ID   PNPH_AQUAE              Reviewed;         277 AA.
AC   O66839;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Probable 6-oxopurine nucleoside phosphorylase {ECO:0000255|HAMAP-Rule:MF_01963};
DE            EC=2.4.2.1 {ECO:0000255|HAMAP-Rule:MF_01963};
DE   AltName: Full=Purine nucleoside phosphorylase {ECO:0000255|HAMAP-Rule:MF_01963};
DE            Short=PNP {ECO:0000255|HAMAP-Rule:MF_01963};
GN   OrderedLocusNames=aq_568;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
CC   -!- FUNCTION: Purine nucleoside phosphorylase which is highly specific for
CC       6-oxopurine nucleosides. Cleaves guanosine or inosine to respective
CC       bases and sugar-1-phosphate molecules. Involved in purine salvage.
CC       {ECO:0000255|HAMAP-Rule:MF_01963}.
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_01963};
CC   -!- PATHWAY: Purine metabolism; purine nucleoside salvage.
CC       {ECO:0000255|HAMAP-Rule:MF_01963}.
CC   -!- SUBUNIT: Homohexamer. Dimer of a homotrimer. {ECO:0000255|HAMAP-
CC       Rule:MF_01963}.
CC   -!- MISCELLANEOUS: Although this enzyme belongs to the family of MTA
CC       phosphorylases based on sequence homology, it has been shown that
CC       conserved amino acid substitutions in the substrate binding pocket
CC       convert the substrate specificity of this enzyme from 6-aminopurines to
CC       6-oxopurines. {ECO:0000255|HAMAP-Rule:MF_01963}.
CC   -!- SIMILARITY: Belongs to the PNP/MTAP phosphorylase family. MTAP
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01963}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE000657; AAC06801.1; -; Genomic_DNA.
DR   PIR; C70351; C70351.
DR   RefSeq; NP_213399.1; NC_000918.1.
DR   RefSeq; WP_010880337.1; NC_000918.1.
DR   AlphaFoldDB; O66839; -.
DR   SMR; O66839; -.
DR   STRING; 224324.aq_568; -.
DR   EnsemblBacteria; AAC06801; AAC06801; aq_568.
DR   KEGG; aae:aq_568; -.
DR   PATRIC; fig|224324.8.peg.465; -.
DR   eggNOG; COG0005; Bacteria.
DR   HOGENOM; CLU_054456_0_2_0; -.
DR   InParanoid; O66839; -.
DR   OMA; ADPFCPE; -.
DR   OrthoDB; 1364220at2; -.
DR   UniPathway; UPA00606; -.
DR   Proteomes; UP000000798; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0017061; F:S-methyl-5-thioadenosine phosphorylase activity; IBA:GO_Central.
DR   GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IBA:GO_Central.
DR   GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-UniRule.
DR   CDD; cd09010; MTAP_SsMTAPII_like_MTIP; 1.
DR   Gene3D; 3.40.50.1580; -; 1.
DR   HAMAP; MF_01963; MTAP; 1.
DR   InterPro; IPR010044; MTAP.
DR   InterPro; IPR000845; Nucleoside_phosphorylase_d.
DR   InterPro; IPR035994; Nucleoside_phosphorylase_sf.
DR   InterPro; IPR018099; Purine_phosphorylase-2_CS.
DR   PANTHER; PTHR42679; PTHR42679; 1.
DR   Pfam; PF01048; PNP_UDP_1; 1.
DR   SUPFAM; SSF53167; SSF53167; 1.
DR   TIGRFAMs; TIGR01694; MTAP; 1.
DR   PROSITE; PS01240; PNP_MTAP_2; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase; Purine salvage; Reference proteome; Transferase.
FT   CHAIN           1..277
FT                   /note="Probable 6-oxopurine nucleoside phosphorylase"
FT                   /id="PRO_0000415080"
FT   BINDING         8
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT   BINDING         50..51
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT   BINDING         83..84
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT   BINDING         199
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT   BINDING         200
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT   BINDING         223..225
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT   SITE            181
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT   SITE            235
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
SQ   SEQUENCE   277 AA;  30812 MW;  1C90A95984B0B04E CRC64;
     MLGIIGGSGL YNLPGIKVKE EVQVKTPFGE PSSPVVIAEV EGKKVAFLAR HGRGHEYPPH
     LVPYRANLWA LREVGVKRVL GISAVGGINE LLMPGDFVVI HDYLDFTKTR RSTYYEGKFS
     VKVEGEDKVA KLLREGKVVH VDMSEAYCPE MRKVLIQILK EKNFRFHPKG VYACTEGPRF
     ETPSEIKMLK LLGADVVGMT GYPEVALARE LTMCYASLCV VANPAAGIAG YRLTSNEVIQ
     LMKRKEEEIK EVVLKFIKEL PEIRSCDCEK SLEGAEV