ID   PUNA_MYCLE              Reviewed;         268 AA.
AC   P46862;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Purine nucleoside phosphorylase;
DE            Short=PNP;
DE            Short=Pu-NPase;
DE            EC=2.4.2.1;
DE   AltName: Full=Inosine phosphorylase;
DE   AltName: Full=Inosine-guanosine phosphorylase;
GN   Name=punA; Synonyms=deoD; OrderedLocusNames=ML0707; ORFNames=L308_F2_56;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Smith D.R., Robison K.;
RL   Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
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, inosine, 2'-deoxyguanosine and 2'-deoxyinosine.
CC       {ECO:0000250|UniProtKB:P77834}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a purine 2'-deoxy-D-ribonucleoside + phosphate = 2-deoxy-
CC         alpha-D-ribose 1-phosphate + a purine nucleobase;
CC         Xref=Rhea:RHEA:36431, ChEBI:CHEBI:26386, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57259, ChEBI:CHEBI:142361; EC=2.4.2.1;
CC         Evidence={ECO:0000250|UniProtKB:P77834};
CC   -!- PATHWAY: Purine metabolism; purine nucleoside salvage.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:P77834}.
CC   -!- SIMILARITY: Belongs to the PNP/MTAP phosphorylase family.
CC       {ECO:0000305}.
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DR   EMBL; U00022; AAA17341.1; -; Genomic_DNA.
DR   EMBL; AL583919; CAC30216.1; -; Genomic_DNA.
DR   PIR; S73042; S73042.
DR   RefSeq; NP_301562.1; NC_002677.1.
DR   RefSeq; WP_010907886.1; NC_002677.1.
DR   AlphaFoldDB; P46862; -.
DR   SMR; P46862; -.
DR   STRING; 272631.ML0707; -.
DR   EnsemblBacteria; CAC30216; CAC30216; CAC30216.
DR   KEGG; mle:ML0707; -.
DR   PATRIC; fig|272631.5.peg.1272; -.
DR   Leproma; ML0707; -.
DR   eggNOG; COG0005; Bacteria.
DR   HOGENOM; CLU_054456_1_1_11; -.
DR   OMA; EGVYAQF; -.
DR   UniPathway; UPA00606; -.
DR   Proteomes; UP000000806; Chromosome.
DR   GO; GO:0004731; F:purine-nucleoside phosphorylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro.
DR   CDD; cd09009; PNP-EcPNPII_like; 1.
DR   Gene3D; 3.40.50.1580; -; 1.
DR   InterPro; IPR000845; Nucleoside_phosphorylase_d.
DR   InterPro; IPR035994; Nucleoside_phosphorylase_sf.
DR   InterPro; IPR011269; PUNP.
DR   InterPro; IPR011268; Purine_phosphorylase.
DR   InterPro; IPR018099; Purine_phosphorylase-2_CS.
DR   PANTHER; PTHR11904; PTHR11904; 1.
DR   Pfam; PF01048; PNP_UDP_1; 1.
DR   PIRSF; PIRSF000477; PurNPase; 1.
DR   SUPFAM; SSF53167; SSF53167; 1.
DR   TIGRFAMs; TIGR01697; PNPH-PUNA-XAPA; 1.
DR   TIGRFAMs; TIGR01698; PUNP; 1.
DR   PROSITE; PS01240; PNP_MTAP_2; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..268
FT                   /note="Purine nucleoside phosphorylase"
FT                   /id="PRO_0000184543"
FT   BINDING         36
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000250|UniProtKB:P9WP01"
FT   BINDING         68
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000250|UniProtKB:P45563"
FT   BINDING         88..90
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000250|UniProtKB:P45563"
FT   BINDING         120
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000250|UniProtKB:P45563"
FT   BINDING         189
FT                   /ligand="a purine D-ribonucleoside"
FT                   /ligand_id="ChEBI:CHEBI:142355"
FT                   /evidence="ECO:0000250|UniProtKB:P45563"
FT   BINDING         208
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000250|UniProtKB:P45563"
FT   BINDING         231
FT                   /ligand="a purine D-ribonucleoside"
FT                   /ligand_id="ChEBI:CHEBI:142355"
FT                   /evidence="ECO:0000250|UniProtKB:P45563"
SQ   SEQUENCE   268 AA;  27980 MW;  46C622532FC96A0F CRC64;
     MTYTLLDPDE LARRAAQVIG ERTGILKHDV AVVLGSGWSS AVAALGSSRA VFPQAELPGF
     ITPNAAGHTG ELLSVRIGAH RVLVLAGRIH PYEGHDLRHV VHPVRTACAA GARIIVLTNA
     AGGLRADMAV GQLVLISDHL NLTTRSPLVG THFVDLTNAY TTRLRKLASD TDPTLTEGVY
     AAQPGPHYET PAEIRMLRML GADLVGMSTV HETIAARAAG AEVLGVSLVT NLAAGITGKP
     LNHAEVLAAG TASANRIGSL LADIIARF