(data stored in ACNUC29543 zone)

SWISSPROT: PPNP_ACIBT

ID   PPNP_ACIBT              Reviewed;         108 AA.
AC   A3M1J3;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 2.
DT   08-MAY-2019, entry version 59.
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=A1S_0323;
OS   Acinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 /
OS   NCDC KC755 / 5377).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter;
OC   Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=400667;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377;
RX   PubMed=17344419; DOI=10.1101/gad.1510307;
RA   Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N.,
RA   Gerstein M., Snyder M.;
RT   "New insights into Acinetobacter baumannii pathogenesis revealed by
RT   high-density pyrosequencing and transposon mutagenesis.";
RL   Genes Dev. 21:601-614(2007).
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; CP000521; ABO10787.2; -; Genomic_DNA.
DR   SMR; A3M1J3; -.
DR   EnsemblBacteria; ABO10787; ABO10787; A1S_0323.
DR   KEGG; acb:A1S_0323; -.
DR   HOGENOM; HOG000218057; -.
DR   KO; K09913; -.
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; A3M1J3.
DR   SWISS-2DPAGE; A3M1J3.
KW   Glycosyltransferase; Transferase.
FT   CHAIN         1    108       Pyrimidine/purine nucleoside
FT                                phosphorylase.
FT                                /FTId=PRO_0000298686.
SQ   SEQUENCE   108 AA;  12060 MW;  1521357954B501C7 CRC64;
     MSSTQFDHVT VIKKSNVYFG GACISHTVQF EDGTKKTLGV ILPTEQPLTF ETHVPERMEI
     ISGECRVKIA DSNESELFRA GQSFYVPGNS VFKIETDEVL DYVCHLEG
//

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