PNPH_THEKO
ID PNPH_THEKO Reviewed; 267 AA.
AC Q5JJB8;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=TK1482;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
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; AP006878; BAD85671.1; -; Genomic_DNA.
DR RefSeq; WP_011250433.1; NC_006624.1.
DR AlphaFoldDB; Q5JJB8; -.
DR SMR; Q5JJB8; -.
DR IntAct; Q5JJB8; 1.
DR MINT; Q5JJB8; -.
DR STRING; 69014.TK1482; -.
DR PRIDE; Q5JJB8; -.
DR EnsemblBacteria; BAD85671; BAD85671; TK1482.
DR GeneID; 3234499; -.
DR KEGG; tko:TK1482; -.
DR PATRIC; fig|69014.16.peg.1443; -.
DR eggNOG; arCOG01327; Archaea.
DR HOGENOM; CLU_054456_0_2_2; -.
DR InParanoid; Q5JJB8; -.
DR OMA; MTQCPEA; -.
DR OrthoDB; 63298at2157; -.
DR PhylomeDB; Q5JJB8; -.
DR BioCyc; MetaCyc:MON-19658; -.
DR UniPathway; UPA00606; -.
DR Proteomes; UP000000536; 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..267
FT /note="Probable 6-oxopurine nucleoside phosphorylase"
FT /id="PRO_0000415087"
FT BINDING 10
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 188
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT BINDING 189
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT BINDING 212..214
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT SITE 170
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT SITE 224
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
SQ SEQUENCE 267 AA; 29804 MW; 2E1BA87711CB899B CRC64;
MPRIAIIGGS GVYDPALLTN IREETVETPY GTVKVKIGEY NGEEIVFLAR HGEGHSVPPH
KINYRANIWA LYELGVERIL STSAVGSLNL DMKPGDFVIL DQLMDFTKTR HYTFYDGEES
PHDRKFVAHV DFTEPYCPEL RKALMNAARE LGFTYHPMGT YACMEGPRFE TRAEIRALKI
LGADVVGMTQ CPEAALAREL EMCYASVAIV TNYAAGISPN KLTHTEVVEL MAQKSNEIKL
LLMKAIEYIP KERRCPCKDA LKGATGE
