PUNA_MYCTU
ID PUNA_MYCTU Reviewed; 268 AA.
AC P9WP01; 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 52.
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=Rv3307; ORFNames=MTV016.06;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH 9-DEAZAHYPOXANTHINE
RP AND PHOSPHATE.
RX PubMed=11444966; DOI=10.1021/bi010585p;
RA Shi W., Basso L.A., Santos D.S., Tyler P.C., Furneaux R.H., Blanchard J.S.,
RA Almo S.C., Schramm V.L.;
RT "Structures of purine nucleoside phosphorylase from Mycobacterium
RT tuberculosis in complexes with immucillin-H and its pieces.";
RL Biochemistry 40:8204-8215(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; AL123456; CCP46126.1; -; Genomic_DNA.
DR PIR; B70842; B70842.
DR RefSeq; NP_217824.1; NC_000962.3.
DR RefSeq; WP_003417233.1; NZ_NVQJ01000003.1.
DR PDB; 1G2O; X-ray; 1.75 A; A/B/C=1-268.
DR PDB; 1I80; X-ray; 2.00 A; A/B/C=1-268.
DR PDB; 1N3I; X-ray; 1.90 A; A/B/C=1-268.
DR PDB; 3IOM; X-ray; 2.14 A; A/B=1-268.
DR PDB; 3SCZ; X-ray; 1.95 A; A/B=1-268.
DR PDBsum; 1G2O; -.
DR PDBsum; 1I80; -.
DR PDBsum; 1N3I; -.
DR PDBsum; 3IOM; -.
DR PDBsum; 3SCZ; -.
DR AlphaFoldDB; P9WP01; -.
DR SMR; P9WP01; -.
DR STRING; 83332.Rv3307; -.
DR BindingDB; P9WP01; -.
DR ChEMBL; CHEMBL1169594; -.
DR DrugBank; DB03551; (3R,4R)-3-Hydroxy-4-(hydroxymethyl)-1-[(4-oxo-4,4a,5,7a-tetrahydro-3H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]pyrrolidinium.
DR DrugBank; DB03411; 2-Hydroxymethyl-Pyrrolidine-3,4-Diol.
DR DrugBank; DB04095; 9-Deazahypoxanthine.
DR DrugCentral; P9WP01; -.
DR PaxDb; P9WP01; -.
DR DNASU; 887542; -.
DR GeneID; 45427302; -.
DR GeneID; 887542; -.
DR KEGG; mtu:Rv3307; -.
DR TubercuList; Rv3307; -.
DR eggNOG; COG0005; Bacteria.
DR OMA; EGVYAQF; -.
DR PhylomeDB; P9WP01; -.
DR UniPathway; UPA00606; -.
DR PRO; PR:P9WP01; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004731; F:purine-nucleoside phosphorylase activity; IDA:MTBBASE.
DR GO; GO:0006161; P:deoxyguanosine catabolic process; IDA:MTBBASE.
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 1: Evidence at protein level;
KW 3D-structure; Glycosyltransferase; Reference proteome; Transferase.
FT CHAIN 1..268
FT /note="Purine nucleoside phosphorylase"
FT /id="PRO_0000184544"
FT BINDING 36
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000269|PubMed:11444966,
FT ECO:0007744|PDB:1G2O, ECO:0007744|PDB:1I80"
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:0000269|PubMed:11444966,
FT ECO:0007744|PDB:1G2O, ECO:0007744|PDB:1I80"
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:0000269|PubMed:11444966"
FT BINDING 208
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000269|PubMed:11444966,
FT ECO:0007744|PDB:1G2O, ECO:0007744|PDB:1I80"
FT BINDING 231
FT /ligand="a purine D-ribonucleoside"
FT /ligand_id="ChEBI:CHEBI:142355"
FT /evidence="ECO:0000269|PubMed:11444966"
FT HELIX 8..23
FT /evidence="ECO:0007829|PDB:1G2O"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:1G2O"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:1G2O"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:1G2O"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:1G2O"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:1G2O"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:3SCZ"
FT STRAND 71..77
FT /evidence="ECO:0007829|PDB:1G2O"
FT STRAND 80..86
FT /evidence="ECO:0007829|PDB:1G2O"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:1G2O"
FT HELIX 97..100
FT /evidence="ECO:0007829|PDB:1G2O"
FT HELIX 102..109
FT /evidence="ECO:0007829|PDB:1G2O"
FT STRAND 114..123
FT /evidence="ECO:0007829|PDB:1G2O"
FT STRAND 133..141
FT /evidence="ECO:0007829|PDB:1G2O"
FT HELIX 162..171
FT /evidence="ECO:0007829|PDB:1G2O"
FT STRAND 176..182
FT /evidence="ECO:0007829|PDB:1G2O"
FT HELIX 191..200
FT /evidence="ECO:0007829|PDB:1G2O"
FT STRAND 203..209
FT /evidence="ECO:0007829|PDB:1G2O"
FT HELIX 210..218
FT /evidence="ECO:0007829|PDB:1G2O"
FT STRAND 222..232
FT /evidence="ECO:0007829|PDB:1G2O"
FT TURN 234..236
FT /evidence="ECO:0007829|PDB:3SCZ"
FT HELIX 243..251
FT /evidence="ECO:0007829|PDB:1G2O"
FT HELIX 254..267
FT /evidence="ECO:0007829|PDB:1G2O"
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
