A4F5; -.
DR   SMR; D8A4F5; -.
DR   EnsemblBacteria; EFK21973; EFK21973; HMPREF9530_01393.
DR   BioCyc; GCF_000164355-HMP:HMPREF9530_RS18990-MONOMER; -.
DR   Proteomes; UP000005688; Unassembled WGS sequence.
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;
KW   Complete proteome {ECO:0000313|Proteomes:UP000005688};
KW   Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_01537,
KW   ECO:0000256|SAAS:SAAS01088087};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01537,
KW   ECO:0000256|SAAS:SAAS01088085}.
SQ   SEQUENCE   94 AA;  10234 MW;  D7EF5C0AFD86D661 CRC64;
     MLQSNEYFSG KVKSIGFSSS STGRASVGVM VEGEYTFSTA EPEEMTVISG ALNVLLPDAT
     DWQVYEAGSV FNVPGHSEFH LQVAEPTSYL CRYL
//