ID   PNPH_DICTD              Reviewed;         263 AA.
AC   B8E181;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 65.
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=Dtur_0928;
OS   Dictyoglomus turgidum (strain DSM 6724 / Z-1310).
OC   Bacteria; Dictyoglomi; Dictyoglomales; Dictyoglomaceae; Dictyoglomus.
OX   NCBI_TaxID=515635;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6724 / Z-1310;
RX   PubMed=28066333; DOI=10.3389/fmicb.2016.01979;
RA   Brumm P.J., Gowda K., Robb F.T., Mead D.A.;
RT   "The complete genome sequence of hyperthermophile Dictyoglomus turgidum DSM
RT   6724 reveals a specialized carbohydrate fermentor.";
RL   Front. Microbiol. 7:1979-1979(2016).
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}.
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DR   EMBL; CP001251; ACK42209.1; -; Genomic_DNA.
DR   RefSeq; WP_012583293.1; NC_011661.1.
DR   RefSeq; YP_002352823.1; NC_011661.1.
DR   AlphaFoldDB; B8E181; -.
DR   SMR; B8E181; -.
DR   STRING; 515635.Dtur_0928; -.
DR   EnsemblBacteria; ACK42209; ACK42209; Dtur_0928.
DR   KEGG; dtu:Dtur_0928; -.
DR   PATRIC; fig|515635.4.peg.965; -.
DR   eggNOG; COG0005; Bacteria.
DR   HOGENOM; CLU_054456_0_2_0; -.
DR   InParanoid; B8E181; -.
DR   OMA; MTQCPEA; -.
DR   OrthoDB; 1364220at2; -.
DR   UniPathway; UPA00606; -.
DR   Proteomes; UP000007719; 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..263
FT                   /note="Probable 6-oxopurine nucleoside phosphorylase"
FT                   /id="PRO_0000415081"
FT   BINDING         9
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT   BINDING         49..50
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT   BINDING         82..83
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT   BINDING         181
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT   BINDING         182
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT   BINDING         205..207
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT   SITE            164
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT   SITE            217
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
SQ   SEQUENCE   263 AA;  29405 MW;  64B2331F6F124FE0 CRC64;
     MRIAIIGGTG VYDPKFLENP EEIKVSTPYG EVKLLKGIYQ GEEVGFLARH GAGHTVPPHR
     INYKANMWAL KSLGVERILS TTAVGSLKLN LVPGDLVILD QFIDFTKNRD HTFYNGDDGK
     VIHIDFTNPY CPELRNILYE TSKEIGIKAH PFGTYVCTEG PRFETPAEIK MYSFFGDVVG
     MTNVPEVILA RELEICYASV SLVTNYAAGI SPNPLTHSEV LEVMTQNIEK VRKLFAAVIP
     KIPKERNCIC KNALKEYREK GLL