ID   PUNA_MYCTO              Reviewed;         268 AA.
AC   P9WP00; L0TDR7; O53359; P0A538;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 38.
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=MT3406;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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; AE000516; AAK47749.1; -; Genomic_DNA.
DR   PIR; B70842; B70842.
DR   RefSeq; WP_003417233.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WP00; -.
DR   SMR; P9WP00; -.
DR   EnsemblBacteria; AAK47749; AAK47749; MT3406.
DR   GeneID; 45427302; -.
DR   KEGG; mtc:MT3406; -.
DR   PATRIC; fig|83331.31.peg.3665; -.
DR   HOGENOM; CLU_054456_1_1_11; -.
DR   UniPathway; UPA00606; -.
DR   Proteomes; UP000001020; 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; Transferase.
FT   CHAIN           1..268
FT                   /note="Purine nucleoside phosphorylase"
FT                   /id="PRO_0000427038"
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;  27572 MW;  12AA429779CE89F6 CRC64;
     MADPRPDPDE LARRAAQVIA DRTGIGEHDV AVVLGSGWLP AVAALGSPTT VLPQAELPGF
     VPPTAAGHAG ELLSVPIGAH RVLVLAGRIH AYEGHDLRYV VHPVRAARAA GAQIMVLTNA
     AGGLRADLQV GQPVLISDHL NLTARSPLVG GEFVDLTDAY SPRLRELARQ SDPQLAEGVY
     AGLPGPHYET PAEIRMLQTL GADLVGMSTV HETIAARAAG AEVLGVSLVT NLAAGITGEP
     LSHAEVLAAG AASATRMGAL LADVIARF