PNPH_STRCO
ID PNPH_STRCO Reviewed; 280 AA.
AC Q9KYV7;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Purine nucleoside phosphorylase {ECO:0000255|HAMAP-Rule:MF_01963};
DE Short=PNP {ECO:0000255|HAMAP-Rule:MF_01963};
DE EC=2.4.2.1 {ECO:0000255|HAMAP-Rule:MF_01963};
GN OrderedLocusNames=SCO3188;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
CC -!- FUNCTION: Purine nucleoside phosphorylase 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 lacks several conserved
CC amino acids in the substrate binding pocket that confer specificity
CC towards MTA. {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; AL939115; CAB90972.1; -; Genomic_DNA.
DR RefSeq; NP_627402.1; NC_003888.3.
DR RefSeq; WP_003975629.1; NZ_VNID01000013.1.
DR AlphaFoldDB; Q9KYV7; -.
DR SMR; Q9KYV7; -.
DR STRING; 100226.SCO3188; -.
DR GeneID; 1098622; -.
DR KEGG; sco:SCO3188; -.
DR PATRIC; fig|100226.15.peg.3248; -.
DR eggNOG; COG0005; Bacteria.
DR HOGENOM; CLU_054456_0_2_11; -.
DR InParanoid; Q9KYV7; -.
DR OMA; ADPFCPE; -.
DR PhylomeDB; Q9KYV7; -.
DR UniPathway; UPA00606; -.
DR Proteomes; UP000001973; 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.
DR TIGRFAMs; TIGR01694; MTAP; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase; Purine salvage; Reference proteome; Transferase.
FT CHAIN 1..280
FT /note="Purine nucleoside phosphorylase"
FT /id="PRO_0000415083"
FT BINDING 15
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT BINDING 55..56
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT BINDING 194
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT BINDING 195
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT BINDING 218..220
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT SITE 231
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
SQ SEQUENCE 280 AA; 29755 MW; CA99954C27D27D8A CRC64;
MANKVKAEIG VIGGSGFYSF LDDVTEVRVD TPYGPPSDSL FLGEVAGRRV AFLPRHGRGH
HLPPHRINYR ANLWALRSVG ARQVLGPCAV GGLRPEYGPG TLLVPDQFVD RTRSRPSTYF
DGLPMPDGTV PNVVHVSLAD PYCPTGRAAA LKAARGREWE PVDGGTLVVV EGPRFGTRAE
SLWHRAQGWS VVGMTGHPEA ALARELELCY TSLTLVTDLD AGAESGEGVS HEEVLRVFAA
NVDRLRGVLF DAVAALPASG ERDCPCGAAL GGMDPGIALP
