ID   PNPH_MOOTA              Reviewed;         260 AA.
AC   Q2RKL6;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 86.
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=Moth_0705;
OS   Moorella thermoacetica (strain ATCC 39073 / JCM 9320).
OC   Bacteria; Bacillota; Clostridia; Moorellales; Moorellaceae; Moorella.
OX   NCBI_TaxID=264732;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39073 / JCM 9320;
RX   PubMed=18631365; DOI=10.1111/j.1462-2920.2008.01679.x;
RA   Pierce E., Xie G., Barabote R.D., Saunders E., Han C.S., Detter J.C.,
RA   Richardson P., Brettin T.S., Das A., Ljungdahl L.G., Ragsdale S.W.;
RT   "The complete genome sequence of Moorella thermoacetica (f. Clostridium
RT   thermoaceticum).";
RL   Environ. Microbiol. 10:2550-2573(2008).
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; CP000232; ABC19023.1; -; Genomic_DNA.
DR   RefSeq; YP_429566.1; NC_007644.1.
DR   AlphaFoldDB; Q2RKL6; -.
DR   SMR; Q2RKL6; -.
DR   STRING; 264732.Moth_0705; -.
DR   EnsemblBacteria; ABC19023; ABC19023; Moth_0705.
DR   KEGG; mta:Moth_0705; -.
DR   PATRIC; fig|264732.11.peg.754; -.
DR   eggNOG; COG0005; Bacteria.
DR   HOGENOM; CLU_054456_0_2_9; -.
DR   OrthoDB; 1523230at2; -.
DR   UniPathway; UPA00606; -.
DR   GO; GO:0017061; F:S-methyl-5-thioadenosine phosphorylase activity; IEA:InterPro.
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; Nucleoside phosphorylase domain; 1.
DR   HAMAP; MF_01963; MTAP; 1.
DR   InterPro; IPR010044; MTAP.
DR   InterPro; IPR000845; Nucleoside_phosphorylase_d.
DR   InterPro; IPR035994; Nucleoside_phosphorylase_sf.
DR   NCBIfam; TIGR01694; MTAP; 1.
DR   PANTHER; PTHR42679; S-METHYL-5'-THIOADENOSINE PHOSPHORYLASE; 1.
DR   PANTHER; PTHR42679:SF2; S-METHYL-5'-THIOADENOSINE PHOSPHORYLASE; 1.
DR   Pfam; PF01048; PNP_UDP_1; 1.
DR   SUPFAM; SSF53167; Purine and uridine phosphorylases; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase; Purine salvage; Transferase.
FT   CHAIN           1..260
FT                   /note="Probable 6-oxopurine nucleoside phosphorylase"
FT                   /id="PRO_0000415082"
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         182
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT   BINDING         183
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT   BINDING         206..208
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            218
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
SQ   SEQUENCE   260 AA;  28319 MW;  336D6524DA87688F CRC64;
     MRIAIIGGSG VYDPGILTNI HEERVETPYG AAVLKVGTYH GEEIGFMPRH GDKHTVPPHK
     VNYRANIWAL KMLKVERVLA TAAVGSTNPE FRPGDFVIVN DFLDFTKTRT YTFFEGGETG
     VVHTDFTTPY CPELGQVLVE TAARLGIKAH AGGVYACTEG PRFETPAEIR MIRQLGGDLV
     GMTNVPEVVL AHEVGLCYGL IAMVTNMAAG ISSTPLSHEE VLEIMDQNGK NLRDLIMQAI
     PGIPRQRNCR CSLAAGKIEV
//