PNPH_KORCO
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 03-AUG-2022, entry version 67.
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; Candidatus 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 OMA; MTQCPEA; -.
DR OrthoDB; 63298at2157; -.
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; -; 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; PTHR42679; 1.
DR Pfam; PF01048; PNP_UDP_1; 1.
DR SUPFAM; SSF53167; SSF53167; 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