ID   PNPH_KORCO              Reviewed;         270 AA.
AC   B1L719;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 70.
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=Kcr_1502;
OS   Korarchaeum cryptofilum (strain OPF8).
OC   Archaea; Candidatus Korarchaeota; Korarchaeum.
OX   NCBI_TaxID=374847;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OPF8;
RX   PubMed=18535141; DOI=10.1073/pnas.0801980105;
RA   Elkins J.G., Podar M., Graham D.E., Makarova K.S., Wolf Y., Randau L.,
RA   Hedlund B.P., Brochier-Armanet C., Kunin V., Anderson I., Lapidus A.,
RA   Goltsman E., Barry K., Koonin E.V., Hugenholtz P., Kyrpides N., Wanner G.,
RA   Richardson P., Keller M., Stetter K.O.;
RT   "A korarchaeal genome reveals new insights into the evolution of the
RT   Archaea.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:8102-8107(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; CP000968; ACB08248.1; -; Genomic_DNA.
DR   RefSeq; WP_012310145.1; NC_010482.1.
DR   AlphaFoldDB; B1L719; -.
DR   SMR; B1L719; -.
DR   STRING; 374847.Kcr_1502; -.
DR   EnsemblBacteria; ACB08248; ACB08248; Kcr_1502.
DR   GeneID; 6094779; -.
DR   KEGG; kcr:Kcr_1502; -.
DR   eggNOG; arCOG01327; Archaea.
DR   HOGENOM; CLU_054456_0_2_2; -.
DR   InParanoid; B1L719; -.
DR   OrthoDB; 7681at2157; -.
DR   PhylomeDB; B1L719; -.
DR   UniPathway; UPA00606; -.
DR   Proteomes; UP000001686; 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; 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   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; Reference proteome; Transferase.
FT   CHAIN           1..270
FT                   /note="Probable 6-oxopurine nucleoside phosphorylase"
FT                   /id="PRO_0000415085"
FT   BINDING         10
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT   BINDING         48..49
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT   BINDING         191
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT   BINDING         192
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT   BINDING         215..217
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT   SITE            173
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT   SITE            228
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
SQ   SEQUENCE   270 AA;  29588 MW;  69C874638AF82A82 CRC64;
     MVRVGIIGGS GLYELLENPR IVRLDTPFGH CDVQLGELAG EEVAFIPRHG ASHRLPPYKV
     NYKANLYALN MLEVERIIAT NAVGSINPAL EPGTIVIPHD FIDMTKCRDV TFYDGETTIK
     VRGREVSGVV HVSMTPYTYC PEIRASIIEA AEHMGLGVRD GGVYVCTEGN RFETPAEIRA
     FSILGGDIVG MTGCPEASLA RELAICYASI SVVTNYAAGV SGAVKLTQGE VIEIFSRKIQ
     DISRLIEETI RRIPKRRECP CKDALSEYLK
//