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PPNP2_PSYCK
ID   PPNP2_PSYCK             Reviewed;          94 AA.
AC   Q1QCI5;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Pyrimidine/purine nucleoside phosphorylase 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_01537};
DE   AltName: Full=Cytidine phosphorylase 2 {ECO:0000255|HAMAP-Rule:MF_01537};
DE   AltName: Full=Guanosine phosphorylase 2 {ECO:0000255|HAMAP-Rule:MF_01537};
DE   AltName: Full=Inosine phosphorylase 2 {ECO:0000255|HAMAP-Rule:MF_01537};
DE   AltName: Full=Thymidine phosphorylase 2 {ECO:0000255|HAMAP-Rule:MF_01537};
DE   AltName: Full=Uridine phosphorylase 2 {ECO:0000255|HAMAP-Rule:MF_01537};
DE   AltName: Full=Xanthosine phosphorylase 2 {ECO:0000255|HAMAP-Rule:MF_01537};
GN   Name=ppnP2 {ECO:0000255|HAMAP-Rule:MF_01537}; OrderedLocusNames=Pcryo_0835;
OS   Psychrobacter cryohalolentis (strain ATCC BAA-1226 / DSM 17306 / VKM B-2378
OS   / K5).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Psychrobacter.
OX   NCBI_TaxID=335284;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1226 / DSM 17306 / VKM B-2378 / K5;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Sims D.R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Richardson P.;
RT   "Complete sequence of chromosome of Psychrobacter cryohalolentis K5.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000323; ABE74618.1; -; Genomic_DNA.
DR   RefSeq; WP_011513181.1; NC_007969.1.
DR   AlphaFoldDB; Q1QCI5; -.
DR   SMR; Q1QCI5; -.
DR   STRING; 335284.Pcryo_0835; -.
DR   KEGG; pcr:Pcryo_0835; -.
DR   eggNOG; COG3123; Bacteria.
DR   HOGENOM; CLU_157874_0_0_6; -.
DR   OMA; YHYICHF; -.
DR   Proteomes; UP000002425; 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;
KW   Glycosyltransferase; Transferase.
FT   CHAIN           1..94
FT                   /note="Pyrimidine/purine nucleoside phosphorylase 2"
FT                   /id="PRO_0000298717"
SQ   SEQUENCE   94 AA;  10451 MW;  ED7DA451B9E919AB CRC64;
     MPSVNNYFEN KVTSIAFQTA TKPATVGVME IGEYEFGTSE FETMSVVSGA LTVKLPESDE
     WQTFNAGEQF TIEANQKFQV KVEVESAYLC TYGK
 
 
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