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PPNP_HYDCU
ID   PPNP_HYDCU              Reviewed;         104 AA.
AC   Q31FE7;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Pyrimidine/purine nucleoside phosphorylase {ECO:0000255|HAMAP-Rule:MF_01537};
DE            EC=2.4.2.1 {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   AltName: Full=Inosine phosphorylase {ECO:0000255|HAMAP-Rule:MF_01537};
DE   AltName: Full=Thymidine phosphorylase {ECO:0000255|HAMAP-Rule:MF_01537};
DE   AltName: Full=Uridine phosphorylase {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}; OrderedLocusNames=Tcr_1534;
OS   Hydrogenovibrio crunogenus (strain DSM 25203 / XCL-2) (Thiomicrospira
OS   crunogena).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Piscirickettsiaceae; Hydrogenovibrio.
OX   NCBI_TaxID=317025;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25203 / XCL-2;
RX   PubMed=17105352; DOI=10.1371/journal.pbio.0040383;
RA   Scott K.M., Sievert S.M., Abril F.N., Ball L.A., Barrett C.J., Blake R.A.,
RA   Boller A.J., Chain P.S.G., Clark J.A., Davis C.R., Detter C., Do K.F.,
RA   Dobrinski K.P., Faza B.I., Fitzpatrick K.A., Freyermuth S.K., Harmer T.L.,
RA   Hauser L.J., Huegler M., Kerfeld C.A., Klotz M.G., Kong W.W., Land M.,
RA   Lapidus A., Larimer F.W., Longo D.L., Lucas S., Malfatti S.A., Massey S.E.,
RA   Martin D.D., McCuddin Z., Meyer F., Moore J.L., Ocampo L.H. Jr., Paul J.H.,
RA   Paulsen I.T., Reep D.K., Ren Q., Ross R.L., Sato P.Y., Thomas P.,
RA   Tinkham L.E., Zeruth G.T.;
RT   "The genome of deep-sea vent chemolithoautotroph Thiomicrospira crunogena
RT   XCL-2.";
RL   PLoS Biol. 4:1-17(2006).
CC   -!- FUNCTION: Catalyzes the phosphorolysis of diverse nucleosides, yielding
CC       D-ribose 1-phosphate and the respective free bases. Can use uridine,
CC       adenosine, guanosine, cytidine, thymidine, inosine and xanthosine as
CC       substrates. Also catalyzes the reverse reactions. {ECO:0000255|HAMAP-
CC       Rule:MF_01537}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a purine D-ribonucleoside + phosphate = a purine nucleobase +
CC         alpha-D-ribose 1-phosphate; Xref=Rhea:RHEA:19805, ChEBI:CHEBI:26386,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57720, ChEBI:CHEBI:142355; EC=2.4.2.1;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01537};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine + phosphate = adenine + alpha-D-ribose 1-phosphate;
CC         Xref=Rhea:RHEA:27642, ChEBI:CHEBI:16335, ChEBI:CHEBI:16708,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; EC=2.4.2.1;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01537};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cytidine + phosphate = alpha-D-ribose 1-phosphate + cytosine;
CC         Xref=Rhea:RHEA:52540, ChEBI:CHEBI:16040, ChEBI:CHEBI:17562,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; EC=2.4.2.2;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01537};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanosine + phosphate = alpha-D-ribose 1-phosphate + guanine;
CC         Xref=Rhea:RHEA:13233, ChEBI:CHEBI:16235, ChEBI:CHEBI:16750,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; EC=2.4.2.1;
CC         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; EC=2.4.2.1;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01537};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=phosphate + thymidine = 2-deoxy-alpha-D-ribose 1-phosphate +
CC         thymine; Xref=Rhea:RHEA:16037, ChEBI:CHEBI:17748, ChEBI:CHEBI:17821,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57259; EC=2.4.2.2;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01537};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=phosphate + uridine = alpha-D-ribose 1-phosphate + uracil;
CC         Xref=Rhea:RHEA:24388, ChEBI:CHEBI:16704, ChEBI:CHEBI:17568,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; EC=2.4.2.2;
CC         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, ChEBI:CHEBI:18107,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; EC=2.4.2.1;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01537};
CC   -!- SIMILARITY: Belongs to the nucleoside phosphorylase PpnP family.
CC       {ECO:0000255|HAMAP-Rule:MF_01537}.
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DR   EMBL; CP000109; ABB42126.1; -; Genomic_DNA.
DR   RefSeq; WP_011370955.1; NC_007520.2.
DR   AlphaFoldDB; Q31FE7; -.
DR   SMR; Q31FE7; -.
DR   STRING; 317025.Tcr_1534; -.
DR   EnsemblBacteria; ABB42126; ABB42126; Tcr_1534.
DR   KEGG; tcx:Tcr_1534; -.
DR   eggNOG; COG3123; Bacteria.
DR   HOGENOM; CLU_157874_1_0_6; -.
DR   OMA; YHYICHF; -.
DR   OrthoDB; 1937865at2; -.
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   Glycosyltransferase; Transferase.
FT   CHAIN           1..104
FT                   /note="Pyrimidine/purine nucleoside phosphorylase"
FT                   /id="PRO_0000298733"
SQ   SEQUENCE   104 AA;  11243 MW;  90534CB20D51375D CRC64;
     MSQFENVTVV KAANVYYDGK VSSRTVLFAD GSKKTLGLLL PGEYEFGTEA AEIMEMLAGD
     VDVLLPGETK WQSLSAGESF NVPANSKFGI NVKTVADYCC SYID
 
 
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