ID   PNPH_YEAST              Reviewed;         311 AA.
AC   Q05788; D6VYL0;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 184.
DE   RecName: Full=Purine nucleoside phosphorylase;
DE            Short=PNP;
DE            EC=2.4.2.1;
DE   AltName: Full=Inosine phosphorylase;
DE   AltName: Full=Inosine-guanosine phosphorylase;
GN   Name=PNP1; OrderedLocusNames=YLR209C; ORFNames=L8167.19;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA   Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA   Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA   Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA   Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA   Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA   Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA   Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA   Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA   Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA   Zollner A., Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(1997).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [4]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC   -!- FUNCTION: The purine nucleoside phosphorylases catalyze the
CC       phosphorolytic breakdown of the N-glycosidic bond in the beta-
CC       (deoxy)ribonucleoside molecules, with the formation of the
CC       corresponding free purine bases and pentose-1-phosphate. Cleaves
CC       guanosine and inosine (By similarity). {ECO:0000250}.
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   -!- PATHWAY: Purine metabolism; purine nucleoside salvage.
CC   -!- MISCELLANEOUS: Present with 1630 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the PNP/MTAP phosphorylase family.
CC       {ECO:0000305}.
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DR   EMBL; U14913; AAB67440.1; -; Genomic_DNA.
DR   EMBL; AY557950; AAS56276.1; -; Genomic_DNA.
DR   EMBL; BK006945; DAA09526.1; -; Genomic_DNA.
DR   PIR; S48560; S48560.
DR   RefSeq; NP_013310.1; NM_001182096.1.
DR   AlphaFoldDB; Q05788; -.
DR   SMR; Q05788; -.
DR   BioGRID; 31477; 126.
DR   DIP; DIP-4300N; -.
DR   IntAct; Q05788; 2.
DR   STRING; 4932.YLR209C; -.
DR   iPTMnet; Q05788; -.
DR   MaxQB; Q05788; -.
DR   PaxDb; 4932-YLR209C; -.
DR   PeptideAtlas; Q05788; -.
DR   EnsemblFungi; YLR209C_mRNA; YLR209C; YLR209C.
DR   GeneID; 850906; -.
DR   KEGG; sce:YLR209C; -.
DR   AGR; SGD:S000004199; -.
DR   SGD; S000004199; PNP1.
DR   VEuPathDB; FungiDB:YLR209C; -.
DR   eggNOG; KOG3984; Eukaryota.
DR   GeneTree; ENSGT00950000182991; -.
DR   HOGENOM; CLU_054456_1_2_1; -.
DR   InParanoid; Q05788; -.
DR   OMA; EGVYAQF; -.
DR   OrthoDB; 5475828at2759; -.
DR   BioCyc; YEAST:YLR209C-MONOMER; -.
DR   BRENDA; 2.4.2.1; 984.
DR   Reactome; R-SCE-6798695; Neutrophil degranulation.
DR   Reactome; R-SCE-74217; Purine salvage.
DR   Reactome; R-SCE-74259; Purine catabolism.
DR   Reactome; R-SCE-9755088; Ribavirin ADME.
DR   UniPathway; UPA00606; -.
DR   BioGRID-ORCS; 850906; 0 hits in 10 CRISPR screens.
DR   ChiTaRS; PNP1; yeast.
DR   PRO; PR:Q05788; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; Q05788; Protein.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0047724; F:inosine nucleosidase activity; IDA:SGD.
DR   GO; GO:0070635; F:nicotinamide riboside hydrolase activity; IDA:SGD.
DR   GO; GO:0004731; F:purine-nucleoside phosphorylase activity; IDA:SGD.
DR   GO; GO:0046115; P:guanosine catabolic process; IMP:SGD.
DR   GO; GO:0006148; P:inosine catabolic process; IMP:SGD.
DR   GO; GO:0034356; P:NAD biosynthesis via nicotinamide riboside salvage pathway; IGI:SGD.
DR   GO; GO:0019358; P:nicotinate nucleotide salvage; IGI:SGD.
DR   CDD; cd09009; PNP-EcPNPII_like; 1.
DR   Gene3D; 3.40.50.1580; Nucleoside phosphorylase domain; 1.
DR   InterPro; IPR000845; Nucleoside_phosphorylase_d.
DR   InterPro; IPR035994; Nucleoside_phosphorylase_sf.
DR   InterPro; IPR011268; Purine_phosphorylase.
DR   InterPro; IPR018099; Purine_phosphorylase-2_CS.
DR   NCBIfam; TIGR01697; PNPH-PUNA-XAPA; 1.
DR   PANTHER; PTHR11904; METHYLTHIOADENOSINE/PURINE NUCLEOSIDE PHOSPHORYLASE; 1.
DR   PANTHER; PTHR11904:SF9; PURINE NUCLEOSIDE PHOSPHORYLASE-RELATED; 1.
DR   Pfam; PF01048; PNP_UDP_1; 1.
DR   PIRSF; PIRSF000477; PurNPase; 1.
DR   SUPFAM; SSF53167; Purine and uridine phosphorylases; 1.
DR   PROSITE; PS01240; PNP_MTAP_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Glycosyltransferase; Phosphoprotein; Reference proteome;
KW   Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CHAIN           2..311
FT                   /note="Purine nucleoside phosphorylase"
FT                   /id="PRO_0000184538"
FT   BINDING         46
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000250|UniProtKB:P55859"
FT   BINDING         81
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000250|UniProtKB:P55859"
FT   BINDING         101..103
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000250|UniProtKB:P55859"
FT   BINDING         134
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000250|UniProtKB:P55859"
FT   BINDING         219
FT                   /ligand="a purine D-ribonucleoside"
FT                   /ligand_id="ChEBI:CHEBI:142355"
FT                   /evidence="ECO:0000250|UniProtKB:P55859"
FT   BINDING         238
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000250|UniProtKB:P55859"
FT   BINDING         261
FT                   /ligand="a purine D-ribonucleoside"
FT                   /ligand_id="ChEBI:CHEBI:142355"
FT                   /evidence="ECO:0000250|UniProtKB:P55859"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   MOD_RES         275
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
SQ   SEQUENCE   311 AA;  33755 MW;  159DB9F9EC393BCA CRC64;
     MSDILNVSQQ REAITKAAAY ISAILEPHFK NTTNFEPPRT LIICGSGLGG ISTKLSRDNP
     PPVTVPYQDI PGFKKSTVPG HSGTLMFGSM NGSPVVLMNG RLHGYEGNTL FETTFPIRVL
     NHMGHVRNLI VTNAAGGINA KYQACDLMCI YDHLNIPGLA GQHPLRGPNL DEDGPRFLAL
     SDAYDLELRK LLFKKWKELK IQRPLHEGTY TFVSGPTFET RAESKMIRML GGDAVGMSTV
     PEVIVARHCG WRVLALSLIT NTCVVDSPAS ALDESPVPLE KGKATHAEVL ENGKIASNDV
     QNLIAAVMGE L
//