PUNA_BACSU
ID PUNA_BACSU Reviewed; 271 AA.
AC P46354;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Purine nucleoside phosphorylase 1;
DE Short=PNP 1;
DE EC=2.4.2.1;
DE AltName: Full=Inosine phosphorylase;
DE AltName: Full=Inosine-guanosine phosphorylase;
DE AltName: Full=Purine nucleoside phosphorylase I;
DE Short=PNP I;
DE Short=Pu-NPase I;
GN Name=punA; Synonyms=deoD, pnp, yqkO; OrderedLocusNames=BSU23490;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / BR151;
RX PubMed=10537218; DOI=10.1099/00221287-145-10-2957;
RA Schuch R., Garibian A., Saxild H.H., Piggot P.J., Nygaard P.;
RT "Nucleosides as a carbon source in Bacillus subtilis: characterization of
RT the drm-pupG operon.";
RL Microbiology 145:2957-2966(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / JH642;
RX PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA Kobayashi Y.;
RT "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT Bacillus subtilis genome containing the skin element and many sporulation
RT genes.";
RL Microbiology 142:3103-3111(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 161-271.
RC STRAIN=168 / MB24;
RX PubMed=1629150; DOI=10.1128/jb.174.15.4885-4892.1992;
RA Wu J.-J., Schuch R., Piggot P.J.;
RT "Characterization of a Bacillus subtilis sporulation operon that includes
RT genes for an RNA polymerase sigma factor and for a putative DD-
RT carboxypeptidase.";
RL J. Bacteriol. 174:4885-4892(1992).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=168;
RX PubMed=17218307; DOI=10.1074/mcp.m600464-mcp200;
RA Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R.,
RA Mann M.;
RT "The serine/threonine/tyrosine phosphoproteome of the model bacterium
RT Bacillus subtilis.";
RL Mol. Cell. Proteomics 6:697-707(2007).
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; U32685; AAA74434.1; -; Genomic_DNA.
DR EMBL; D84432; BAA12651.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14281.1; -; Genomic_DNA.
DR EMBL; M85047; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; D69680; D69680.
DR RefSeq; NP_390230.1; NC_000964.3.
DR RefSeq; WP_003230447.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P46354; -.
DR SMR; P46354; -.
DR STRING; 224308.BSU23490; -.
DR iPTMnet; P46354; -.
DR jPOST; P46354; -.
DR PaxDb; P46354; -.
DR PRIDE; P46354; -.
DR EnsemblBacteria; CAB14281; CAB14281; BSU_23490.
DR GeneID; 938731; -.
DR KEGG; bsu:BSU23490; -.
DR PATRIC; fig|224308.179.peg.2559; -.
DR eggNOG; COG0005; Bacteria.
DR InParanoid; P46354; -.
DR OMA; EGVYAQF; -.
DR PhylomeDB; P46354; -.
DR BioCyc; BSUB:BSU23490-MON; -.
DR BRENDA; 2.4.2.1; 658.
DR UniPathway; UPA00606; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004731; F:purine-nucleoside phosphorylase activity; IBA:GO_Central.
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; IPR011270; Pur_Nuc_Pase_Ino/Guo-sp.
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; TIGR01700; PNPH; 1.
DR TIGRFAMs; TIGR01697; PNPH-PUNA-XAPA; 1.
DR PROSITE; PS01240; PNP_MTAP_2; 1.
PE 1: Evidence at protein level;
KW Glycosyltransferase; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..271
FT /note="Purine nucleoside phosphorylase 1"
FT /id="PRO_0000184540"
FT BINDING 28
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250|UniProtKB:P9WP01"
FT BINDING 59
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250|UniProtKB:P45563"
FT BINDING 79..81
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250|UniProtKB:P45563"
FT BINDING 111
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250|UniProtKB:P45563"
FT BINDING 191
FT /ligand="a purine D-ribonucleoside"
FT /ligand_id="ChEBI:CHEBI:142355"
FT /evidence="ECO:0000250|UniProtKB:P45563"
FT BINDING 210
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250|UniProtKB:P45563"
FT BINDING 233
FT /ligand="a purine D-ribonucleoside"
FT /ligand_id="ChEBI:CHEBI:142355"
FT /evidence="ECO:0000250|UniProtKB:P45563"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17218307"
FT CONFLICT 184
FT /note="A -> D (in Ref. 4; M85047)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="G -> A (in Ref. 4; M85047)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 271 AA; 29127 MW; 420B26E7309D9FC9 CRC64;
MKDRIERAAA FIKQNLPESP KIGLILGSGL GILADEIENP VKLKYEDIPE FPVSTVEGHA
GQLVLGTLEG VSVIAMQGRF HFYEGYSMEK VTFPVRVMKA LGVEALIVTN AAGGVNTEFR
AGDLMIITDH INFMGTNPLI GPNEADFGAR FPDMSSAYDK DLSSLAEKIA KDLNIPIQKG
VYTAVTGPSY ETPAEVRFLR TMGSDAVGMS TVPEVIVANH AGMRVLGISC ISNAAAGILD
QPLSHDEVME VTEKVKAGFL KLVKAIVAQY E
